Aspergillus Nidulans in the CNS

Don Scott dscott at mcs.net
Mon Mar 3 14:45:12 EST 1997


Having chilkdren, grandchildren and greatgrandchildren, I empathize with
you.   I did a Medline search that turned up 16 possibly relevant
citations with abstracts, which I attach hereto.   I do not fully
understand it, but there seems to be some genetic similarity betqween
key genes in A. nidulans and brain tubulins.  Please look at some of
the  first abstracts but pay particular attentio to  record 8 reporting
a brain infection, and to record 13.    Antimitotic substances may work,
but the question is what they will do to the brain.  Furthermore they
may have to be directly introduced into the spinal fluid, and the
hazards of such action may not be known.

You may be, in part, a "victim" of the litigious nature of our society,
restricting the treating physicians from trying novel procedures.

Good luck.

Don

PLEASE HELP wrote:
> 
> PLEASE HELP
> 
> We are the parents of a nineteen month old Baby Boy with a life threatening
> disease.   To our knowledge this is the first case of a fungal infection of
> this type known anywhere in the world.   If you can provide any suggestions
> for helping our little Boy we would be most grateful.
> 
> Infection:  Aspergillus Nidulans in the Central Nervous System.   The
> fungus surrounds the base of the brain and is present in other locations on
> the covering of the meninges.   This was diagnosed following a biopsy taken
> from his lumbar region.   Biopsy was taken September 13, 1996.
> 
> Cause of Infection:  Unknown
> 
> Patient's Present condition:  Beginning to show signs of Hydrocephalus.
> Vomiting is becoming more frequent.  Febers and pain becoming more frequent
> and severe.   He is developing a little trouble walking.
> 
> Course of Treatment:   Begain treatment in September on Amphotericin B and
> 4 FC given by IV.   Treatment was determined to be unsuccessful.  After one
> month MRI showed disease had progressed.
> The next treatment was Amphotericin Liposomal given by IV and Oral
> Itraconazole.  An MRI taken one month after this treatment was started,
> appeared to show a slight reduction in the size of the fungal growths,
> however a followup MRI taken thirty days later showed the fungus was once
> again growing.   At this point the decision was made to put in a resevoir
> to administer Ampho B directly into his DSF.   On January 9, 1997 a second
> biopsy was taken from His spine.   The biopsy confirmed the fungus was
> Aspergillus, but the cultures would not grow so it could not be confirmed
> the fungus was Nidulans.
> An MRI taken February 3, 1997 has shown that the fungus increased in size
> considerably even with this treatment and there are new lesions.
> The therapy is now going to be couble the dose of Oral Itraconazole
> (10mg/kg) and the Itrathecal Amphotericin therapy has been discontinued.
> He is going to given Gamma Interferon sub-cutaneiously to boost immune
> function though no immune deficiency has ever been detected.   He had a
> negative result when tested for CGD.

-- 

"Nothing else matters much - not wealth, nor learning, nor even 
health - without this gift: the spiritual capacity to keep zest in
living."
                         Harry Emerson Fosdick
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 Record 1 of 16 in MEDLINE EXPRESS (R) 1991-1995

TITLE
     NudF, a nuclear migration gene in Aspergillus nidulans, is similar to
     the human LIS-1 gene required for neuronal migration.
AUTHOR(S)
     Xiang-X; Osmani-AH; Osmani-SA; Xin-M; Morris-NR
ADDRESS OF AUTHOR
     Department of Pharmacology, University of Medicine and Dentistry of New
     Jersey, Robert Wood Johnson Medical School, Piscataway 08854-5635, USA.
SOURCE (BIBLIOGRAPHIC CITATION)
     Mol-Biol-Cell. 1995 Mar; 6(3): 297-310
Library Holdings Message
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Call Number
     Price: $11.50 plus fax surcharge
INTERNATIONAL STANDARD SERIAL NUMBER
     1059-1524
PUBLICATION YEAR
     1995
LANGUAGE OF ARTICLE
     ENGLISH
COUNTRY OF PUBLICATION
     UNITED-STATES
ABSTRACT
     During a study of the genetics of nuclear migration in the filamentous
     fungus Aspergillus nidulans, we cloned a gene, nudF, which is required
     for nuclear migration during vegetative growth as well as development.
     The NUDF protein level is controlled by another protein NUDC, and extra
     copies of the nudF gene can suppress the nudC3 mutation. nudF encodes a
     protein with 42% sequence identity to the human LIS-1 (Miller-Dieker
     lissencephaly-1) gene, which is required for proper neuronal migration
     during brain development. This strong similarity suggests that the
     LIS-1 gene product may have a function similar to that of NUDF and
     supports previous findings to suggest that nuclear migration may play a
     role in neuronal migration.
MINOR MESH HEADINGS
     Amino-Acid-Sequence; Aspergillus-nidulans-growth-and-development;
     Aspergillus-nidulans-ultrastructure; Cell-Movement;
     Cell-Nucleus-physiology; Cell-Polarity; Fungal-Proteins-biosynthesis;
     Fungal-Proteins-physiology; Gene-Expression-Regulation,-Fungal;
     Molecular-Sequence-Data; Movement-; Proteins-chemistry;
     Sequence-Alignment; Sequence-Homology,-Amino-Acid
MAJOR MeSH HEADINGS
     *Aspergillus-nidulans-genetics; *Fungal-Proteins-genetics;
     *Genes,-Structural,-Fungal
CHECKTAGS
     Comparative-Study; Support,-U.S.-Gov't,-P.H.S.
GENE SYMBOL
     nudF; nudC; LIS-1; nud6; nud7; nudA
PUBLICATION TYPE
     JOURNAL-ARTICLE
CAS REGISTRY NUMBER OR EC NUMBER
     0; 0; 0; 0; 0
NAME OF SUBSTANCE
     Fungal-Proteins; LIS1-protein; NUDC-protein; NUDF-protein; Proteins
MEDLINE ACCESSION NUMBER
     95337460
UPDATE CODE
     9510
SECONDARY SOURCE IDENTIFIER
     GENBANK/U22009

----------------------------------------------------------------------------
 Record 2 of 16 in MEDLINE EXPRESS (R) 1991-1995

TITLE
     Purification and characterization of assembly-competent tubulin from
     Aspergillus nidulans.
AUTHOR(S)
     Yoon-Y; Oakley-BR
ADDRESS OF AUTHOR
     Department of Molecular Genetics, Ohio State University, Columbus
     43210, USA.
SOURCE (BIBLIOGRAPHIC CITATION)
     Biochemistry. 1995 May 16; 34(19): 6373-81
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Call Number
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INTERNATIONAL STANDARD SERIAL NUMBER
     0006-2960
PUBLICATION YEAR
     1995
LANGUAGE OF ARTICLE
     ENGLISH
COUNTRY OF PUBLICATION
     UNITED-STATES
ABSTRACT
     We have developed a procedure for purifying assembly-competent tubulin
     from Aspergillus nidulans. To our knowledge, this is the first report
     of the purification of assembly-competent tubulin from a filamentous
     fungus, and the procedure should be of great value in analyzing the
     large number of alpha- and beta-tubulin mutations that have been
     isolated and characterized in A. nidulans. Our procedure consists of
     overproduction of alpha- and beta-tubulin, partial purification by
     ion-exchange chromatography, and final purification by rounds of
     assembly and disassembly. We have found that taxol promotes the
     assembly of A. nidulans tubulin into microtubules, but a higher
     concentration of taxol is required for maximal assembly of A. nidulans
     tubulin than is required for brain tubulin. The critical concentration
     for assembly in the presence of taxol is also significantly higher for
     A. nidulans tubulin than for brain tubulin. In addition, A. nidulans
     microtubules that were assembled and maintained in the presence of
     taxol depolymerized in conditions in which taxol-stabilized mammalian
     microtubules remain intact. These results suggest that A. nidulans
     tubulin has a lower affinity for taxol than mammalian tubulin.
MINOR MESH HEADINGS
     Amino-Acid-Sequence; Cattle-;
     Fungal-Proteins-isolation-and-purification; Microscopy,-Electron;
     Molecular-Sequence-Data; Paclitaxel-pharmacology;
     Protein-Binding-drug-effects; Recombinant-Proteins; Sequence-Alignment;
     Sequence-Homology,-Amino-Acid; Tubulin-metabolism
MAJOR MeSH HEADINGS
     *Aspergillus-nidulans-chemistry; *Microtubules-chemistry;
     *Tubulin-isolation-and-purification
CHECKTAGS
     Animal; Comparative-Study; Support,-U.S.-Gov't,-Non-P.H.S.;
     Support,-U.S.-Gov't,-P.H.S.
GENE SYMBOL
     tubA; benA
PUBLICATION TYPE
     JOURNAL-ARTICLE
CONTRACT OR GRANT NUMBERS
     GM31837GMNIGMS
CAS REGISTRY NUMBER OR EC NUMBER
     0; 0; 0; 33069-62-4
NAME OF SUBSTANCE
     Fungal-Proteins; Recombinant-Proteins; Tubulin; Paclitaxel
MEDLINE ACCESSION NUMBER
     95275830
UPDATE CODE
     9509

----------------------------------------------------------------------------
 Record 3 of 16 in MEDLINE EXPRESS (R) 1991-1995

TITLE
     Cytoplasmic dynein is involved in nuclear migration in Aspergillus
     nidulans.
AUTHOR(S)
     Xiang-X; Beckwith-SM; Morris-NR
ADDRESS OF AUTHOR
     University of Medicine and Dentistry of New Jersey, Robert Wood Johnson
     Medical School, Department of Pharmacology, Piscataway 08854-5635.
SOURCE (BIBLIOGRAPHIC CITATION)
     Proc-Natl-Acad-Sci-U-S-A. 1994 Mar 15; 91(6): 2100-4
INTERNATIONAL STANDARD SERIAL NUMBER
     0027-8424
PUBLICATION YEAR
     1994
LANGUAGE OF ARTICLE
     ENGLISH
COUNTRY OF PUBLICATION
     UNITED-STATES
ABSTRACT
     Nuclear migration plays an important role in the growth and development
     of many organisms including the multinuclear fungus Aspergillus
     nidulans. We have identified four genes, nudA, nudC, nudF, and nudG, in
     which temperature-sensitive mutations affect nuclear distribution. In
     this report, we describe the cloning of the nudA gene by
     complementation of the mutant phenotype by using a chromosome
     VIII-specific cosmid library. A genomic fragment of nudA hybridized to
     an mRNA of approximately 14 kb. Sequencing analysis of nudA revealed
     four ATP-binding sites that are characteristic of the cytoplasmic
     dynein heavy chain. The amino acid sequence of the nudA gene product
     shows 52% overall identity with the rat brain cytoplasmic dynein heavy
     chain. Our study provides in vivo evidence that dynein, a microtubule
     motor molecule, plays a role in the nuclear migration process.
MINOR MESH HEADINGS
     Adenosine-Triphosphate-metabolism; Amino-Acid-Sequence;
     Aspergillus-nidulans-genetics; Cloning,-Molecular;
     Dynein-ATPase-metabolism; Genes,-Fungal; Genetic-Complementation-Test;
     Molecular-Sequence-Data; Mutation-; Phenotype-; Restriction-Mapping;
     Sequence-Homology,-Amino-Acid; Temperature-
MAJOR MeSH HEADINGS
     *Aspergillus-nidulans-growth-and-development; *Cell-Nucleus-metabolism;
     *Cytoplasm-metabolism; *Dynein-ATPase-genetics
CHECKTAGS
     Animal; Support,-U.S.-Gov't,-P.H.S.
GENE SYMBOL
     nudA; nudC; nudF; nudG
PUBLICATION TYPE
     JOURNAL-ARTICLE
CAS REGISTRY NUMBER OR EC NUMBER
     EC 3.6.1.33; 56-65-5
NAME OF SUBSTANCE
     Dynein-ATPase; Adenosine-Triphosphate
MEDLINE ACCESSION NUMBER
     94181539
UPDATE CODE
     9406
SECONDARY SOURCE IDENTIFIER
     GENBANK/U03904

----------------------------------------------------------------------------
 Record 4 of 16 in MEDLINE EXPRESS (R) 1991-1995

TITLE
     Binding selectivity of rhizoxin, phomopsin A, vinblastine, and
     ansamitocin P-3 to fungal tubulins: differential interactions of these
     antimitotic agents with brain and fungal tubulins [published erratum
     appears in Biochem Biophys Res Commun 1993 Feb 15;190(3):1180]
AUTHOR(S)
     Li-Y; Kobayashi-H; Hashimoto-Y; Iwasaki-S
ADDRESS OF AUTHOR
     Institute of Applied Microbiology, University of Tokyo, Japan.
SOURCE (BIBLIOGRAPHIC CITATION)
     Biochem-Biophys-Res-Commun. 1992 Sep 16; 187(2): 722-9
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Call Number
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INTERNATIONAL STANDARD SERIAL NUMBER
     0006-291X
PUBLICATION YEAR
     1992
LANGUAGE OF ARTICLE
     ENGLISH
COUNTRY OF PUBLICATION
     UNITED-STATES
ABSTRACT
     The binding of four potent antimitotic agents, rhizoxin (RZX),
     phomopsin A (PMS-A), ansamitocin P-3 (ASMP-3), and vinblastine (VLB),
     to tubulins from RZX-sensitive and -resistant strains of Aspergillus
     nidulans, Schizosaccharomyces pombe, and Saccharomyces cerevisiae was
     investigated. Mycelial extracts to which RZX could bind contained
     beta-tubulin with Asn as the 100th amino acid residue (Asn-100) in all
     cases, and those without affinity for RZX contained beta-tubulins with
     either Ile-100 or Val-100. Though PMS-A shares the same binding site as
     RZX and ASMP-3 on porcine brain tubulin (Asn-100), only ASMP-3 bound
     Asn-100 fungal tubulins in a competitive manner with respect to RZX.
     PMS-A and VLB, which strongly bind to porcine brain tubulin, did not
     bind to any of the fungal mycelial extracts examined. The results
     indicate differential interactions of these antimitotic agents with
     brain and fungal tubulins.
MINOR MESH HEADINGS
     Aspergillus-nidulans-metabolism; Binding-Sites; Binding,-Competitive;
     Brain-metabolism; Brain-Chemistry; Fungi-chemistry;
     Lactones-metabolism; Maytansine-analogs-and-derivatives;
     Maytansine-metabolism; Mycotoxins-metabolism;
     Saccharomyces-cerevisiae-metabolism; Schizosaccharomyces-metabolism;
     Swine-; Vinblastine-metabolism
MAJOR MeSH HEADINGS
     *Antineoplastic-Agents-metabolism; *Fungi-metabolism;
     *Tubulin-metabolism
CHECKTAGS
     Animal; Comparative-Study
PUBLICATION TYPE
     JOURNAL-ARTICLE
CAS REGISTRY NUMBER OR EC NUMBER
     0; 0; 0; 0; 35846-53-8; 64925-80-0; 69279-90-9; 865-21-4; 90996-54-6
NAME OF SUBSTANCE
     Antineoplastic-Agents; Lactones; Mycotoxins; Tubulin; Maytansine;
     phomopsin; ansamitocins; Vinblastine; rhizoxin
MEDLINE ACCESSION NUMBER
     92412113
UPDATE CODE
     9212

----------------------------------------------------------------------------
 Record 5 of 16 in MEDLINE EXPRESS (R) 1991-1995

TITLE
     Protein structure of pig liver 4-aminobutyrate aminotransferase and
     comparison with a cDNA-deduced sequence.
AUTHOR(S)
     De-Biase-D; Maras-B; Bossa-F; Barra-D; John-RA
ADDRESS OF AUTHOR
     Dipartimento di Scienze Biochimiche A. Rossi Fanelli, Universita La
     Sapienza, Roma, Italy.
SOURCE (BIBLIOGRAPHIC CITATION)
     Eur-J-Biochem. 1992 Sep 1; 208(2): 351-7
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Call Number
     Price: $16.75 plus fax surcharge
INTERNATIONAL STANDARD SERIAL NUMBER
     0014-2956
PUBLICATION YEAR
     1992
LANGUAGE OF ARTICLE
     ENGLISH
COUNTRY OF PUBLICATION
     GERMANY
ABSTRACT
     The amino acid sequence of pig liver 4-aminobutyrate aminotransferase
     has been determined by gas-phase sequencing of proteolytically derived
     peptide fragments. The sequence differs substantially from that
     predicted for the same enzyme on the basis of the sequence of cDNA
     derived from pig brain in recently published work [Kwon, O., Park, J. &
     Churchich, J. E. (1992) J. Biol. Chem. 267, 7215-7216]. Apart from a
     few minor differences, the two sequences are completely different in
     the segment of protein comprising the 36 residues at positions 107-142.
     Insertion of a cytosine between bases 402 and 403 in the cDNA sequence,
     together with deletion of the guanine at position 510, results in a DNA
     sequence which predicts exactly the amino acid sequence determined by
     peptide analysis in the present work. The mammalian enzyme has
     approximately 44% sequence identity with the same enzyme from two
     unicellular eukaryotes (Saccharomyces cerevisiae, Aspergillus nidulans)
     and 22% identity with that from Escherichia coli.
MINOR MESH HEADINGS
     Amino-Acid-Sequence; Aminobutyrate-Aminotransferase-genetics;
     Base-Sequence; Chromatography,-High-Pressure-Liquid;
     Molecular-Sequence-Data; Peptide-Fragments-chemistry;
     Sequence-Homology,-Nucleic-Acid;
     Spectrometry,-Mass,-Fast-Atom-Bombardment; Swine-; Trypsin-metabolism
MAJOR MeSH HEADINGS
     *Aminobutyrate-Aminotransferase-chemistry; *DNA-chemistry;
     *Liver-enzymology
CHECKTAGS
     Animal; Comparative-Study; Support,-Non-U.S.-Gov't
PUBLICATION TYPE
     JOURNAL-ARTICLE
CAS REGISTRY NUMBER OR EC NUMBER
     EC 2.6.1.19; EC 3.4.21.4; 0; 9007-49-2
NAME OF SUBSTANCE
     Aminobutyrate-Aminotransferase; Trypsin; Peptide-Fragments; DNA
MEDLINE ACCESSION NUMBER
     92394130
UPDATE CODE
     9212
SECONDARY SOURCE IDENTIFIER
     GENBANK/P80147

----------------------------------------------------------------------------
 Record 6 of 16 in MEDLINE EXPRESS (R) 1991-1995

TITLE
     Mutational analysis of calmodulin in Saccharomyces cerevisiae.
AUTHOR(S)
     Davis-TN
ADDRESS OF AUTHOR
     Department of Biochemistry, University of Washington, Seattle.
SOURCE (BIBLIOGRAPHIC CITATION)
     Cell-Calcium. 1992 Jun-Jul; 13(6-7): 435-44
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Call Number
     Price: $16.00 plus fax surcharge
INTERNATIONAL STANDARD SERIAL NUMBER
     0143-4160
PUBLICATION YEAR
     1992
LANGUAGE OF ARTICLE
     ENGLISH
COUNTRY OF PUBLICATION
     SCOTLAND
ABSTRACT
     Calmodulin is well characterized as an intracellular Ca2+ receptor in
     nonproliferating tissues such as muscle and brain. Several observations
     indicate that calmodulin is also required for cellular growth and
     division. Deletion of the calmodulin gene is a lethal mutation in
     Saccharomyces cerevisiae, Schizosaccharomyces pombe and Aspergillus
     nidulans. Expression of calmodulin antisense RNA in mouse C127 cells
     causes a transient arrest at G1 and metaphase. Although these results
     indicate calmodulin plays a critical function during proliferation,
     they do not reveal the function. S. cerevisiae offers an excellent
     system for identifying calmodulin functions. Because calmodulin mutants
     can be readily constructed by gene replacement the consequences of
     mutations in calmodulin can be directly examined in vivo without
     interference from wild-type calmodulin. The available wealth of
     information concerning all aspects of the yeast life cycle provides a
     large framework for interpretation of new results. The recent
     dissection of cell cycle regulation is just the latest example of the
     important insights provided by analyzing basic cellular processes in
     yeast. Whether studies of calmodulin in yeast will reveal a universal
     function is unknown. One encouraging result is that yeast cells relying
     on vertebrate calmodulin as their only source of calmodulin survive and
     grow well, even if the amount of vertebrate calmodulin is equivalent to
     the normal steady state levels of yeast calmodulin. This review
     discusses the varied techniques we are using to identify the functions
     of calmodulin in yeast. As part of the analysis, we are defining the
     essential elements of calmodulin structure.
MINOR MESH HEADINGS
     Calmodulin-genetics; Mutation-
MAJOR MeSH HEADINGS
     *Calmodulin-physiology; *Fungal-Proteins-genetics;
     *Saccharomyces-cerevisiae-physiology
PUBLICATION TYPE
     JOURNAL-ARTICLE; REVIEW; REVIEW,-TUTORIAL
CAS REGISTRY NUMBER OR EC NUMBER
     0; 0
NAME OF SUBSTANCE
     Calmodulin; Fungal-Proteins
MEDLINE ACCESSION NUMBER
     92370658
UPDATE CODE
     9211

----------------------------------------------------------------------------
 Record 7 of 16 in MEDLINE EXPRESS (R) 1991-1995

TITLE
     Cloning and sequence determination of a cDNA encoding Aspergillus
     nidulans calmodulin-dependent multifunctional protein kinase.
AUTHOR(S)
     Kornstein-LB; Gaiso-ML; Hammell-RL; Bartelt-DC
ADDRESS OF AUTHOR
     Department of Biological Sciences, St. John's University Jamaica, NY
     11439.
SOURCE (BIBLIOGRAPHIC CITATION)
     Gene. 1992 Apr 1; 113(1): 75-82
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Call Number
     Price: $23.50 plus fax surcharge
INTERNATIONAL STANDARD SERIAL NUMBER
     0378-1119
PUBLICATION YEAR
     1992
LANGUAGE OF ARTICLE
     ENGLISH
COUNTRY OF PUBLICATION
     NETHERLANDS
ABSTRACT
     A partial cDNA encoding Aspergillus nidulans calmodulin-dependent
     multifunctional protein kinase (ACMPK) was isolated from a lambda ZAP
     expression library by immunoselection using monospecific polyclonal
     antibodies to the enzyme. The sequence of both strands of the cDNA
     (CMKa) was determined. The deduced amino acid (aa) sequence contained
     all eleven consensus domains found in serine/threonine protein kinases
     [Hanks et al., Science 241 (1988) 42-52], as well as a putative
     calmodulin-binding domain. The cDNA contained an intron, lacked an
     in-frame start codon, and was not polyadenylated. A full-length copy of
     CMKa was subsequently isolated from a lambda gt10 library of A.
     nidulans cDNA using a restriction fragment of the first clone as a
     probe. It contained an in-frame start codon, an open reading frame
     (ORF) of 1242 bp and was polyadenylated. The ORF encoded a protein of
     414 aa residues with an M(r) of 46,895 and an isoelectric point pI =
     6.4. These values are in good agreement with that observed for the
     native enzyme [Bartelt et al., Proc. Natl. Acad. Sci. USA 85 (1988)
     3279-3283]. When aligned to optimize homology, 29% of the predicted aa
     sequence of ACMPK is identical to that of the alpha-subunit of rat
     brain calmodulin-dependent protein kinase II. ACMPK shares 40 and 44%
     identity in aa sequence with YCMK1 and YCMK2, respectively, two
     Ca2+/calmodulin-dependent protein kinases recently cloned from
     Saccharomyces cerevisiae [Pausch et al., EMBO J. 10 (1991) 1511-1522].
     Results of Southern analysis of restriction digests of genomic DNA
     indicate that ACMPK is encoded by a single-copy gene.
MINOR MESH HEADINGS
     Amino-Acid-Sequence; Aspergillus-nidulans-enzymology; Base-Sequence;
     Cloning,-Molecular-methods; DNA,-Fungal-isolation-and-purification;
     Gene-Library; Immunoassay-; Introns-; Molecular-Sequence-Data;
     Oligodeoxyribonucleotides-; Phosphorylation-; Protein-Kinases-analysis;
     Restriction-Mapping; Sequence-Homology,-Nucleic-Acid
MAJOR MeSH HEADINGS
     *Aspergillus-nidulans-genetics; *DNA,-Fungal-genetics;
     *Protein-Kinases-genetics
CHECKTAGS
     Comparative-Study; Support,-Non-U.S.-Gov't; Support,-U.S.-Gov't,-P.H.S.
PUBLICATION TYPE
     JOURNAL-ARTICLE
CONTRACT OR GRANT NUMBERS
     GM37288GMNIGMS
CAS REGISTRY NUMBER OR EC NUMBER
     EC 2.7.1.-; EC 2.7.1.37; 0; 0
NAME OF SUBSTANCE
     calmodulin-dependent-multiprotein-kinase; Protein-Kinases; DNA,-Fungal;
     Oligodeoxyribonucleotides
MEDLINE ACCESSION NUMBER
     92225350
UPDATE CODE
     9207
SECONDARY SOURCE IDENTIFIER
     GENBANK/M74120; GENBANK/X58742; GENBANK/X58743; GENBANK/M76682;
     GENBANK/X60732; GENBANK/X60733; GENBANK/M79307; GENBANK/M79308;
     GENBANK/M79309; GENBANK/M79310

----------------------------------------------------------------------------
 Record 8 of 16 in MEDLINE EXPRESS (R) 1990

TITLE
     A case of cerebral aspergillosis caused by Aspergillus nidulans.
     Clinical, pathologic and mycologic identifications.
AUTHOR(S)
     Tong-QJ; Chai-WX; Wang-ZF; Kou-JF; Qi-ZT; Wang-DL
ADDRESS OF AUTHOR
     Department of Neurology, Beijing Friendship Hospital.
SOURCE (BIBLIOGRAPHIC CITATION)
     Chin-Med-J-Engl. 1990 Jun; 103(6): 518-22
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Call Number
     Price: $23.50 plus fax surcharge
INTERNATIONAL STANDARD SERIAL NUMBER
     0366-6999
PUBLICATION YEAR
     1990
LANGUAGE OF ARTICLE
     ENGLISH
COUNTRY OF PUBLICATION
     CHINA
ABSTRACT
     A case of cerebral aspergillosis is reported, the presenting symptom
     was numbness of right face, which worsened after one year. CT-scan
     showed two enhanced low-density patches in the anterior and basal parts
     of right temporal lobe. During operation, an abscess in the deep part
     of right temporal lobe was revealed. The patient gradually felt
     amaurosis and oculomotor palsy of right eye. About six months later,
     she died from intracranial hypertension. Biopsy, as well as autopsy
     findings suggested fungal infection, and was identified as Aspergillus
     nidulans, which has probably never been reported in the literature.
MINOR MESH HEADINGS
     Aspergillus-nidulans-isolation-and-purification;
     Brain-Abscess-etiology; Brain-Abscess-microbiology; Middle-Age
MAJOR MeSH HEADINGS
     *Aspergillosis-; *Aspergillus-nidulans; *Brain-Abscess-pathology
CHECKTAGS
     Case-Report; Female; Human
PUBLICATION TYPE
     JOURNAL-ARTICLE; REVIEW; REVIEW-OF-REPORTED-CASES
MEDLINE ACCESSION NUMBER
     91005486
UPDATE CODE
     9101

----------------------------------------------------------------------------
 Record 9 of 16 in MEDLINE EXPRESS (R) 1990

TITLE
     Chloroacetaldehyde is a powerful inducer of mitotic aneuploidy in
     Aspergillus nidulans.
AUTHOR(S)
     Crebelli-R; Conti-G; Conti-L; Carere-A
ADDRESS OF AUTHOR
     Istituto Superiore di Sanita, Rome, Italy.
SOURCE (BIBLIOGRAPHIC CITATION)
     Mutagenesis. 1990 Mar; 5(2): 165-8
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Call Number
     Price: $13.50 plus fax surcharge
INTERNATIONAL STANDARD SERIAL NUMBER
     0267-8357
PUBLICATION YEAR
     1990
LANGUAGE OF ARTICLE
     ENGLISH
COUNTRY OF PUBLICATION
     ENGLAND
ABSTRACT
     The vinyl chloride metabolite chloroacetaldehyde (CAA) was tested for
     the induction of mitotic chromosome malsegregation in Aspergillus
     nidulans. Exposure of germinating conidia to CAA (16-64 microM)
     produced high rates of abnormal colonies with segregation of the whole
     first chromosome in the diploid strain P1, and abnormal, putative
     hyperploids in the haploid strain 35, indicating that CAA primarily
     induces abnormal chromosome segregation. Comparative assays with the
     known spindle poison chloral hydrate (CH), active in the dose range
     6-10 mM, highlighted the unusual effectiveness of CAA in aneuploidy
     induction (the lowest effective concentration was 16 microM).
     Experiments on brain tubulin polymerization revealed an inhibitory
     effect by CAA only at concentrations 100-fold higher than those active
     in the induction of chromosome misdistribution in A. nidulans, possibly
     suggesting the involvement of alternative targets in its mechanism of
     action.
MINOR MESH HEADINGS
     Acetaldehyde-toxicity; Aspergillus-nidulans-genetics; Cattle-;
     Crossing-Over-Genetics-drug-effects; Microtubules-drug-effects
MAJOR MeSH HEADINGS
     *Acetaldehyde-analogs-and-derivatives; *Aneuploidy-;
     *Aspergillus-nidulans-drug-effects; *Chromosomes,-Fungal-drug-effects;
     *Mutagens-
CHECKTAGS
     Animal; In-Vitro; Support,-Non-U.S.-Gov't
PUBLICATION TYPE
     JOURNAL-ARTICLE
CAS REGISTRY NUMBER OR EC NUMBER
     0; 107-20-0; 75-07-0
NAME OF SUBSTANCE
     Mutagens; chloroacetaldehyde; Acetaldehyde
MEDLINE ACCESSION NUMBER
     90258753
UPDATE CODE
     9008

----------------------------------------------------------------------------
 Record 10 of 16 in MEDLINE EXPRESS (R) 1983-1989

TITLE
     Rhizoxin resistant mutants with an altered beta-tubulin gene in
     Aspergillus nidulans.
AUTHOR(S)
     Takahashi-M; Kobayashi-H; Iwasaki-S
ADDRESS OF AUTHOR
     Institute of Applied Microbiology, University of Tokyo, Japan.
SOURCE (BIBLIOGRAPHIC CITATION)
     Mol-Gen-Genet. 1989 Dec; 220(1): 53-9
Library Holdings Message
     Press  to receive the full text via fax.
Call Number
     Price: $16.50 plus fax surcharge
INTERNATIONAL STANDARD SERIAL NUMBER
     0026-8925
PUBLICATION YEAR
     1989
LANGUAGE OF ARTICLE
     ENGLISH
COUNTRY OF PUBLICATION
     GERMANY,-WEST
ABSTRACT
     Rhizoxin and ansamitocin P-3 (a maytansinoid compound), potent
     inhibitors of mammalian brain tubulin assembly, inhibit growth of a
     variety of fungi including Aspergillus nidulans. Mutants of A.
     nidulans, benA10 which is a benomyl resistant beta-tubulin gene mutant
     and tubA1 which is a benomyl supersensitive alpha-tubulin gene mutant,
     were both sensitive to rhizoxin and ansamitocin P-3 to the same extent
     as wild-type strains. We isolated 18 rhizoxin resistant mutants of A.
     nidulans. All of these mutants were cross-resistant to ansamitocin P-3,
     but not to benzimidazole antimitotic drugs. These mutants mapped to two
     loci, rhiA and rhiB, and all of those with high resistance mapped to
     rhiA. The fact that the protein extracts of rhiA mutants lost rhizoxin
     binding affinity and that rhiA was closely linked to benA, the major
     beta-tubulin gene in A. nidulans, indicated that rhiA must be a
     structural gene for beta-tubulin and that rhiA mutants are a new class
     of beta-tubulin gene mutants. All of this suggested that, in A.
     nidulans, these antimitotic drugs bind to beta-tubulin, and that
     rhizoxin and ansamitocin P-3 share the same binding site but the site
     does not overlap with the benzimidazole binding site. Protein extracts
     from a rhiB mutant retained rhizoxin binding affinity, therefore this
     rhizoxin resistance mechanism should not be a tubulin mediated process.
MINOR MESH HEADINGS
     Aspergillus-nidulans-drug-effects;
     Aspergillus-nidulans-growth-and-development;
     Benomyl-administration-and-dosage; Benomyl-pharmacology;
     Benzimidazoles-administration-and-dosage; Benzimidazoles-pharmacology;
     Cell-Division-drug-effects; Dose-Response-Relationship,-Drug;
     Drug-Resistance,-Microbial-genetics;
     Lactones-administration-and-dosage; Lactones-pharmacology;
     Lactones-pharmacokinetics
MAJOR MeSH HEADINGS
     *Antibiotics,-Antifungal-pharmacology; *Aspergillus-nidulans-genetics;
     *Genes,-Fungal; *Mutation-; *Tubulin-genetics
CHECKTAGS
     Support,-Non-U.S.-Gov't
PUBLICATION TYPE
     JOURNAL-ARTICLE
CAS REGISTRY NUMBER OR EC NUMBER
     0; 0; 0; 0; 17804-35-2; 51-17-2; 90996-54-6
NAME OF SUBSTANCE
     Antibiotics,-Antifungal; Benzimidazoles; Lactones; Tubulin; Benomyl;
     benzimidazole; rhizoxin
MEDLINE ACCESSION NUMBER
     90114108
UPDATE CODE
     9004

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 Record 11 of 16 in MEDLINE EXPRESS (R) 1983-1989

TITLE
     Calmodulin-dependent multifunctional protein kinase in Aspergillus
     nidulans.
AUTHOR(S)
     Bartelt-DC; Fidel-S; Farber-LH; Wolff-DJ; Hammell-RL
ADDRESS OF AUTHOR
     Department of Pharmacology, University of Medicine and Dentistry of New
     Jersey, Robert Wood Johnson Medical School, Piscataway 08854.
SOURCE (BIBLIOGRAPHIC CITATION)
     Proc-Natl-Acad-Sci-U-S-A. 1988 May; 85(10): 3279-83
INTERNATIONAL STANDARD SERIAL NUMBER
     0027-8424
PUBLICATION YEAR
     1988
LANGUAGE OF ARTICLE
     ENGLISH
COUNTRY OF PUBLICATION
     UNITED-STATES
ABSTRACT
     A Ca2+/calmodulin (CaM)-dependent multifunctional protein kinase has
     been isolated from Aspergillus nidulans and purified to homogeneity.
     Unlike any CaM-dependent multifunctional protein kinase described
     previously, the native enzyme from Aspergillus behaves as a monomer.
     The calculated molecular weight is 41,200. NaDodSO4/PAGE reveals a
     single protein band with an apparent Mr of 51,000. Two-dimensional
     isoelectric focusing/NaDodSO4/PAGE of the purified enzyme showed one
     major and one minor more acidic Coomassie blue-stained spot, both of
     which bind 125I-labeled calmodulin in a calcium-dependent manner. The
     kinase is autophosphorylated in a calcium- and CaM-dependent manner,
     yielding an increase in the amount and number of more acidic forms of
     the enzyme. The Aspergillus kinase catalyzes the Ca2+/CaM-dependent
     phosphorylation of known substrates of type II Ca2+/CaM-dependent
     protein kinases, including glycogen synthase, microtubule-associated
     protein 2, synapsin, tubulin, gizzard myosin light chain, and casein.
     Cross-reactivity between antiserum raised against native rat brain
     protein kinase II and 125I-labeled Aspergillus kinase has been
     detected. Two forms of CaM have been isolated from Aspergillus
     nidulans, both of which activate the Aspergillus kinase at lower
     concentrations than that required for activation by bovine brain CaM.
MINOR MESH HEADINGS
     Brain-enzymology; Kinetics-; Molecular-Weight;
     Protein-Kinases-isolation-and-purification; Rats-;
     Substrate-Specificity
MAJOR MeSH HEADINGS
     *Aspergillus-niger-enzymology; *Protein-Kinases-metabolism
CHECKTAGS
     Animal; Comparative-Study; Support,-Non-U.S.-Gov't;
     Support,-U.S.-Gov't,-P.H.S.
PUBLICATION TYPE
     JOURNAL-ARTICLE
CONTRACT OR GRANT NUMBERS
     GM37288; NS11252; GM34711
CAS REGISTRY NUMBER OR EC NUMBER
     EC 2.7.1.37; EC 2.7.10.-
NAME OF SUBSTANCE
     Protein-Kinases; Calmodulin-Dependent-Protein-Kinases
MEDLINE ACCESSION NUMBER
     88217884
UPDATE CODE
     8808

----------------------------------------------------------------------------
 Record 12 of 16 in MEDLINE EXPRESS (R) 1983-1989

TITLE
     An evaluation of the mutagenic, carcinogenic and teratogenic potential
     of microwaves.
AUTHOR(S)
     Leonard-A; Berteaud-AJ; Bruyere-A
SOURCE (BIBLIOGRAPHIC CITATION)
     Mutat-Res. 1983 Sep; 123(1): 31-46
Library Holdings Message
     Press  to receive the full text via fax.
Call Number
     Price: $23.50 plus fax surcharge
INTERNATIONAL STANDARD SERIAL NUMBER
     0027-5107
PUBLICATION YEAR
     1983
LANGUAGE OF ARTICLE
     ENGLISH
COUNTRY OF PUBLICATION
     NETHERLANDS
ABSTRACT
     A notable proportion of the population is exposed to an increasing
     number of devices emitting microwaves, a form of non-ionizing
     electromagnetic radiation in the range 300-30000 mHz. The activation
     energy of microwave radiations is too small to directly modify any
     chemical bonds in the irradiated matter. At microwave frequencies the
     macroscopic dielectric properties of tissues are strongly determined by
     their water content. Tissues like muscle, brain, skin, with a high
     water content, have higher permittivity and conductivity values than
     bone or fat with low water contents. Owing to the energy transfer, to
     living tissues, by a dipolar relaxation mechanism of water molecules,
     the penetration of microwaves is limited and one observes a fast and
     very efficient heat-loss production. A review of the available
     literature shows that most results on the mutagenicity of microwaves
     are negative or can often be explained by a temperature enhancement. If
     microwaves are apparently unable to damage DNA at sub-thermal exposure
     levels, some results indicate, however, that they might easily
     potentiate the damaging action of other DNA antagonist agents such as
     UV or chemicals.
MINOR MESH HEADINGS
     Aspergillus-nidulans-genetics; Cells,-Cultured; Chromosome-Aberrations;
     Drosophila-melanogaster-genetics; Lymphocytes-physiology;
     Lymphocytes-radiation-effects; Plants-genetics;
     Saccharomyces-cerevisiae-genetics; Species-Specificity
MAJOR MeSH HEADINGS
     *Abnormalities-etiology; *Microwaves-adverse-effects; *Mutation-;
     *Neoplasms-etiology
CHECKTAGS
     Animal; Human; Support,-Non-U.S.-Gov't
PUBLICATION TYPE
     JOURNAL-ARTICLE
MEDLINE ACCESSION NUMBER
     83297468
UPDATE CODE
     8312

----------------------------------------------------------------------------
 Record 13 of 16 in MEDLINE EXPRESS (R) 1966-1982

TITLE
     Enhancement of tissue invasion in murine aspergillosis by systemic
     administration of suspensions of killed Corynebacterium parvum.
AUTHOR(S)
     Purnell-DM
SOURCE (BIBLIOGRAPHIC CITATION)
     Am-J-Pathol. 1976 Jun; 83(3): 547-55
Library Holdings Message
     0002-9440 11 The American Journal of Pathology web site:
     http://www.at-home.com/PATHOLOGY/
INTERNATIONAL STANDARD SERIAL NUMBER
     0002-9440
PUBLICATION YEAR
     1976
LANGUAGE OF ARTICLE
     ENGLISH
COUNTRY OF PUBLICATION
     UNITED-STATES
ABSTRACT
     The effect of killed Corynebacterium parvum vaccine on the course of
     murine aspergillosis is described. A grid-counting technique was
     employed to quantitate tissue invasion by Aspergillus nidulans in the
     brain, heart, and kidneys (the target organs) of normal mice and of
     mice treated systemically with killed C. parvum vaccine. Simultaneous
     treatment of mice with C. parvum and A. nidulans significantly
     increased the mortality rate, in contrast to treatment of mice with C.
     parvum prior to or following A. nidulans, which had no significant
     effect on mortality. Fungal invasion of the tissues of the brain and
     kidneys was significantly increased in mice pretreated or posttreated
     with C. parvum, but fungal invasion of the heart was not effected by
     these treatements. Simultaneous treatment of mice with C. parvum and A.
     nidulans significantly increased fungal invasion of the heart but did
     not effect tissue invasion of the brain and kidneys. It was concluded
     that killed C. parvum vaccine reduces host resistance to Aspergillus
     infection and facilitates the curse of fatal murine aspergillosis.
     These results suggest further caution in applying systemic C. parvum in
     the therapy of human neoplasia.
MINOR MESH HEADINGS
     Aspergillosis-microbiology; Aspergillosis-therapy;
     Aspergillus-nidulans; Bacterial-Vaccines-therapeutic-use; Mice-;
     Mice,-Inbred-DBA
MAJOR MeSH HEADINGS
     *Aspergillosis-pathology; *Disease-Models,-Animal;
     *Propionibacterium-acnes
CHECKTAGS
     Animal; Male
PUBLICATION TYPE
     JOURNAL-ARTICLE
MEDLINE ACCESSION NUMBER
     76229156
UPDATE CODE
     7610
SUBSET
     AIM

----------------------------------------------------------------------------
 Record 14 of 16 in MEDLINE EXPRESS (R) 1966-1982

TITLE
     Tubulin-like protein from Aspergillus nidulans.
AUTHOR(S)
     Sheir-Neiss-G; Nardi-RV; Gealt-MA; Morris-NR
SOURCE (BIBLIOGRAPHIC CITATION)
     Biochem-Biophys-Res-Commun. 1976 Mar 22; 69(2): 285-90
Library Holdings Message
     Press  to receive the full text via fax.
Call Number
     Price: $26.75 plus fax surcharge
INTERNATIONAL STANDARD SERIAL NUMBER
     0006-291X
PUBLICATION YEAR
     1976
LANGUAGE OF ARTICLE
     ENGLISH
COUNTRY OF PUBLICATION
     UNITED-STATES
MINOR MESH HEADINGS
     Brain-Chemistry; Chickens-; Electrophoresis,-Polyacrylamide-Gel;
     Species-Specificity; Swine-
MAJOR MeSH HEADINGS
     *Aspergillus-nidulans-metabolism;
     *Glycoproteins-isolation-and-purification;
     *Tubulin-isolation-and-purification
CHECKTAGS
     Animal; Comparative-Study; Support,-U.S.-Gov't,-Non-P.H.S.;
     Support,-U.S.-Gov't,-P.H.S.
PUBLICATION TYPE
     JOURNAL-ARTICLE
MEDLINE ACCESSION NUMBER
     76184115
UPDATE CODE
     7608

----------------------------------------------------------------------------
 Record 15 of 16 in MEDLINE EXPRESS (R) 1966-1982

TITLE
     Quantitative tissue invasion of the murine brain as a phenotypic marker
     of strain virulence in Aspergillus nidulans.
AUTHOR(S)
     Purnell-DM
SOURCE (BIBLIOGRAPHIC CITATION)
     Sabouraudia. 1975 Jul; 13(2): 209-16
INTERNATIONAL STANDARD SERIAL NUMBER
     0036-2174
PUBLICATION YEAR
     1975
LANGUAGE OF ARTICLE
     ENGLISH
COUNTRY OF PUBLICATION
     SCOTLAND
ABSTRACT
     In this study the extent of fungal invasion in tissues of the target
     organs (brain, heart and kidney) has been quantitated histologically in
     DBA/2J mice inoculated intravenously with 3 strains of Aspergillus
     nidulans of different virulence. This was done to determine the
     relation between tissue invasion and strain virulence as determined by
     time-mortality bioassay. It was found that quantitatively tissue
     invasion by A. nidulans was target organ specific. Relative tissue
     invasion within each of the tissues examined was dependent on the
     strain of A. nidulans injected. In the brain a direct relationship
     between strain virulence and the extent of tissue invasion was found.
     This relationship was not observed in the other 2 target organs. The
     observations suggest that an important phenotypic marker of murine
     virulence in A. nidulans is the relative ability to invade the tissues
     of the murine brain.
MINOR MESH HEADINGS
     Aspergillosis-mortality; Heart-microbiology; Kidney-microbiology;
     Mice-; Mice,-Inbred-Strains; Phenotype-; Virulence-
MAJOR MeSH HEADINGS
     *Aspergillosis-microbiology; *Aspergillus-nidulans-pathogenicity;
     *Brain-microbiology
CHECKTAGS
     Animal; Male
PUBLICATION TYPE
     JOURNAL-ARTICLE
MEDLINE ACCESSION NUMBER
     76013697
UPDATE CODE
     7601

----------------------------------------------------------------------------
 Record 16 of 16 in MEDLINE EXPRESS (R) 1966-1982

TITLE
     The histopathologic response of mice to Aspergillus nidulans:
     comparison between genetically defined haploid and diploid strains of
     different virulence.
AUTHOR(S)
     Purnell-DM
SOURCE (BIBLIOGRAPHIC CITATION)
     Drugs. 1974; 7(1): 95-104
Library Holdings Message
     Press  to receive the full text via fax.
Call Number
     Price: $28.50 plus fax surcharge
INTERNATIONAL STANDARD SERIAL NUMBER
     0012-6667
PUBLICATION YEAR
     1974
LANGUAGE OF ARTICLE
     ENGLISH
COUNTRY OF PUBLICATION
     SWITZERLAND
MINOR MESH HEADINGS
     Aspergillosis-microbiology;
     Aspergillus-nidulans-isolation-and-purification; Brain-pathology;
     Injections,-Intravenous; Kidney-pathology; Lethal-Dose-50;
     Liver-pathology; Lung-pathology; Mice-; Mice,-Inbred-DBA;
     Myocardium-pathology; Spores,-Fungal
MAJOR MeSH HEADINGS
     *Aspergillosis-pathology; *Aspergillus-nidulans-pathogenicity;
     *Diploidy-; *Haploidy-; *Virulence-
CHECKTAGS
     Animal; Comparative-Study; Male
PUBLICATION TYPE
     JOURNAL-ARTICLE
MEDLINE ACCESSION NUMBER
     74270264
UPDATE CODE
     7410

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