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  • 1995-1999  (6)
  • Key wordsNeurospora crassa  (4)
  • Apoptosis  (1)
  • Calcium efflux  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Induction of apoptotic cell death in rat thymus and spleen after a bolus injection of methamphetamine (1996)
    Springer
    International journal of legal medicine 109 (1996), S. 23-28 
    Details
    ISSN: 1437-1596
    Keywords: Apoptosis ; Methamphetamine ; Lymphocytes ; Thymus ; Spleen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine , Law
    Notes: Abstract We examined whether methamphetamine (MAP) induced apoptotic cell death in vivo. Male Wistar rats were injected intraperitoneally with 25 mg MAP/Kg body weight and were sacrificed at 4, 8 and 24 h. As early as 4 h after a single dose of MAP, DNA ladder bands representing DNA fragmentation into multiples of the internucleosomal DNA length of about 180 by were observed by gel electrophoresis in thymic and splenic DNA. DNA from control rats injected with 1 ml physiological saline/Kg body weight showed no ladder band patterns. The proportion of fragmented DNA from the thymus increased in a time-dependent manner up to 8 h and faint ladder band patterns were observed at 24 h, indicating that cell death via apoptosis occurred at an early stage and then apoptotic bodies were scavenged. DNA fragmentation in the thymus and spleen induced with MAP was also confirmed by the terminal deoxynucleotidyl transferase-mediated dUTPbiotin nick end labeling (TUNEL) method in situ. In control thymus samples, stained cells were numerous in the cortex but sparse in the medulla. At the boundary area between the cortex and medulla, stained cells were seen as a layer. In the MAP-treated rats, stained cells were increased and dispersed equally in the cortex and medulla. In control spleen samples, stained cells were numerous in all areas excluding the germinal centers. Cells at the germinal centers were stained intensively in MAP-treated rat spleen. Light microscopical analyses allowed us to identify lymphocytes during the course of apoptotic cell death. Electron microscopic studies showed morphological landmarks for the process of cellular apoptosis in both organs e.g. lymphocytes with chromatin condensed into crescents at the periphery of the nuclei and apoptotic bodies. These results indicate that MAP induced cell death of the thymic and splenic lymphocytes via apoptosis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01369597
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Senescence marker protein-30 (SMP30) enhances the calcium efflux from renal tubular epithelial cells (1999)
    Springer
    Clinical and experimental nephrology 3 (1999), S. 261-267 
    Details
    ISSN: 1437-7799
    Keywords: Key words SMP30 ; Calcium efflux ; Tubular epithelia ; Calcium pump ; Calmodulin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Background. Senescence marker protein-30 (SMP30), a calcium binding protein, is preferentially expressed in the renal proximal tubules and hepatocytes and is presumed to play a role in Ca2+ homeostasis. Methods. To explore its physiological functions in the tubular cells, we investigated the effect of SMP30 on Ca2+ efflux via the ATP-dependent plasma membrane calcium pump. LLC-PK1 cells were stably transfected with a cDNA encoding SMP30, and the established transfectants were subjected to ATP responses. Results. Overexpression of SMP30 significantly increased Ca2+ efflux under both basal and ATP-stimulated conditions. Inhibition of calmodulin by trifluoperazine abrogated the enhanced Ca2+ efflux, suggesting that SMP30 activated the calmodulin-dependent Ca2+ pump. It is known that Ca2+ superfluous influx induces cellular injury. Compared with mock-transfected cells, LLC-PK1 cells expressing SMP30 showed resistance to cellular death triggered by Ca2+ superfluous influx. Conclusion. These results suggest the possibility that, in renal tubular cells, endogenous SMP30 participates in Ca2+ efflux via activating the calmodulin-dependent Ca2+ pump and thereby confers resistance of the cells against injury caused by high intracellular Ca2+ concentrations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s101570050045
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  • 3
    Electronic Resource
    Electronic Resource
    Cloning and characterization of the yeast RAD1 homolog gene (mus-38) from Neurospora crassa: evidence for involvement in nucleotide excision repair (1998)
    Springer
    Current genetics 33 (1998), S. 276-283 
    Details
    ISSN: 1432-0983
    Keywords: Key wordsNeurospora crassa ; Nucleotide excision repair ; mus-38 ; RAD1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A Neurospora crassa gene encoding a product with homology to the Saccharomyces cerevisiae Rad1 nucleotide excision repair (NER) protein was isolated by degenerate PCR. The predicted protein consists of 892 amino acids with a molecular weight of 100.4 kDa, and 32–37% identity to the XPF/ERCC4 protein family. The homolog was mapped to the left arm of linkage group I, the location of the mus-38 gene. Subsequently, gene inactivation and complementation studies identified the RAD1 homolog as mus-38. Immunological assays showed that the mus-18 (UV-specific endonuclease) and mus-38 strains have partial and normal UV-damage excision activities, respectively, but removal of thymine dimers and TC (6-4) photoproducts is abolished in the mus-18 mus-38 double mutant. The double mutant also was synergistically more sensitive to UV than either single mutant. The data suggest that mus-38 may participate in a different NER pathway from that involving the mus-18 gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050337
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  • 4
    Electronic Resource
    Electronic Resource
    The mus-8 gene of Neurospora crassa encodes a structural and functional homolog of the Rad6 protein of Saccharomyces cerevisiae (1996)
    Springer
    Current genetics 30 (1996), S. 224-231 
    Details
    ISSN: 1432-0983
    Keywords: Key wordsNeurospora crassa ; mus-8 ; Rad6 ; Post-replication repair
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We cloned a DNA repair gene, mus-8, of Neurospora crassa and sequenced the genomic DNA and cDNA. Nucleotide-sequence analysis indicated that the mus-8 gene contains an open reading frame (ORF) of 456 bp, interrupted by three small introns. The deduced amino-acid sequence showed that the mus-8 gene encodes a 17 kDa protein which has 77.5% and 83.3% identity to the Rad6 protein of Saccharomyces cerevisiae and the rhp6+ protein of Schizosaccharomyces pombe, respectively. The Rad6 protein is a ubiquitin-conjugating enzyme (E2) and is required for DNA repair, mutagenesis, and sporulation in yeast. Introduction of the mus-8 gene into a S. cerevisiae rad6 mutant resulted in significant recovery of DNA repair functions, especially UV-mutagenesis, and also sporulation, both of which are defective in the rad6 mutant. It is therefore postulated that mus-8 of Neurospora has a function very similar to that demonstrated for RAD6 of S. cerevisiae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050125
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  • 5
    Electronic Resource
    Electronic Resource
    Isolation and characterization of the krev-1 gene, a novel member of ras superfamily in Neurospora crassa: involvement in sexual cycle progression (1997)
    Springer
    Molecular genetics and genomics 255 (1997), S. 429-437 
    Details
    ISSN: 1617-4623
    Keywords: Key wordsNeurospora crassa ; ras superfamily ; krev-1 ; Krev-1/rap1A/smg21A
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Genes belonging to the ras superfamily encode low-molecular-weight GTP/GDP-binding proteins that are highly conserved in wide variety of organisms. We used the polymerase chain reaction (PCR) to isolate a novel member of the ras superfamily from the filamentous fungus Neurospora crassa and obtained a mammalian Krev-1 homolog. We named the gene krev-1 and analyzed its structure and function. The krev-1 gene encodes a polypeptide of 225 amino acids, which is nearly 60% homologous to the mammalian Krev-1 p21. The krev-1 gene product (KREV1) is functionally analogous to mammalian Krev-1 p21 and Rsr1p/Bud1p, a Krev-1 homolog from the yeast Saccharomyces cerevisiae. GAL1-driven expression of KREV1 in a wild-type yeast strain resulted in a random budding pattern, as did its mammalian counterpart Krev-1 p21. We disrupted the krev-1 gene by RIP (repeat-induced point mutation), but the krev-1 disruptants showed no abnormalities. By in vitro mutagenesis, we constructed several mutant krev-1 genes (G21V, A68T, and D128A) which mimic constitutively active mutants of Ha-ras, and the krev-1 (K25N) mutant which is analogous to a dominant-negative mutant of Ha-ras. Each mutant gene was introduced into the wild-type strain and the phenotypes were analyzed. We could not observe any difference in vegetative growth between these transformants. When each strain was used as the female in mating tests, the development of perithecia from protoperithecia was inhibited in all cases. The results indicate that the krev-1 gene may be involved in sexual cycle progression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050515
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  • 6
    Electronic Resource
    Electronic Resource
    Genetic and molecular characterization of Neurospora crassamus-23 :a gene involved in recombinational repair (1997)
    Springer
    Molecular genetics and genomics 256 (1997), S. 436-445 
    Details
    ISSN: 1617-4623
    Keywords: Key wordsNeurospora crassa ; mus-23 ; MRE11 ; Recombinational repair ; Histidine sensitivity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A newly isolated mutant, mus-23, of Neurosporacrassa was found to be highly sensitive to a wide variety of mutagens, including UV light, methyl methanesulfonate, 4-nitroquinoline 1-oxide, N-methyl-N′-nitro-N-nitrosoguanidine and tert-butyl hydroperoxide. This mutant was originally isolated as a mutant that could not grow on medium containing histidine. Meiosis and sporulation were defective in homozygous crosses between mus-23 haploids. The mus-23 gene is located on the right arm of LGII, between fl and trp-3. Analyses of epistasis between mus-23 and other mutations that cause defects in DNA repair indicated that the mus-23 gene belongs to the same DNA repair group as mei-3, which is the Neurospora homolog of the Saccharomyces cerevisiae gene RAD51. The double mutant carrying mus-23 and uvs-3 mutations was lethal. The mus-23 gene was cloned by complementation of the MMS-sensitive phenotype of the mus-23 mutant. The gene contained an open reading frame of 1578 bp and did not contain any introns. The molecular weight of the predicted mus-23 gene product was 60.4 kDa. Computer analyses revealed that the MUS23 protein has significant homology to Mre11p, which is known to be involved in recombinational repair in S. cerevisiae. The level of mus-23 transcripts increased significantly within 60 min of treatment with UV or MMS and then gradually decreased. The role of MUS23 protein in recombinational repair is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050587
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