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
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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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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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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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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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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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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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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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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
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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
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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
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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
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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
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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
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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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