From owner-7tms_r@net.bio.net Tue Dec 03 22:00:00 1996 Path: biosci!ihnp4.ucsd.edu!swrinde!howland.erols.net!news-peer.gsl.net!news.gsl.net!news-dc.gsl.net!news.gsl.net!news.NetVision.net.il!news From: Martin Sanders Newsgroups: bionet.molbio.proteins.7tms_r,bionet.molbio.proteins.fluorescent,bionet.molecules.peptides Subject: Optimize protein HPLC by monitoring conductivity and pH Date: 4 Dec 1996 18:29:23 GMT Organization: NetVision LTD. Lines: 14 Message-ID: <584fu3$o9v@news.NetVision.net.il> NNTP-Posting-Host: ts002p12.pop2a.netvision.net.il Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 1.2N (Windows; I; 16bit) Xref: biosci bionet.molbio.proteins.7tms_r:945 bionet.molbio.proteins.fluorescent:854 bionet.molecules.peptides:547 You can improve the separation of proteins and other biopolymers in HPLC systems for ion exchange, hydroxylapatite, and hydrophobic interaction by monitoring the conductivity of the eluent stream using an inexpensive flow through conductivity monitor. Proteins normally elute at the same conductivity for each run and monitoring conductivity of each run can therefore provide evidence that chromatographic conditions have been reproduced while giving an accurate picture of the salt gradient for each run. Can also be used to monitor HPLC column regeneration and monitor desalting of proteins by gel filtration. Monitoring of eluent pH is also discussed. For further details contact Lazar Research Labs. Inc. by emailing service@lazarlab.com or faxing 1-213-931-1434 or viewing the Lazar web site at http://www.lazarlab.com From owner-7tms_r@net.bio.net Wed Dec 04 22:00:00 1996 Path: biosci!ihnp4.ucsd.edu!swrinde!howland.erols.net!news.sprintlink.net!news-peer.sprintlink.net!uunet!in2.uu.net!151.99.250.2!server-b.cs.interbusiness.it!usenet From: celli@cmns.mnegri.it (Nicola Celli) Newsgroups: bionet.molbio.proteins.7tms_r Subject: NB4 expression library Date: 5 Dec 1996 11:47:05 GMT Organization: Consorzio Mario Negri Sud Lines: 19 Sender: -Not-Authenticated-[8336] Message-ID: <586cnp$dt1@server-b.cs.interbusiness.it> NNTP-Posting-Host: 195.120.213.76 X-Posted-From: InterNews 1.0.5@envir01.cmns.mnegri.it Xdisclaimer: No attempt was made to authenticate the sender's name. Hi. We are working with NB4 cells (promyelocytic leukemia) and looking for a new gene. Now we would like to screen a NB4 expression library with antibodies obtained in our laboratory. It's obvious that should be easier (and faster !) for us to use a premade library than to make it up by ourself. Does anybody possess this library or knows if is commercially available ? Thank you very much for your attention. Ciao. Nicola Celli "G. Paone" Enviromental Healt Center" Consorzio Mario Negri Sud 66030 S. Maria Imbaro (CH) ITALY e-mail: celli@cmns.mnegri.it From owner-7tms_r@net.bio.net Sun Dec 08 22:00:00 1996 Path: biosci!agate!howland.erols.net!newsserver.jvnc.net!netnews.sbphrd.com!Steven_mcclue-1 From: Steven_mcclue-1@sbphrd.com (Steve McClue) Newsgroups: bionet.molbio.proteins.7tms_r Subject: Re: GPCR "Co-Receptors" Date: Mon, 09 Dec 1996 13:12:50 +0000 Organization: SB Pharmaceuticals Lines: 18 Message-ID: References: NNTP-Posting-Host: ham992.ha.uk.sbphrd.com Mime-Version: 1.0 Content-Type: text/plain; charset=ISO-8859-1 Content-Transfer-Encoding: 8bit X-Newsreader: Yet Another NewsWatcher 2.2.0b13 In article , forte@ohsu.edu (Michael Forte) wrote: > Hi Folks, > > Recently, I posted a query here about any info concerning proteins, > particulary transmembrane proteins, which are required for the function of > GPCR. Mike, This is probably an addition to your pile of 'useless responses', but there's now some evidence for 7TM receptor dimerization, whereby the dimer has a high affinity for an agonist, and the monomer a low affinity. In one sense therefore, these GPCRs are acting as co-receptors. Steve From owner-7tms_r@net.bio.net Mon Dec 09 22:00:00 1996 Path: biosci!bcm.tmc.edu!news.msfc.nasa.gov!www.nntp.primenet.com!nntp.primenet.com!howland.erols.net!newsserver.jvnc.net!netnews.sbphrd.com!Steven_mcclue-1 From: Steven_mcclue-1@sbphrd.com (Steve McClue) Newsgroups: bionet.molbio.proteins.7tms_r Subject: Receptor Dimerization (was GPCR "Co-Receptors") Date: Tue, 10 Dec 1996 08:53:56 +0000 Organization: SB Pharmaceuticals Lines: 12 Message-ID: NNTP-Posting-Host: ham992.ha.uk.sbphrd.com Mime-Version: 1.0 Content-Type: text/plain; charset=ISO-8859-1 Content-Transfer-Encoding: 8bit X-Newsreader: Yet Another NewsWatcher 2.2.0b13 A number of people have mailed me to ask about references on receptor dimerization, so I'm posting them here. Try these two: Dopamine D2 receptor dimers and receptor-blocking peptides: Ng et. al. BBRC 227:200-204 (1996) A peptide derived from a B2-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation: Herbert et. al. J. Biol. Chem: 271:16384 - 16392 (1996) Steve From owner-7tms_r@net.bio.net Mon Dec 09 22:00:00 1996 Path: biosci!rutgers!uwm.edu!www.nntp.primenet.com!nntp.primenet.com!newsxfer2.itd.umich.edu!news.itd.umich.edu!usenet From: Rick Neubig Newsgroups: bionet.molbio.proteins.7tms_r Subject: Re: Receptor Dimerization (was GPCR "Co-Receptors") Date: Tue, 10 Dec 1996 05:52:55 -0500 Organization: University of Michigan Lines: 43 Message-ID: <32AD4107.3320@umich.edu> References: Reply-To: RNeubig@umich.edu NNTP-Posting-Host: host-201.subnet-40.med.umich.edu Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 4.0a1 (Win95; I) X-Priority: Normal Steve McClue wrote: > > A number of people have mailed me to ask about references on receptor > dimerization, so I'm posting them here. > Try these two: > > Dopamine D2 receptor dimers and receptor-blocking peptides: Ng et. al. > BBRC 227:200-204 (1996) > > A peptide derived from a B2-adrenergic receptor transmembrane domain > inhibits both receptor dimerization and activation: Herbert et. al. J. > Biol. Chem: 271:16384 - 16392 (1996) > > Steve There is a significant amount of older literature on GPCR dimers but two other recent papers provide evidence of receptor dimerization based on the ability of different non-functional mutants to produce a functional protein when co-expressed. The best explanation is the heterodimerization of the two mutants one providing the "front half" (e.g. TM I-V)and the other providing the "back half" (e.g. TM VI-VII) of the receptor. This raises the question of whether the dimerization of wild type receptors is just due to a "kissing" contact or whether they actually exchange TM domains. Coexpression studies with mutant muscarinic/adrenergic receptors provide evidence for intermolecular "cross-talk" between G-protein-linked receptors. Maggio-R; Vogel-Z; Wess-J Proc-Natl-Acad-Sci-U-S-A. 1993 Apr 1; 90(7): 3103-7 Monnot, C., Bihoreau, C., Conchon, S., Curnow, K.M., Corvol, P., and Clauser, E. Polar residues in the transmembrane domains of the type I angiotensin II receptor are required for binding and coupling. Reconstitution of the binding site by co-expression of two deficient mutants. The Journal of Biological Chemistry 271(3):1507-1513, 1996. _________________________________________________________ Rick Neubig RNeubig@umich.edu Department of Pharmacology University of Michigan Phone (313) 763-3650 FAX (313) 763-4450 http://www-personal.umich.edu/~rneubig/ From owner-7tms_r@net.bio.net Mon Dec 09 22:00:00 1996 Path: biosci!FERRE.SACLAY.CEA.FR!Nicolas From: Nicolas@FERRE.SACLAY.CEA.FR (Nicolas Ancellin) Newsgroups: bionet.molbio.proteins.7tms_r Subject: orpheans GPCR Date: 10 Dec 1996 07:02:09 -0800 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 19 Sender: daemon@net.bio.net Distribution: world Message-ID: NNTP-Posting-Host: net.bio.net Hello Is somebody have any idea about the precise number of orphans proteins coupled receptor already sequenced and also if a data base concerning these guys could obtained? Nicolas ANCELLIN D=E9partement Biologie Cellulaire et Mol=E9culaire Service de Biologie Cellulaire Bat 520 p2 CEN SACLAY F91191 GIF SUR YVETTE CEDEX FRANCE nicolas@ferre.saclay.cea.fr ancellin@dsvidf.cea.fr Tel ((33)-1) 69 08 36 27 fax ((33)-1) 69 08 35 70 =20 From owner-7tms_r@net.bio.net Mon Dec 09 22:00:00 1996 Path: biosci!daresbury!nntp-trd.UNINETT.no!nntp.uio.no!news.apfel.de!nntp.zit.th-darmstadt.de!fu-berlin.de!news-ber1.dfn.de!news-lei1.dfn.de!news-nue1.dfn.de!uni-erlangen.de!winx03!wpxx02!not-for-mail From: krasel@wpxx02.toxi.uni-wuerzburg.de (Cornelius Krasel) Newsgroups: bionet.molbio.proteins.7tms_r Subject: Re: Receptor Dimerization (was GPCR "Co-Receptors") Date: 10 Dec 1996 20:46:38 GMT Organization: University of Wuerzburg, Germany Lines: 30 Message-ID: <58ki7e$37c@winx03.informatik.uni-wuerzburg.de> References: <32AD4107.3320@umich.edu> NNTP-Posting-Host: wpxx02.toxi.uni-wuerzburg.de X-Newsreader: TIN [UNIX 1.3 950824BETA PL0] Rick Neubig (RNeubig@umich.edu) wrote: > Steve McClue wrote: > > A number of people have mailed me to ask about references on receptor > > dimerization, so I'm posting them here. > > > > Dopamine D2 receptor dimers and receptor-blocking peptides: Ng et. al. > > BBRC 227:200-204 (1996) > > > > A peptide derived from a B2-adrenergic receptor transmembrane domain > > inhibits both receptor dimerization and activation: Herbert et. al. J. > > Biol. Chem: 271:16384 - 16392 (1996) > > There is a significant amount of older literature on GPCR dimers but two > other recent papers provide evidence of receptor dimerization based on > the ability of different non-functional mutants to produce a functional > protein when co-expressed. The best explanation is the > heterodimerization of the two mutants one providing the > "front half" (e.g. TM I-V)and the other providing the "back half" > (e.g. TM VI-VII) of the receptor. However, in the electron density maps of two-dimensional rhodopsin crystal sheets there is no visible evidence for dimerization. Is it likely that some GPCRs might dimerize why others do not? --Cornelius. -- /* Cornelius Krasel, U Wuerzburg, Dept. of Pharmacology, Versbacher Str. 9 */ /* D-97078 Wuerzburg, Germany email: phak004@rzbox.uni-wuerzburg.de SP3 */ /* "Science is the game we play with God to find out what His rules are." */ From owner-7tms_r@net.bio.net Tue Dec 10 22:00:00 1996 Path: biosci!VIOLET.INCM.U-NANCY.FR!poda From: poda@VIOLET.INCM.U-NANCY.FR (Gennady PODA) Newsgroups: bionet.molbio.proteins.7tms_r Subject: Receptor Dimerization question Date: 11 Dec 1996 02:04:28 -0800 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 34 Sender: daemon@net.bio.net Distribution: world Message-ID: NNTP-Posting-Host: net.bio.net Dear netters, I just want to add that bR which is not GPCR but 7TM protein was found to be a trimer in crystal. See for the ref.: N.Grigorieff, T.A.Ceska, K.H.Downing, J.M.Baldwin, R.Henderson. Electron-crystallographic refinement of the structure of bacteriorhodopsin. J. Mol. Biol. (1996) 259, 393-421. Gennady >However, in the electron density maps of two-dimensional rhodopsin crystal >sheets there is no visible evidence for dimerization. Is it likely that >some GPCRs might dimerize why others do not? > >--Cornelius. > >-- >/* Cornelius Krasel, U Wuerzburg, Dept. of Pharmacology, Versbacher Str. 9 */ >/* D-97078 Wuerzburg, Germany email: phak004@rzbox.uni-wuerzburg.de SP3 */ >/* "Science is the game we play with God to find out what His rules are." */ ************************************************************ Dr. Gennady PODA Laboratoire de Chimie theorique (UA 510 du C.N.R.S.) Universite Henri Poincare, Nancy-I Faculte des Sciences - Domaine scientifique Victor Grignard B.P. 239 - 54506 Vandoeuvre-les-Nancy Cedex France Fax : + 33 (0)3.83.91.25.30 E-mail : poda@incm.u-nancy.fr ************************************************************ From owner-7tms_r@net.bio.net Tue Dec 10 22:00:00 1996 Path: biosci!NEWSSUN.MED.MIAMI.EDU!vslepak From: vslepak@NEWSSUN.MED.MIAMI.EDU ("Vladlen Z. Slepak") Newsgroups: bionet.molbio.proteins.7tms_r Subject: 7tmr helpers Date: 11 Dec 1996 08:13:13 -0800 Organization: University of Miami Medical School Lines: 6 Sender: daemon@net.bio.net Distribution: world Message-ID: <32AE9709.24A8@newssun.med.miami.edu> Reply-To: vslepak@newssun.med.miami.edu NNTP-Posting-Host: net.bio.net Regarding the discussion of 7TMR "helper proteins" - note a PNAS paper by Ian Dickerson group (University of Miami) who found a small cytosolic protein that helps coupling of certain 7TMRs to G proteins in oocytes. Vlad From owner-7tms_r@net.bio.net Wed Dec 11 22:00:00 1996 Path: biosci!internet!biosci!not-for-mail From: biohelp (BIOSCI Administrator) Newsgroups: bionet.molbio.proteins.7tms_r Subject: BIOSCI/bionet miniFAQ & Fundraiser Date: 12 Dec 1996 02:01:15 -0800 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 239 Sender: daemon@net.bio.net Distribution: world Message-ID: <199612121000.CAA25319@net.bio.net> NNTP-Posting-Host: net.bio.net (LAST REVISION: 30-JUL-95) This BIOSCI "miniFAQ" is designed to answer the questions that come up the *most frequently*. The main BIOSCI FAQ (Frequently Asked Questions) is accessible on the World Wide Web at URL http://www.bio.net/. If you can not find an answer to your question in this or other documentation, the BIOSCI technical support staff answers e-mail queries sent to biosci-help@net.bio.net We can only answer questions about the use of the newsgroups and mailing lists. We unfortunately do not have the staff to do Internet information searches or answer scientific questions. Please post those to the appropriate BIOSCI/bionet newsgroups. Contents: -------- 0) BIOSCI NEEDS YOUR SUPPORT!! 1) Using the WWW to access the BIOSCI/bionet newsgroups. 2) What to do about "spams," i.e., junk mail, ads, etc. 3) Examples of subscribing and unsubscribing to the mailing lists. 4) The BIOSCI user address and research interest directory. 0) BIOSCI NEEDS YOUR SUPPORT!! ------------------------------ BIOSCI's government funding has been expended, and we are now operating solely from advertising revenue that we have raised from our Web site at http://www.bio.net/. We need just a few minutes of your time to help us serve you. You can do two important things which will take very little time for you individually and will immensely help us continue to help you. First, please use our WWW system at http://www.bio.net/ to access the archives. You can post or reply to messages via your Web browser as described in item #1 below. Your usage helps attract sponsors. If you contact any of our sponsors, please be sure to thank them for supporting BIOSCI. It is critical for them to get this feedback if they are to continue their sponsorship for the long term. Second, if you work for a company or organization that provides products or services of interest to the biology community, please pass this message on to your marketing or marketing communications department or other appropriate group. Please ask them to help support BIOSCI by sponsoring our Web site and explain the uses and benefits of the system to the biology community. If they are interested, they can then contact us for further information at our tech support address, biosci-help@net.bio.net. 1) Using the WWW to access the BIOSCI/bionet newsgroups. -------------------------------------------------------- As of 10 December 1995, all BIOSCI/bionet full newsgroups are accessible through the World Wide Web (WWW) at URL http://www.bio.net. One can read and reply publicly or privately to both recent postings and archived messages through one's Web browser if it is configured properly to send e-mail. Each newsgroup is equipped with its own WAIS index. The main BIOSCI home page also has access to the BIO-JOURNALS Table of Contents database WAIS index and the BIOSCI user address database described in another item further below. 2) What to do about "spams," i.e., junk mail, ads, etc. ------------------------------------------------------- BIOSCI is a set of parallel USENET newsgroups (the "bionet" groups), mailing lists, and a hypermail archive at URL http://www.bio.net/. The same postings are distributed on all media (except for a small number of mailing-list-only groups at net.bio.net). Unfortunately it is becoming a despicable practice on the Internet (by a few people out to make a fast buck) to do automated mass postings to thousands of newsgroups and mailing lists. These attempts to grab free advertising are refered to as "spams" in the usual, somewhat boneheaded, net terminology. USENET is more susceptible to this practice, and many spams originate on the USENET groups and then are passed on to the mailing lists. However, spammers also get lists of mailing addresses and hit these too, so neither medium is immune. What should you do personally if you get junk mail? --------------------------------------------------- Just delete it and move on without reading it further. Filing a protest is becoming increasingly useless because spammers are often disguising the addresses where the messages are sent from. Unless you really understand Internet mail systems, your attempt at protest by sending replies to the message will often end up being sent to the address of an innocent person that the spammer is victimizing. What can BIOSCI/bionet do to protect its newsgroups? ---------------------------------------------------- The only solution currently available is to moderate the newsgroup. If this newsgroup is already moderated, then you are in good shape. Moderation protects the USENET distribution from about 95% of the spams that are being sent to date and protects the mailing lists completely. Moderation means, however, that someone has to take the time to review each message before it goes out. We have set up software here that simply allows the moderator to forward to an address at net.bio.net messages that (s)he wishes to have distributed. This takes no more time than that needed to read the message and pass it on, say about 1 min. per message. Most newsgroups currently have a discussion leader who is responsible for their newsgroup. The discussions leaders and their e-mail addresses are listed in the BIOSCI Information Sheet which is available on the Web at http://www.bio.net/. If a newsgroup is being hit with too many junk postings, please contact the discussion leader for that group and see if there is interest in moderating the group. Please do not assume that by simply posting a complaint to the newsgroup itself, anyone on the BIOSCI staff will act on your complaint. 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For those of you with local USENET news systems, the Web interface will also give you faster access to new newsgroups and recent postings. 3) Examples of subscribing and unsubscribing to the mailing lists. ------------------------------------------------------------------ PLEASE NOTE: The BIOSCI management does NOT act on subscription/unsubscription requests that are posted improperly to the newsgroups and mailing lists. People who do this only bother everyone on the lists to no avail. Please be sure to follow the proper procedures below. Gory details are in the BIOSCI Information sheets on the Web at http://www.bio.net. 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You can fill out the address form directly through our Web page at URL http://www.bio.net/adrform.html. The address database is reindexed nightly for WWW access (the URL is http://www.bio.net/). If you are not directly on the Internet but can reach it by e-mail, please use our waismail server to access the user directory. waismail use is described above. You can also request a user address form by e-mail from biosci-help@net.bio.net. Please check your database entry from time-to-time to see if your address information is still up-to-date. Because of our limited personnel resources, we ask that you resubmit a *complete* form to revise your entry; we only replace complete entries and do not have resources to edit old forms. Sincerely, Dave Kristofferson BIOSCI/bionet Manager biosci-help@net.bio.net From owner-7tms_r@net.bio.net Wed Dec 11 22:00:00 1996 Path: biosci!BIOCELL.IRMKANT.RM.CNR.IT!7tm From: 7tm@BIOCELL.IRMKANT.RM.CNR.IT ("\\A") Newsgroups: bionet.molbio.proteins.7tms_r Subject: orphan receptor list Date: 12 Dec 1996 05:42:13 -0800 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 18 Sender: daemon@net.bio.net Distribution: world Message-ID: NNTP-Posting-Host: net.bio.net Nicolas Ancellin wrote: "Is somebody have any idea about the precise number of orphans proteins coupled receptor already sequenced and also if a data base concerning these guys could obtained?" - a list of orphan receptors can be obtained from the following server: http://expasy.hcuge.ch/cgi-bin/lists?7tmrlist.txt ----------------------------- Dr. Maria Stella Lombardi C.N.R. Institute of Cell Biology Viale Marx, 43 - 00137 ROME Italy E-mail: maria@biocell.irmkant.rm.cnr.it ------- From owner-7tms_r@net.bio.net Mon Dec 16 22:00:00 1996 Path: biosci!BIOCSERVER.BIOC.CWRU.EDU!roth From: roth@BIOCSERVER.BIOC.CWRU.EDU Newsgroups: bionet.molbio.proteins.7tms_r Subject: Re: G proteins and structures Date: 17 Dec 1996 14:58:29 -0800 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 31 Sender: daemon@net.bio.net Distribution: world Message-ID: <199612172258.WAA29392@biocserver.BIOC.CWRU.Edu> NNTP-Posting-Host: net.bio.net >Christian Reiser (christian.reiser@rzmail.uni-erlangen.de) wrote: >> does anybody know where I might find >> the structure of Gs, Gi and transducin with all subunits. > >Of Gs, only an NMR structure of the helical domain is known. Last time >I looked, the coordinates of holo-Gi and -transducin were not yet released. >However, you will probably get them if you ask Stephen Sprang (for the >Gi coordinates) or Paul Sigler (transducin) nicely. Try the latest release of Nentrez (Net-entrez) and you will find at least 4 structures of gi and 2 of transducin in various formats (including PDB format). The latest version comes with a nice 3-D viewer as well. All the above is free! Bryan Roth ============================================================= Bryan L.Roth MD, PhD Associate Professor Departments of Psychiatry, Biochemistry and Neurosciences Room W438 Case Western Reserve University Medical School 10900 Euclid Avenue Cleveland, OH 44106-4935 216-368-4544 (Fax) 216-368-2730 (Office) roth@biocserver.cwru.edu From owner-7tms_r@net.bio.net Mon Dec 16 22:00:00 1996 Path: biosci!VAX.GRC.NIA.NIH.GOV!chahrzad From: chahrzad@VAX.GRC.NIA.NIH.GOV Newsgroups: bionet.molbio.proteins.7tms_r Subject: orphan receptor Date: 17 Dec 1996 19:03:52 -0800 Organization: BIOSCI International Newsgroups for Molecular Biology Lines: 11 Sender: daemon@net.bio.net Distribution: world Message-ID: <009ACFEE.A7E464D2.6@vax.grc.nia.nih.gov> NNTP-Posting-Host: net.bio.net We have cloned a unique cDNA from adipocytes. It has 1.5Kb open reading frame and contains putative 7 transmembrane domains. It has no overall homology with other known receptor. However, looking at the orphan receptor lists on the web site posted here, I noticed that are domains common to different receptor families. I am hoping to find a program that could allow me to find regional homology with one or another G-protein linked receptor family, that I could have missed in an overall homology search ( i.e. motifs, etc...). Is there a program that can use to align this novel sequence with the known motifs? Any help is appreciated. Chahrzad Montrose Chahrzad@vax.grc.nia.nih.gov From owner-7tms_r@net.bio.net Mon Dec 16 22:00:00 1996 Path: biosci!rutgers!uwm.edu!news-peer.gsl.net!news.gsl.net!howland.erols.net!newsfeed.internetmci.com!mr.net!newshub.tc.umn.edu!fu-berlin.de!news-ber1.dfn.de!news-lei1.dfn.de!news-nue1.dfn.de!uni-erlangen.de!rznews.rrze.uni-erlangen.de!news From: Christian Reiser Newsgroups: bionet.molbio.proteins.7tms_r Subject: G proteins and structures Date: Tue, 17 Dec 1996 17:17:45 -0800 Organization: Med IV, Nephrologische Forschung Lines: 8 Message-ID: <32B74639.55BA@rzmail.uni-erlangen.de> NNTP-Posting-Host: mfm410.dialin.rrze.uni-erlangen.de Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 2.02 (Win16; I) Hi, does anybody know where I might find the structure of Gs, Gi and transducin with all subunits. Gif or jpeg files would be nice. Is there any newsgroup about G proteins? Thanks for your help. Chris From owner-7tms_r@net.bio.net Mon Dec 16 22:00:00 1996 Path: biosci!daresbury!nntp-trd.UNINETT.no!online.no!sn.no!nntp.uio.no!www.nntp.primenet.com!nntp.primenet.com!su-news-hub1.bbnplanet.com!news.bbnplanet.com!cam-news-hub1.bbnplanet.com!uunet!in1.uu.net!160.45.4.4!fu-berlin.de!news-ber1.dfn.de!news-lei1.dfn.de!news-nue1.dfn.de!uni-erlangen.de!winx03!wpxx02!not-for-mail From: krasel@wpxx02.toxi.uni-wuerzburg.de (Cornelius Krasel) Newsgroups: bionet.molbio.proteins.7tms_r Subject: Re: G proteins and structures Date: 17 Dec 1996 18:54:03 GMT Organization: University of Wuerzburg, Germany Lines: 37 Message-ID: <596q8b$b3@winx03.informatik.uni-wuerzburg.de> References: <32B74639.55BA@rzmail.uni-erlangen.de> NNTP-Posting-Host: wpxx02.toxi.uni-wuerzburg.de X-Newsreader: TIN [UNIX 1.3 950824BETA PL0] Christian Reiser (christian.reiser@rzmail.uni-erlangen.de) wrote: > does anybody know where I might find > the structure of Gs, Gi and transducin with all subunits. Of Gs, only an NMR structure of the helical domain is known. Last time I looked, the coordinates of holo-Gi and -transducin were not yet released. However, you will probably get them if you ask Stephen Sprang (for the Gi coordinates) or Paul Sigler (transducin) nicely. > Gif or jpeg files would be nice. You will still have to convert the coordinates into graphics. Some programs used to do that are - rasmol (it's free!) - molscript - the raster3d package (for raytracing of molscript output) [these are the three I make my pictures with. You need a Unix machine (I use Linux) and a bit of patience.] - a converter for povray which can make colourful structural pictures (I never tried it) - ribbons (I've never tried this either) and of course all the spiffy molecular graphics packages which only run on SGIs and cost 1000s of $$$ :-). Be aware that a *really nice picture* will need some work :-) > Is there any newsgroup about G proteins? I think this newsgroup here is just fine. --Cornelius. -- /* Cornelius Krasel, U Wuerzburg, Dept. of Pharmacology, Versbacher Str. 9 */ /* D-97078 Wuerzburg, Germany email: phak004@rzbox.uni-wuerzburg.de SP3 */ /* "Science is the game we play with God to find out what His rules are." */ From owner-7tms_r@net.bio.net Tue Dec 17 22:00:00 1996 Path: biosci!daresbury!nntp-trd.UNINETT.no!nntp.uio.no!voskovec.radio.cz!btnet-feed2!unlisys!cs.tu-berlin.de!zrz.TU-Berlin.DE!news-ber1.dfn.de!news-lei1.dfn.de!news-nue1.dfn.de!uni-erlangen.de!rznews.rrze.uni-erlangen.de!news From: Christian Reiser Newsgroups: bionet.molbio.proteins.7tms_r Subject: Re: G proteins and structures Date: Wed, 18 Dec 1996 10:39:57 -0800 Organization: Med IV, Nephrologische Forschung Lines: 18 Message-ID: <32B83A7D.1713@rzmail.uni-erlangen.de> References: <199612172258.WAA29392@biocserver.BIOC.CWRU.Edu> NNTP-Posting-Host: mfm410.dialin.rrze.uni-erlangen.de Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 2.02 (Win16; I) roth@BIOCSERVER.BIOC.CWRU.EDU wrote: > > >Christian Reiser (christian.reiser@rzmail.uni-erlangen.de) wrote: > >> does anybody know where I might find > >> the structure of Gs, Gi and transducin with all subunits. > > > > Try the latest release of Nentrez (Net-entrez) and you will find at least 4 > structures of gi and 2 of transducin in various formats (including PDB > format). The latest version comes with a nice 3-D viewer as well. > > All the above is free! > Sorry, but where can I find the latest version of Net-entrez. I tried several search-engines, but could not find anything. Thanks Chris From owner-7tms_r@net.bio.net Tue Dec 17 22:00:00 1996 Path: biosci!daresbury!nntp-trd.UNINETT.no!nntp.uio.no!www.nntp.primenet.com!nntp.primenet.com!mr.net!newshub.tc.umn.edu!fu-berlin.de!news-ber1.dfn.de!news-lei1.dfn.de!news-nue1.dfn.de!uni-erlangen.de!winx03!wpxx02!not-for-mail From: krasel@wpxx02.toxi.uni-wuerzburg.de (Cornelius Krasel) Newsgroups: bionet.molbio.proteins.7tms_r Subject: Re: G proteins and structures Date: 18 Dec 1996 14:47:15 GMT Organization: University of Wuerzburg, Germany Lines: 40 Message-ID: <59905j$vvd@winx03.informatik.uni-wuerzburg.de> References: <199612172258.WAA29392@biocserver.BIOC.CWRU.Edu> <32B83A7D.1713@rzmail.uni-erlangen.de> NNTP-Posting-Host: wpxx02.toxi.uni-wuerzburg.de X-Newsreader: TIN [UNIX 1.3 950824BETA PL0] Christian Reiser (christian.reiser@rzmail.uni-erlangen.de) wrote: [I haven't seen the posting of Bryan Roth yet, but he sent me a copy in email. I replied in email as well.] > roth@BIOCSERVER.BIOC.CWRU.EDU wrote: > > > > >Christian Reiser (christian.reiser@rzmail.uni-erlangen.de) wrote: > > >> does anybody know where I might find > > >> the structure of Gs, Gi and transducin with all subunits. > > > > > > > Try the latest release of Nentrez (Net-entrez) and you will find at least 4 > > structures of gi and 2 of transducin in various formats (including PDB > > format). The latest version comes with a nice 3-D viewer as well. There are no structures of heterotrimers in Entrez (available at http://www3.ncbi.nlm.nih.gov/Entrez/) since Entrez relies on the PDB for the structural data. You can access the coordinates mentioned below via Entrez. Nentrez / Net-entrez is a client program that talks with the Entrez server; see the URL above for a much more precise description. As stated previously, the PDB contains only structures of alpha subunits of transducin (1tad: with GDP and AlF ; 1tag: with GDP ; 1tnd: with GTPgS) and Gi (1gdd: with GDP ; 1gfi: with GDP and AlF ; 1gia: with GTPgS ; 1gil: Q204L with GTPgS). The PDB is accessible at http://www.pdb.bnl.gov/ . If you want a colourful picture, you might try Swiss3DImage as well; have a look at http://expasy.hcuge.ch/sw3d/sw3d-top.html. If the protein of your interest is not shown there but its coordinates are known, you can generate a picture yourself at "Molecules R Us", http://molbio.info.nih.gov/cgi-bin/pdb . Hope that helps, --Cornelius. -- /* Cornelius Krasel, U Wuerzburg, Dept. of Pharmacology, Versbacher Str. 9 */ /* D-97078 Wuerzburg, Germany email: phak004@rzbox.uni-wuerzburg.de SP3 */ /* "Science is the game we play with God to find out what His rules are." */ From owner-7tms_r@net.bio.net Tue Dec 17 22:00:00 1996 Path: biosci!bcm.tmc.edu!news.msfc.nasa.gov!www.nntp.primenet.com!nntp.primenet.com!newsxfer2.itd.umich.edu!news.itd.umich.edu!usenet From: Rick Neubig Newsgroups: bionet.molbio.proteins.7tms_r Subject: Re: orphan receptor Date: Wed, 18 Dec 1996 21:57:07 -0500 Organization: University of Michigan Lines: 31 Message-ID: <32B8AF03.1177@umich.edu> References: <009ACFEE.A7E464D2.6@vax.grc.nia.nih.gov> Reply-To: RNeubig@umich.edu NNTP-Posting-Host: host-202.subnet-40.med.umich.edu Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 4.0a1 (Win95; I) X-Priority: Normal I'd suggest contacting Frank Kolakowski. Here's his FASEB listing. KOLAKOWSKI, LEE F., PhD, Asst Prof, Dept Pharmacol, U Texas Hlth Sci Ctr, 7703 Floyd Curl Dr, San Antonio, TX 78284-7764 (2, 95) Tel: 210 567-4233 FAX: 210 567-4303 Email: kolakowski@uthscsa.edu chahrzad@VAX.GRC.NIA.NIH.GOV wrote: > > We have cloned a unique cDNA from adipocytes. It has 1.5Kb open reading > frame and contains putative 7 transmembrane domains. It has no overall > homology with other known receptor. However, looking at the orphan receptor > lists on the web site posted here, I noticed that are domains common to > different receptor families. I am hoping to find a program that could > allow me to find regional homology with one or another G-protein linked > receptor family, that I could have missed in an overall homology search ( > i.e. motifs, etc...). Is there a program that can use to align this novel > sequence with the known motifs? Any help is appreciated. > Chahrzad Montrose > Chahrzad@vax.grc.nia.nih.gov -- _________________________________________________________ Rick Neubig RNeubig@umich.edu Department of Pharmacology University of Michigan Phone (313) 763-3650 FAX (313) 763-4450 http://www-personal.umich.edu/~rneubig/ From owner-7tms_r@net.bio.net Thu Dec 26 22:00:00 1996 Path: biosci!agate!howland.erols.net!www.nntp.primenet.com!nntp.primenet.com!mindspring!cssun.mathcs.emory.edu!news.service.emory.edu!news From: "Kenneth P. Minneman" Newsgroups: bionet.molbio.proteins.7tms_r Subject: postdoctoral positions (corrected) Date: Fri, 27 Dec 1996 09:08:24 -0800 Organization: Emory University Lines: 34 Message-ID: <32C40288.5926@pharm.emory.edu> Reply-To: Department, of, Pharmacology NNTP-Posting-Host: minnpc.pharm.emory.edu Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 3.01Gold (Win16; I) Whoops: Some problems with the last post. Should read as follow: I am recruiting for two postdoctoral positions in my laboratory, starting some time in the next few months. We study the subtle differences and interactions among closely related GPCR subtypes in the adrenergic receptor family. We are particularly interested in what happens when multiple subtypes coexist on the same cell and target the same intracellular signalling pathways. We use a variety of pharmacological and molecular approaches to examine these questions, mainly in cell lines. Some recent publications include: Zhong, H., Guerrero, S., Esbenshade, T., and Minneman, K.P. Inducible expression of beta-1 and beta-2 adrenergic receptors in rat C6 glioma cells: Functioanl interactions between closely related subtypes. Molecular Pharmacology 50: 175-184 (1996). Theroux, T.L., Esbenshade, T.A., Peavy, R.D. and Minneman, K.P. Coupling efficiencies of human alpha-1-adrenergic receptor subtypes: Titration of receptor density and responsiveness with inducible and repressible expression vectors. Molecular Pharmacology 50: 1376-1387 (1996) For more information check out our lab home page at www.emory.edu/PHARMACOLOGY/MINNEMAN or email me at kminneman@pharm.emory.edu From owner-7tms_r@net.bio.net Thu Dec 26 22:00:00 1996 Path: biosci!newshost.lanl.gov!biosci!daresbury!nntp-trd.UNINETT.no!nntp.uio.no!www.nntp.primenet.com!nntp.primenet.com!swrinde!cssun.mathcs.emory.edu!news.service.emory.edu!news From: "Kenneth P. Minneman" Newsgroups: bionet.molbio.proteins.7tms_r Subject: postdoctoral positions Date: Fri, 27 Dec 1996 09:05:13 -0800 Organization: Emory University Lines: 191 Message-ID: <32C401C9.3213@pharm.emory.edu> Reply-To: Department, of, Pharmacology NNTP-Posting-Host: minnpc.pharm.emory.edu Mime-Version: 1.0 Content-Type: multipart/mixed; boundary="------------6DA13A84A11" X-Mailer: Mozilla 3.01Gold (Win16; I) This is a multi-part message in MIME format. --------------6DA13A84A11 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit I am recruiting for two postdoctoral positions in my laboratory, starting some time in the next few months. We study the subtle differences and interactions among closely related GPCR subtypes in the adrenergic receptor family. We are particularly interested in what happens when multiple subtypes coexist on the same cell and target the same intracellular signalling pathways. We use a variety of pharmacological and molecular approaches to examine these questions, mainly in cell lines. Some recent publications include: Zhong, H., Guerrero, S., Esbenshade, T., and Minneman, K.P. Inducible expression of beta-1 and beta-2 adrenergic receptors in rat C6 glioma cells: Functioanl interactions between closely related subtypes. Molecular Pharmacology 50: 175-184 (1996). Theroux, T.L., Esbenshade, T.A., Peavy, R.D. and Minneman, K.P. Coupling efficiencies of human alpha-1-adrenergic receptor subtypes: Titration of receptor density and responsiveness with inducible and repressible expression vectors. Molecular Pharmacology 50: 1376-1387 (1996) For more information check out our lab home page at or email me at kminneman@pharm.emory.edu --------------6DA13A84A11 Content-Type: text/html; charset=us-ascii; name="MINNEMAN" Content-Transfer-Encoding: 7bit Content-Disposition: inline; filename="MINNEMAN" Content-Base: "http://www.emory.edu/PHARMACOLOGY/MINN EMAN" Minneman Lab

Human alpha-1D receptor

Kenneth P. Minneman:

Laboratory for Receptor Pharmacology

Department of Pharmacology at Emory University


Adrenergic Receptor Subtypes:
Differences and Interactions

    This laboratory focuses on the adrenergic receptor family, using it as a model system to study the properties and interactions of closely-related receptor subtypes within a large family. Since it is now clear that most neurotransmitters and hormones exert their effects through large families of receptor subtypes, the actions and interactions of these subtypes must be clearly understood. This will allow a better understanding of intercellular signalling, as well as the actions of specific agonists and antagonist which exert their actions through these receptor families.

    The adrenergic receptor family

    The Adrenergic Receptor Family is composed of three subfamilies, each containing three distinct subtypes. Each of the nine known subtypes are coded by separate genes, and display unique tissue distribution, drug specificities and regulatory properties. Subtypes within a family generally activate the same signal transduction mechanism, but whether there are subtle differences between subtypes in activating the same signalling mechanism, or whether individual subtypes also activate separate and distinct signalling mechanisms are not known.


Signaling by Alpha-1-Adrenergic Receptor Subtypes

    Signal Transduction by Alpha-1-Adrenergic Receptors: Norepinephrine or epinephrine activate a seven-transmembrane receptor, which activates a heterotrimeric G protein composed of alpha, beta and gamma subunits. The alpha and beta/gamma subunits dissociate and activate phospholipase C (PLC)-beta. This enzyme hydrolyzes phosphatidylinositol-4,5-bisphosphate (PIP2) into two products, inositol 1,4,5 trisphosphate (IP3) and diacylglycerol (DAG). IP3 binds to receptors on the endoplasmic reticulum to release stored intracellular calcium. This released calcium acts synergistically with DAG to activate protein kinase C (PKC), which phosphorylates specific target proteins in the cell to change their functions.

Current Members of the Lab:

Hongying Zhong, Ph.D.

Shelly Wood Guerrero, M.S.

Nidhi Gupta Williams, Ph.D.

Deborah Lee, B.S.

Kenneth P. Minneman, Ph.D.

Current Grants

    R01 NS21325 Convergence of Beta-1 and Beta-2-Adrenergic Receptor Subtypes.

    R01 NS32706 Structure and Function of Alpha-1-Adrenergic Receptor Subtypes.


This page is currently under construction.

Contact us at: kminneman@pharm.emory.edu

This page created with Netscape Navigator Gold

This page last updated on December 4, 1996. 

--------------6DA13A84A11-- From owner-7tms_r@net.bio.net Thu Dec 26 22:00:00 1996 Path: biosci!fcs280s.ncifcrf.gov!cpk-news-feed1.bbnplanet.com!news.bbnplanet.com!su-news-hub1.bbnplanet.com!news.sgi.com!swrinde!cssun.mathcs.emory.edu!news.service.emory.edu!news From: "Kenneth P. Minneman" Newsgroups: bionet.molbio.proteins.7tms_r Subject: postdoctoral positions Date: Fri, 27 Dec 1996 09:05:13 -0800 Organization: Emory University Lines: 191 Message-ID: <32C401C9.3213@pharm.emory.edu> Reply-To: Department, of, Pharmacology NNTP-Posting-Host: minnpc.pharm.emory.edu Mime-Version: 1.0 Content-Type: multipart/mixed; boundary="------------6DA13A84A11" X-Mailer: Mozilla 3.01Gold (Win16; I) This is a multi-part message in MIME format. --------------6DA13A84A11 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit I am recruiting for two postdoctoral positions in my laboratory, starting some time in the next few months. We study the subtle differences and interactions among closely related GPCR subtypes in the adrenergic receptor family. We are particularly interested in what happens when multiple subtypes coexist on the same cell and target the same intracellular signalling pathways. We use a variety of pharmacological and molecular approaches to examine these questions, mainly in cell lines. Some recent publications include: Zhong, H., Guerrero, S., Esbenshade, T., and Minneman, K.P. Inducible expression of beta-1 and beta-2 adrenergic receptors in rat C6 glioma cells: Functioanl interactions between closely related subtypes. Molecular Pharmacology 50: 175-184 (1996). Theroux, T.L., Esbenshade, T.A., Peavy, R.D. and Minneman, K.P. Coupling efficiencies of human alpha-1-adrenergic receptor subtypes: Titration of receptor density and responsiveness with inducible and repressible expression vectors. Molecular Pharmacology 50: 1376-1387 (1996) For more information check out our lab home page at or email me at kminneman@pharm.emory.edu --------------6DA13A84A11 Content-Type: text/html; charset=us-ascii; name="MINNEMAN" Content-Transfer-Encoding: 7bit Content-Disposition: inline; filename="MINNEMAN" Content-Base: "http://www.emory.edu/PHARMACOLOGY/MINN EMAN" Minneman Lab

Human alpha-1D receptor

Kenneth P. Minneman:

Laboratory for Receptor Pharmacology

Department of Pharmacology at Emory University


Adrenergic Receptor Subtypes:
Differences and Interactions

    This laboratory focuses on the adrenergic receptor family, using it as a model system to study the properties and interactions of closely-related receptor subtypes within a large family. Since it is now clear that most neurotransmitters and hormones exert their effects through large families of receptor subtypes, the actions and interactions of these subtypes must be clearly understood. This will allow a better understanding of intercellular signalling, as well as the actions of specific agonists and antagonist which exert their actions through these receptor families.

    The adrenergic receptor family

    The Adrenergic Receptor Family is composed of three subfamilies, each containing three distinct subtypes. Each of the nine known subtypes are coded by separate genes, and display unique tissue distribution, drug specificities and regulatory properties. Subtypes within a family generally activate the same signal transduction mechanism, but whether there are subtle differences between subtypes in activating the same signalling mechanism, or whether individual subtypes also activate separate and distinct signalling mechanisms are not known.


Signaling by Alpha-1-Adrenergic Receptor Subtypes

    Signal Transduction by Alpha-1-Adrenergic Receptors: Norepinephrine or epinephrine activate a seven-transmembrane receptor, which activates a heterotrimeric G protein composed of alpha, beta and gamma subunits. The alpha and beta/gamma subunits dissociate and activate phospholipase C (PLC)-beta. This enzyme hydrolyzes phosphatidylinositol-4,5-bisphosphate (PIP2) into two products, inositol 1,4,5 trisphosphate (IP3) and diacylglycerol (DAG). IP3 binds to receptors on the endoplasmic reticulum to release stored intracellular calcium. This released calcium acts synergistically with DAG to activate protein kinase C (PKC), which phosphorylates specific target proteins in the cell to change their functions.

Current Members of the Lab:

Hongying Zhong, Ph.D.

Shelly Wood Guerrero, M.S.

Nidhi Gupta Williams, Ph.D.

Deborah Lee, B.S.

Kenneth P. Minneman, Ph.D.

Current Grants

    R01 NS21325 Convergence of Beta-1 and Beta-2-Adrenergic Receptor Subtypes.

    R01 NS32706 Structure and Function of Alpha-1-Adrenergic Receptor Subtypes.


This page is currently under construction.

Contact us at: kminneman@pharm.emory.edu

This page created with Netscape Navigator Gold

This page last updated on December 4, 1996. 

--------------6DA13A84A11-- From owner-7tms_r@net.bio.net Thu Dec 26 22:00:00 1996 Path: biosci!bcm.tmc.edu!news.msfc.nasa.gov!news.sgi.com!swrinde!cssun.mathcs.emory.edu!news.service.emory.edu!news From: "Kenneth P. Minneman" Newsgroups: bionet.molbio.proteins.7tms_r Subject: postdoctoral positions Date: Fri, 27 Dec 1996 09:05:13 -0800 Organization: Emory University Lines: 191 Message-ID: <32C401C9.3213@pharm.emory.edu> Reply-To: Department, of, Pharmacology NNTP-Posting-Host: minnpc.pharm.emory.edu Mime-Version: 1.0 Content-Type: multipart/mixed; boundary="------------6DA13A84A11" X-Mailer: Mozilla 3.01Gold (Win16; I) This is a multi-part message in MIME format. --------------6DA13A84A11 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit I am recruiting for two postdoctoral positions in my laboratory, starting some time in the next few months. We study the subtle differences and interactions among closely related GPCR subtypes in the adrenergic receptor family. We are particularly interested in what happens when multiple subtypes coexist on the same cell and target the same intracellular signalling pathways. We use a variety of pharmacological and molecular approaches to examine these questions, mainly in cell lines. Some recent publications include: Zhong, H., Guerrero, S., Esbenshade, T., and Minneman, K.P. Inducible expression of beta-1 and beta-2 adrenergic receptors in rat C6 glioma cells: Functioanl interactions between closely related subtypes. Molecular Pharmacology 50: 175-184 (1996). Theroux, T.L., Esbenshade, T.A., Peavy, R.D. and Minneman, K.P. Coupling efficiencies of human alpha-1-adrenergic receptor subtypes: Titration of receptor density and responsiveness with inducible and repressible expression vectors. Molecular Pharmacology 50: 1376-1387 (1996) For more information check out our lab home page at or email me at kminneman@pharm.emory.edu --------------6DA13A84A11 Content-Type: text/html; charset=us-ascii; name="MINNEMAN" Content-Transfer-Encoding: 7bit Content-Disposition: inline; filename="MINNEMAN" Content-Base: "http://www.emory.edu/PHARMACOLOGY/MINN EMAN" Minneman Lab

Human alpha-1D receptor

Kenneth P. Minneman:

Laboratory for Receptor Pharmacology

Department of Pharmacology at Emory University


Adrenergic Receptor Subtypes:
Differences and Interactions

    This laboratory focuses on the adrenergic receptor family, using it as a model system to study the properties and interactions of closely-related receptor subtypes within a large family. Since it is now clear that most neurotransmitters and hormones exert their effects through large families of receptor subtypes, the actions and interactions of these subtypes must be clearly understood. This will allow a better understanding of intercellular signalling, as well as the actions of specific agonists and antagonist which exert their actions through these receptor families.

    The adrenergic receptor family

    The Adrenergic Receptor Family is composed of three subfamilies, each containing three distinct subtypes. Each of the nine known subtypes are coded by separate genes, and display unique tissue distribution, drug specificities and regulatory properties. Subtypes within a family generally activate the same signal transduction mechanism, but whether there are subtle differences between subtypes in activating the same signalling mechanism, or whether individual subtypes also activate separate and distinct signalling mechanisms are not known.


Signaling by Alpha-1-Adrenergic Receptor Subtypes

    Signal Transduction by Alpha-1-Adrenergic Receptors: Norepinephrine or epinephrine activate a seven-transmembrane receptor, which activates a heterotrimeric G protein composed of alpha, beta and gamma subunits. The alpha and beta/gamma subunits dissociate and activate phospholipase C (PLC)-beta. This enzyme hydrolyzes phosphatidylinositol-4,5-bisphosphate (PIP2) into two products, inositol 1,4,5 trisphosphate (IP3) and diacylglycerol (DAG). IP3 binds to receptors on the endoplasmic reticulum to release stored intracellular calcium. This released calcium acts synergistically with DAG to activate protein kinase C (PKC), which phosphorylates specific target proteins in the cell to change their functions.

Current Members of the Lab:

Hongying Zhong, Ph.D.

Shelly Wood Guerrero, M.S.

Nidhi Gupta Williams, Ph.D.

Deborah Lee, B.S.

Kenneth P. Minneman, Ph.D.

Current Grants

    R01 NS21325 Convergence of Beta-1 and Beta-2-Adrenergic Receptor Subtypes.

    R01 NS32706 Structure and Function of Alpha-1-Adrenergic Receptor Subtypes.


This page is currently under construction.

Contact us at: kminneman@pharm.emory.edu

This page created with Netscape Navigator Gold

This page last updated on December 4, 1996. 

--------------6DA13A84A11-- From owner-7tms_r@net.bio.net Thu Dec 26 22:00:00 1996 Path: biosci!daresbury!nntp-trd.UNINETT.no!nntp.uio.no!www.nntp.primenet.com!nntp.primenet.com!swrinde!cssun.mathcs.emory.edu!news.service.emory.edu!news From: "Kenneth P. Minneman" Newsgroups: bionet.molbio.proteins.7tms_r Subject: postdoctoral positions Date: Fri, 27 Dec 1996 09:05:13 -0800 Organization: Emory University Lines: 191 Message-ID: <32C401C9.3213@pharm.emory.edu> Reply-To: Department, of, Pharmacology NNTP-Posting-Host: minnpc.pharm.emory.edu Mime-Version: 1.0 Content-Type: multipart/mixed; boundary="------------6DA13A84A11" X-Mailer: Mozilla 3.01Gold (Win16; I) This is a multi-part message in MIME format. --------------6DA13A84A11 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit I am recruiting for two postdoctoral positions in my laboratory, starting some time in the next few months. We study the subtle differences and interactions among closely related GPCR subtypes in the adrenergic receptor family. We are particularly interested in what happens when multiple subtypes coexist on the same cell and target the same intracellular signalling pathways. We use a variety of pharmacological and molecular approaches to examine these questions, mainly in cell lines. Some recent publications include: Zhong, H., Guerrero, S., Esbenshade, T., and Minneman, K.P. Inducible expression of beta-1 and beta-2 adrenergic receptors in rat C6 glioma cells: Functioanl interactions between closely related subtypes. Molecular Pharmacology 50: 175-184 (1996). Theroux, T.L., Esbenshade, T.A., Peavy, R.D. and Minneman, K.P. Coupling efficiencies of human alpha-1-adrenergic receptor subtypes: Titration of receptor density and responsiveness with inducible and repressible expression vectors. Molecular Pharmacology 50: 1376-1387 (1996) For more information check out our lab home page at or email me at kminneman@pharm.emory.edu --------------6DA13A84A11 Content-Type: text/html; charset=us-ascii; name="MINNEMAN" Content-Transfer-Encoding: 7bit Content-Disposition: inline; filename="MINNEMAN" Content-Base: "http://www.emory.edu/PHARMACOLOGY/MINN EMAN" Minneman Lab

Human alpha-1D receptor

Kenneth P. Minneman:

Laboratory for Receptor Pharmacology

Department of Pharmacology at Emory University


Adrenergic Receptor Subtypes:
Differences and Interactions

    This laboratory focuses on the adrenergic receptor family, using it as a model system to study the properties and interactions of closely-related receptor subtypes within a large family. Since it is now clear that most neurotransmitters and hormones exert their effects through large families of receptor subtypes, the actions and interactions of these subtypes must be clearly understood. This will allow a better understanding of intercellular signalling, as well as the actions of specific agonists and antagonist which exert their actions through these receptor families.

    The adrenergic receptor family

    The Adrenergic Receptor Family is composed of three subfamilies, each containing three distinct subtypes. Each of the nine known subtypes are coded by separate genes, and display unique tissue distribution, drug specificities and regulatory properties. Subtypes within a family generally activate the same signal transduction mechanism, but whether there are subtle differences between subtypes in activating the same signalling mechanism, or whether individual subtypes also activate separate and distinct signalling mechanisms are not known.


Signaling by Alpha-1-Adrenergic Receptor Subtypes

    Signal Transduction by Alpha-1-Adrenergic Receptors: Norepinephrine or epinephrine activate a seven-transmembrane receptor, which activates a heterotrimeric G protein composed of alpha, beta and gamma subunits. The alpha and beta/gamma subunits dissociate and activate phospholipase C (PLC)-beta. This enzyme hydrolyzes phosphatidylinositol-4,5-bisphosphate (PIP2) into two products, inositol 1,4,5 trisphosphate (IP3) and diacylglycerol (DAG). IP3 binds to receptors on the endoplasmic reticulum to release stored intracellular calcium. This released calcium acts synergistically with DAG to activate protein kinase C (PKC), which phosphorylates specific target proteins in the cell to change their functions.

Current Members of the Lab:

Hongying Zhong, Ph.D.

Shelly Wood Guerrero, M.S.

Nidhi Gupta Williams, Ph.D.

Deborah Lee, B.S.

Kenneth P. Minneman, Ph.D.

Current Grants

    R01 NS21325 Convergence of Beta-1 and Beta-2-Adrenergic Receptor Subtypes.

    R01 NS32706 Structure and Function of Alpha-1-Adrenergic Receptor Subtypes.


This page is currently under construction.

Contact us at: kminneman@pharm.emory.edu

This page created with Netscape Navigator Gold

This page last updated on December 4, 1996. 

--------------6DA13A84A11-- From owner-7tms_r@net.bio.net Thu Dec 26 22:00:00 1996 Path: biosci!rutgers!cnn.Princeton.EDU!udel-eecis!newsfeed.direct.ca!op.net!www.nntp.primenet.com!nntp.primenet.com!feed1.news.erols.com!howland.erols.net!newsfeed.internetmci.com!news.msfc.nasa.gov!voskovec.radio.cz!btnet-feed2!unlisys!cs.tu-berlin.de!zrz.TU-Berlin.DE!news-ber1.dfn.de!news-lei1.dfn.de!news-nue1.dfn.de!uni-erlangen.de!rznews.rrze.uni-erlangen.de!news From: Christian Reiser Newsgroups: bionet.molbio.proteins.7tms_r Subject: Re: G proteins and structures Date: Wed, 18 Dec 1996 10:39:57 -0800 Organization: Med IV, Nephrologische Forschung Lines: 18 Message-ID: <32B83A7D.1713@rzmail.uni-erlangen.de> References: <199612172258.WAA29392@biocserver.BIOC.CWRU.Edu> NNTP-Posting-Host: mfm410.dialin.rrze.uni-erlangen.de Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 2.02 (Win16; I) roth@BIOCSERVER.BIOC.CWRU.EDU wrote: > > >Christian Reiser (christian.reiser@rzmail.uni-erlangen.de) wrote: > >> does anybody know where I might find > >> the structure of Gs, Gi and transducin with all subunits. > > > > Try the latest release of Nentrez (Net-entrez) and you will find at least 4 > structures of gi and 2 of transducin in various formats (including PDB > format). The latest version comes with a nice 3-D viewer as well. > > All the above is free! > Sorry, but where can I find the latest version of Net-entrez. I tried several search-engines, but could not find anything. Thanks Chris From owner-7tms_r@net.bio.net Thu Dec 26 22:00:00 1996 Path: biosci!ihnp4.ucsd.edu!swrinde!www.nntp.primenet.com!nntp.primenet.com!mindspring!cssun.mathcs.emory.edu!news.service.emory.edu!news From: "Kenneth P. Minneman" Newsgroups: bionet.molbio.proteins.7tms_r Subject: postdoctoral positions (corrected) Date: Fri, 27 Dec 1996 09:08:24 -0800 Organization: Emory University Lines: 34 Message-ID: <32C40288.5926@pharm.emory.edu> Reply-To: Department, of, Pharmacology NNTP-Posting-Host: minnpc.pharm.emory.edu Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 3.01Gold (Win16; I) Whoops: Some problems with the last post. Should read as follow: I am recruiting for two postdoctoral positions in my laboratory, starting some time in the next few months. We study the subtle differences and interactions among closely related GPCR subtypes in the adrenergic receptor family. We are particularly interested in what happens when multiple subtypes coexist on the same cell and target the same intracellular signalling pathways. We use a variety of pharmacological and molecular approaches to examine these questions, mainly in cell lines. Some recent publications include: Zhong, H., Guerrero, S., Esbenshade, T., and Minneman, K.P. Inducible expression of beta-1 and beta-2 adrenergic receptors in rat C6 glioma cells: Functioanl interactions between closely related subtypes. Molecular Pharmacology 50: 175-184 (1996). Theroux, T.L., Esbenshade, T.A., Peavy, R.D. and Minneman, K.P. Coupling efficiencies of human alpha-1-adrenergic receptor subtypes: Titration of receptor density and responsiveness with inducible and repressible expression vectors. Molecular Pharmacology 50: 1376-1387 (1996) For more information check out our lab home page at www.emory.edu/PHARMACOLOGY/MINNEMAN or email me at kminneman@pharm.emory.edu From owner-7tms_r@net.bio.net Thu Dec 26 22:00:00 1996 Path: biosci!ihnp4.ucsd.edu!munnari.OZ.AU!news.ecn.uoknor.edu!feed1.news.erols.com!howland.erols.net!swrinde!cssun.mathcs.emory.edu!news.service.emory.edu!news From: "Kenneth P. Minneman" Newsgroups: bionet.molbio.proteins.7tms_r Subject: postdoctoral positions Date: Fri, 27 Dec 1996 09:05:13 -0800 Organization: Emory University Lines: 191 Message-ID: <32C401C9.3213@pharm.emory.edu> Reply-To: Department, of, Pharmacology NNTP-Posting-Host: minnpc.pharm.emory.edu Mime-Version: 1.0 Content-Type: multipart/mixed; boundary="------------6DA13A84A11" X-Mailer: Mozilla 3.01Gold (Win16; I) This is a multi-part message in MIME format. --------------6DA13A84A11 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit I am recruiting for two postdoctoral positions in my laboratory, starting some time in the next few months. We study the subtle differences and interactions among closely related GPCR subtypes in the adrenergic receptor family. We are particularly interested in what happens when multiple subtypes coexist on the same cell and target the same intracellular signalling pathways. We use a variety of pharmacological and molecular approaches to examine these questions, mainly in cell lines. Some recent publications include: Zhong, H., Guerrero, S., Esbenshade, T., and Minneman, K.P. Inducible expression of beta-1 and beta-2 adrenergic receptors in rat C6 glioma cells: Functioanl interactions between closely related subtypes. Molecular Pharmacology 50: 175-184 (1996). Theroux, T.L., Esbenshade, T.A., Peavy, R.D. and Minneman, K.P. Coupling efficiencies of human alpha-1-adrenergic receptor subtypes: Titration of receptor density and responsiveness with inducible and repressible expression vectors. Molecular Pharmacology 50: 1376-1387 (1996) For more information check out our lab home page at or email me at kminneman@pharm.emory.edu --------------6DA13A84A11 Content-Type: text/html; charset=us-ascii; name="MINNEMAN" Content-Transfer-Encoding: 7bit Content-Disposition: inline; filename="MINNEMAN" Content-Base: "http://www.emory.edu/PHARMACOLOGY/MINN EMAN" Minneman Lab

Human alpha-1D receptor

Kenneth P. Minneman:

Laboratory for Receptor Pharmacology

Department of Pharmacology at Emory University


Adrenergic Receptor Subtypes:
Differences and Interactions

    This laboratory focuses on the adrenergic receptor family, using it as a model system to study the properties and interactions of closely-related receptor subtypes within a large family. Since it is now clear that most neurotransmitters and hormones exert their effects through large families of receptor subtypes, the actions and interactions of these subtypes must be clearly understood. This will allow a better understanding of intercellular signalling, as well as the actions of specific agonists and antagonist which exert their actions through these receptor families.

    The adrenergic receptor family

    The Adrenergic Receptor Family is composed of three subfamilies, each containing three distinct subtypes. Each of the nine known subtypes are coded by separate genes, and display unique tissue distribution, drug specificities and regulatory properties. Subtypes within a family generally activate the same signal transduction mechanism, but whether there are subtle differences between subtypes in activating the same signalling mechanism, or whether individual subtypes also activate separate and distinct signalling mechanisms are not known.


Signaling by Alpha-1-Adrenergic Receptor Subtypes

    Signal Transduction by Alpha-1-Adrenergic Receptors: Norepinephrine or epinephrine activate a seven-transmembrane receptor, which activates a heterotrimeric G protein composed of alpha, beta and gamma subunits. The alpha and beta/gamma subunits dissociate and activate phospholipase C (PLC)-beta. This enzyme hydrolyzes phosphatidylinositol-4,5-bisphosphate (PIP2) into two products, inositol 1,4,5 trisphosphate (IP3) and diacylglycerol (DAG). IP3 binds to receptors on the endoplasmic reticulum to release stored intracellular calcium. This released calcium acts synergistically with DAG to activate protein kinase C (PKC), which phosphorylates specific target proteins in the cell to change their functions.

Current Members of the Lab:

Hongying Zhong, Ph.D.

Shelly Wood Guerrero, M.S.

Nidhi Gupta Williams, Ph.D.

Deborah Lee, B.S.

Kenneth P. Minneman, Ph.D.

Current Grants

    R01 NS21325 Convergence of Beta-1 and Beta-2-Adrenergic Receptor Subtypes.

    R01 NS32706 Structure and Function of Alpha-1-Adrenergic Receptor Subtypes.


This page is currently under construction.

Contact us at: kminneman@pharm.emory.edu

This page created with Netscape Navigator Gold

This page last updated on December 4, 1996. 

--------------6DA13A84A11-- From owner-7tms_r@net.bio.net Thu Dec 26 22:00:00 1996 Path: biosci!bcm.tmc.edu!news.msfc.nasa.gov!www.nntp.primenet.com!nntp.primenet.com!mindspring!cssun.mathcs.emory.edu!news.service.emory.edu!news From: "Kenneth P. Minneman" Newsgroups: bionet.molbio.proteins.7tms_r Subject: postdoctoral positions (corrected) Date: Fri, 27 Dec 1996 09:08:24 -0800 Organization: Emory University Lines: 34 Message-ID: <32C40288.5926@pharm.emory.edu> Reply-To: Department, of, Pharmacology NNTP-Posting-Host: minnpc.pharm.emory.edu Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 3.01Gold (Win16; I) Whoops: Some problems with the last post. Should read as follow: I am recruiting for two postdoctoral positions in my laboratory, starting some time in the next few months. We study the subtle differences and interactions among closely related GPCR subtypes in the adrenergic receptor family. We are particularly interested in what happens when multiple subtypes coexist on the same cell and target the same intracellular signalling pathways. We use a variety of pharmacological and molecular approaches to examine these questions, mainly in cell lines. Some recent publications include: Zhong, H., Guerrero, S., Esbenshade, T., and Minneman, K.P. Inducible expression of beta-1 and beta-2 adrenergic receptors in rat C6 glioma cells: Functioanl interactions between closely related subtypes. Molecular Pharmacology 50: 175-184 (1996). Theroux, T.L., Esbenshade, T.A., Peavy, R.D. and Minneman, K.P. Coupling efficiencies of human alpha-1-adrenergic receptor subtypes: Titration of receptor density and responsiveness with inducible and repressible expression vectors. Molecular Pharmacology 50: 1376-1387 (1996) For more information check out our lab home page at www.emory.edu/PHARMACOLOGY/MINNEMAN or email me at kminneman@pharm.emory.edu From owner-7tms_r@net.bio.net Thu Dec 26 22:00:00 1996 Path: biosci!newshost.lanl.gov!biosci!ihnp4.ucsd.edu!swrinde!www.nntp.primenet.com!nntp.primenet.com!mindspring!cssun.mathcs.emory.edu!news.service.emory.edu!news From: "Kenneth P. Minneman" Newsgroups: bionet.molbio.proteins.7tms_r Subject: postdoctoral positions (corrected) Date: Fri, 27 Dec 1996 09:08:24 -0800 Organization: Emory University Lines: 34 Message-ID: <32C40288.5926@pharm.emory.edu> Reply-To: Department, of, Pharmacology NNTP-Posting-Host: minnpc.pharm.emory.edu Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 3.01Gold (Win16; I) Whoops: Some problems with the last post. Should read as follow: I am recruiting for two postdoctoral positions in my laboratory, starting some time in the next few months. We study the subtle differences and interactions among closely related GPCR subtypes in the adrenergic receptor family. We are particularly interested in what happens when multiple subtypes coexist on the same cell and target the same intracellular signalling pathways. We use a variety of pharmacological and molecular approaches to examine these questions, mainly in cell lines. Some recent publications include: Zhong, H., Guerrero, S., Esbenshade, T., and Minneman, K.P. Inducible expression of beta-1 and beta-2 adrenergic receptors in rat C6 glioma cells: Functioanl interactions between closely related subtypes. Molecular Pharmacology 50: 175-184 (1996). Theroux, T.L., Esbenshade, T.A., Peavy, R.D. and Minneman, K.P. Coupling efficiencies of human alpha-1-adrenergic receptor subtypes: Titration of receptor density and responsiveness with inducible and repressible expression vectors. Molecular Pharmacology 50: 1376-1387 (1996) For more information check out our lab home page at www.emory.edu/PHARMACOLOGY/MINNEMAN or email me at kminneman@pharm.emory.edu From owner-7tms_r@net.bio.net Thu Dec 26 22:00:00 1996 Path: biosci!news.artemis.com!uunet!in2.uu.net!204.180.128.35!news.mindspring.com!mindspring!cssun.mathcs.emory.edu!news.service.emory.edu!news From: "Kenneth P. Minneman" Newsgroups: bionet.molbio.proteins.7tms_r Subject: postdoctoral positions (corrected) Date: Fri, 27 Dec 1996 09:08:24 -0800 Organization: Emory University Lines: 34 Message-ID: <32C40288.5926@pharm.emory.edu> Reply-To: Department, of, Pharmacology NNTP-Posting-Host: minnpc.pharm.emory.edu Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 3.01Gold (Win16; I) Whoops: Some problems with the last post. Should read as follow: I am recruiting for two postdoctoral positions in my laboratory, starting some time in the next few months. We study the subtle differences and interactions among closely related GPCR subtypes in the adrenergic receptor family. We are particularly interested in what happens when multiple subtypes coexist on the same cell and target the same intracellular signalling pathways. We use a variety of pharmacological and molecular approaches to examine these questions, mainly in cell lines. Some recent publications include: Zhong, H., Guerrero, S., Esbenshade, T., and Minneman, K.P. Inducible expression of beta-1 and beta-2 adrenergic receptors in rat C6 glioma cells: Functioanl interactions between closely related subtypes. Molecular Pharmacology 50: 175-184 (1996). Theroux, T.L., Esbenshade, T.A., Peavy, R.D. and Minneman, K.P. Coupling efficiencies of human alpha-1-adrenergic receptor subtypes: Titration of receptor density and responsiveness with inducible and repressible expression vectors. Molecular Pharmacology 50: 1376-1387 (1996) For more information check out our lab home page at www.emory.edu/PHARMACOLOGY/MINNEMAN or email me at kminneman@pharm.emory.edu From owner-7tms_r@net.bio.net Thu Dec 26 22:00:00 1996 Path: biosci!fcs280s.ncifcrf.gov!cpk-news-feed1.bbnplanet.com!news.bbnplanet.com!cpk-news-hub1.bbnplanet.com!mindspring!cssun.mathcs.emory.edu!news.service.emory.edu!news From: "Kenneth P. Minneman" Newsgroups: bionet.molbio.proteins.7tms_r Subject: postdoctoral positions (corrected) Date: Fri, 27 Dec 1996 09:08:24 -0800 Organization: Emory University Lines: 34 Message-ID: <32C40288.5926@pharm.emory.edu> Reply-To: Department, of, Pharmacology NNTP-Posting-Host: minnpc.pharm.emory.edu Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 3.01Gold (Win16; I) Whoops: Some problems with the last post. Should read as follow: I am recruiting for two postdoctoral positions in my laboratory, starting some time in the next few months. We study the subtle differences and interactions among closely related GPCR subtypes in the adrenergic receptor family. We are particularly interested in what happens when multiple subtypes coexist on the same cell and target the same intracellular signalling pathways. We use a variety of pharmacological and molecular approaches to examine these questions, mainly in cell lines. Some recent publications include: Zhong, H., Guerrero, S., Esbenshade, T., and Minneman, K.P. Inducible expression of beta-1 and beta-2 adrenergic receptors in rat C6 glioma cells: Functioanl interactions between closely related subtypes. Molecular Pharmacology 50: 175-184 (1996). Theroux, T.L., Esbenshade, T.A., Peavy, R.D. and Minneman, K.P. Coupling efficiencies of human alpha-1-adrenergic receptor subtypes: Titration of receptor density and responsiveness with inducible and repressible expression vectors. Molecular Pharmacology 50: 1376-1387 (1996) For more information check out our lab home page at www.emory.edu/PHARMACOLOGY/MINNEMAN or email me at kminneman@pharm.emory.edu From owner-7tms_r@net.bio.net Thu Dec 26 22:00:00 1996 Path: biosci!lhc.nlm.nih.gov!biosci!daresbury!nntp-trd.UNINETT.no!nntp.uio.no!www.nntp.primenet.com!nntp.primenet.com!swrinde!cssun.mathcs.emory.edu!news.service.emory.edu!news From: "Kenneth P. Minneman" Newsgroups: bionet.molbio.proteins.7tms_r Subject: postdoctoral positions Date: Fri, 27 Dec 1996 09:05:13 -0800 Organization: Emory University Lines: 191 Message-ID: <32C401C9.3213@pharm.emory.edu> Reply-To: Department, of, Pharmacology NNTP-Posting-Host: minnpc.pharm.emory.edu Mime-Version: 1.0 Content-Type: multipart/mixed; boundary="------------6DA13A84A11" X-Mailer: Mozilla 3.01Gold (Win16; I) This is a multi-part message in MIME format. --------------6DA13A84A11 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit I am recruiting for two postdoctoral positions in my laboratory, starting some time in the next few months. We study the subtle differences and interactions among closely related GPCR subtypes in the adrenergic receptor family. We are particularly interested in what happens when multiple subtypes coexist on the same cell and target the same intracellular signalling pathways. We use a variety of pharmacological and molecular approaches to examine these questions, mainly in cell lines. Some recent publications include: Zhong, H., Guerrero, S., Esbenshade, T., and Minneman, K.P. Inducible expression of beta-1 and beta-2 adrenergic receptors in rat C6 glioma cells: Functioanl interactions between closely related subtypes. Molecular Pharmacology 50: 175-184 (1996). Theroux, T.L., Esbenshade, T.A., Peavy, R.D. and Minneman, K.P. Coupling efficiencies of human alpha-1-adrenergic receptor subtypes: Titration of receptor density and responsiveness with inducible and repressible expression vectors. Molecular Pharmacology 50: 1376-1387 (1996) For more information check out our lab home page at or email me at kminneman@pharm.emory.edu --------------6DA13A84A11 Content-Type: text/html; charset=us-ascii; name="MINNEMAN" Content-Transfer-Encoding: 7bit Content-Disposition: inline; filename="MINNEMAN" Content-Base: "http://www.emory.edu/PHARMACOLOGY/MINN EMAN" Minneman Lab

Human alpha-1D receptor

Kenneth P. Minneman:

Laboratory for Receptor Pharmacology

Department of Pharmacology at Emory University


Adrenergic Receptor Subtypes:
Differences and Interactions

    This laboratory focuses on the adrenergic receptor family, using it as a model system to study the properties and interactions of closely-related receptor subtypes within a large family. Since it is now clear that most neurotransmitters and hormones exert their effects through large families of receptor subtypes, the actions and interactions of these subtypes must be clearly understood. This will allow a better understanding of intercellular signalling, as well as the actions of specific agonists and antagonist which exert their actions through these receptor families.

    The adrenergic receptor family

    The Adrenergic Receptor Family is composed of three subfamilies, each containing three distinct subtypes. Each of the nine known subtypes are coded by separate genes, and display unique tissue distribution, drug specificities and regulatory properties. Subtypes within a family generally activate the same signal transduction mechanism, but whether there are subtle differences between subtypes in activating the same signalling mechanism, or whether individual subtypes also activate separate and distinct signalling mechanisms are not known.


Signaling by Alpha-1-Adrenergic Receptor Subtypes

    Signal Transduction by Alpha-1-Adrenergic Receptors: Norepinephrine or epinephrine activate a seven-transmembrane receptor, which activates a heterotrimeric G protein composed of alpha, beta and gamma subunits. The alpha and beta/gamma subunits dissociate and activate phospholipase C (PLC)-beta. This enzyme hydrolyzes phosphatidylinositol-4,5-bisphosphate (PIP2) into two products, inositol 1,4,5 trisphosphate (IP3) and diacylglycerol (DAG). IP3 binds to receptors on the endoplasmic reticulum to release stored intracellular calcium. This released calcium acts synergistically with DAG to activate protein kinase C (PKC), which phosphorylates specific target proteins in the cell to change their functions.

Current Members of the Lab:

Hongying Zhong, Ph.D.

Shelly Wood Guerrero, M.S.

Nidhi Gupta Williams, Ph.D.

Deborah Lee, B.S.

Kenneth P. Minneman, Ph.D.

Current Grants

    R01 NS21325 Convergence of Beta-1 and Beta-2-Adrenergic Receptor Subtypes.

    R01 NS32706 Structure and Function of Alpha-1-Adrenergic Receptor Subtypes.


This page is currently under construction.

Contact us at: kminneman@pharm.emory.edu

This page created with Netscape Navigator Gold

This page last updated on December 4, 1996. 

--------------6DA13A84A11-- From owner-7tms_r@net.bio.net Thu Dec 26 22:00:00 1996 Path: biosci!lhc.nlm.nih.gov!biosci!ihnp4.ucsd.edu!swrinde!www.nntp.primenet.com!nntp.primenet.com!mindspring!cssun.mathcs.emory.edu!news.service.emory.edu!news From: "Kenneth P. Minneman" Newsgroups: bionet.molbio.proteins.7tms_r Subject: postdoctoral positions (corrected) Date: Fri, 27 Dec 1996 09:08:24 -0800 Organization: Emory University Lines: 34 Message-ID: <32C40288.5926@pharm.emory.edu> Reply-To: Department, of, Pharmacology NNTP-Posting-Host: minnpc.pharm.emory.edu Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 3.01Gold (Win16; I) Whoops: Some problems with the last post. Should read as follow: I am recruiting for two postdoctoral positions in my laboratory, starting some time in the next few months. We study the subtle differences and interactions among closely related GPCR subtypes in the adrenergic receptor family. We are particularly interested in what happens when multiple subtypes coexist on the same cell and target the same intracellular signalling pathways. We use a variety of pharmacological and molecular approaches to examine these questions, mainly in cell lines. Some recent publications include: Zhong, H., Guerrero, S., Esbenshade, T., and Minneman, K.P. Inducible expression of beta-1 and beta-2 adrenergic receptors in rat C6 glioma cells: Functioanl interactions between closely related subtypes. Molecular Pharmacology 50: 175-184 (1996). Theroux, T.L., Esbenshade, T.A., Peavy, R.D. and Minneman, K.P. Coupling efficiencies of human alpha-1-adrenergic receptor subtypes: Titration of receptor density and responsiveness with inducible and repressible expression vectors. Molecular Pharmacology 50: 1376-1387 (1996) For more information check out our lab home page at www.emory.edu/PHARMACOLOGY/MINNEMAN or email me at kminneman@pharm.emory.edu From owner-7tms_r@net.bio.net Thu Dec 26 22:00:00 1996 Path: biosci!daresbury!nntp-trd.UNINETT.no!nntp.uio.no!www.nntp.primenet.com!nntp.primenet.com!mindspring!cssun.mathcs.emory.edu!news.service.emory.edu!news From: "Kenneth P. Minneman" Newsgroups: bionet.molbio.proteins.7tms_r Subject: postdoctoral positions (corrected) Date: Fri, 27 Dec 1996 09:08:24 -0800 Organization: Emory University Lines: 34 Message-ID: <32C40288.5926@pharm.emory.edu> Reply-To: Department, of, Pharmacology NNTP-Posting-Host: minnpc.pharm.emory.edu Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 3.01Gold (Win16; I) Whoops: Some problems with the last post. Should read as follow: I am recruiting for two postdoctoral positions in my laboratory, starting some time in the next few months. We study the subtle differences and interactions among closely related GPCR subtypes in the adrenergic receptor family. We are particularly interested in what happens when multiple subtypes coexist on the same cell and target the same intracellular signalling pathways. We use a variety of pharmacological and molecular approaches to examine these questions, mainly in cell lines. Some recent publications include: Zhong, H., Guerrero, S., Esbenshade, T., and Minneman, K.P. Inducible expression of beta-1 and beta-2 adrenergic receptors in rat C6 glioma cells: Functioanl interactions between closely related subtypes. Molecular Pharmacology 50: 175-184 (1996). Theroux, T.L., Esbenshade, T.A., Peavy, R.D. and Minneman, K.P. Coupling efficiencies of human alpha-1-adrenergic receptor subtypes: Titration of receptor density and responsiveness with inducible and repressible expression vectors. Molecular Pharmacology 50: 1376-1387 (1996) For more information check out our lab home page at www.emory.edu/PHARMACOLOGY/MINNEMAN or email me at kminneman@pharm.emory.edu From owner-7tms_r@net.bio.net Fri Dec 27 22:00:00 1996 Path: biosci!ihnp4.ucsd.edu!munnari.OZ.AU!news.ecn.uoknor.edu!feed1.news.erols.com!howland.erols.net!portc02.blue.aol.com!newsfeed.pitt.edu!newsflash.concordia.ca!sunqbc.risq.net!news.risq.qc.ca!news.mcgill.ca!news From: mceh Newsgroups: bionet.molbio.proteins.7tms_r Subject: knock-outs and transgenic Date: Sat, 28 Dec 1996 19:50:24 -0500 Organization: MNI Lines: 5 Message-ID: <32C5C050.7D09@musicb.mcgill.ca> Reply-To: br7a@musicb.mcgill.ca NNTP-Posting-Host: 132.206.201.4 Mime-Version: 1.0 Content-Type: text/plain; charset=us-ascii Content-Transfer-Encoding: 7bit X-Mailer: Mozilla 3.0Gold (Win95; I) Hi, Do you know a lab developping knock-out or transgenic rats? If so can you give me their address? Thank you Isabelle From owner-7tms_r@net.bio.net Sun Dec 29 22:00:00 1996 Path: biosci!bcm.tmc.edu!cs.utexas.edu!howland.erols.net!usenet.kornet.nm.kr!newsfeed.dacom.co.kr!usenet.dacom.co.kr!not-for-mail From: "Jongmin-Nam" Newsgroups: bionet.molbio.proteins.7tms_r Subject: protein secretion system?? Date: 31 Dec 1996 05:22:57 GMT Organization: DACOM Internet Service Lines: 8 Message-ID: <01bbf6da$da1c1ec0$45a87ca4@urimini.dacom.co.kr> NNTP-Posting-Host: 164.124.168.69 X-Newsreader: Microsoft Internet News 4.70.1155 Could anyone tell me what is type 1 and type 2 protein secretion systems? I cannot define these systems clearly. help me. thank you.