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  • 1
    Electronic Resource
    Electronic Resource
    A novel ubiquitin-specific protease, synUSP, is localized at the post-synaptic density and post-synaptic lipid raft (2003)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 87 (2003), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Recent reports suggest an important role for protein ubiquitination in synaptic plasticity. We cloned, from the rat brain, a novel gene that encoded an ubiquitin-specific protease (USP), and termed this protein synaptic ubiquitin-specific protease (synUSP, GenBankTM Accession no. 〈accessionId ref="info:ddbj-embl-genbank/AB073880"〉AB073880). The homologous human gene was mapped to a locus on chromosome 1p36.12. The deduced synUSP protein consisted of 1036 amino acids, and possessed an ubiquitin-like domain at the C-terminus, Cys- and His-boxes, leucine zipper motifs, and six amino acid-repeats of L/ILCPHG. The protein possessed de-ubiquitinating activity toward a model substrate, as expected from its sequence. The protein of 125 kDa was present in the rat brain; in particular, it was enriched in the post-synaptic density and the dendritic lipid raft fractions. The immunostaining of cortical neurons confirmed the post-synaptic localization. The mRNA for synUSP was localized to dendrites, as well as somas, of neuronal cells. Thus, both the mRNA and the protein were localized in the post-synaptic compartments. These results suggest a regulatory mechanism for the ubiquitin-related system at the post-synaptic sites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.2003.02024.x
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  • 2
    Electronic Resource
    Electronic Resource
    The NK-2 Homeobox Gene and the Early Development of the Central Nervous System of Drosophila (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 758 (1995), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1995.tb24830.x
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  • 3
    Electronic Resource
    Electronic Resource
    Molecular Cloning and Characterization of Complementary and Genomic DNA Clones for Mouse C4 and SLP (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Immunological reviews 87 (1985), S. 0 
    Details
    ISSN: 1600-065X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-065X.1985.tb01146.x
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  • 4
    Electronic Resource
    Electronic Resource
    Three extra copies of a C4-related gene in H-2 w7 mice are C4/Slp hybrid genes generated by multiple recombinational events (1990)
    Springer
    Immunogenetics 32 (1990), S. 431-439 
    Details
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Mice bearing the H-2 w7 haplotype have five C4-related genes and constitutively express the Slp antigen. To understand the structure and evolution of the five C4-related genes of the C3H.W7 mouse, we have determined nucleotide sequences of the 5′ end region of these genes. A C4/Slp hybrid nature was confirmed for three of five C4-related genes as predicted previously by restriction enzyme analysis. The nucleotide sequences of the 5′ flanking regions of these three hybrid genes showed close similarity to that of the C4 gene, while the 3′ side of the ninth exon of the three hybrid genes showed close similarity to that of the Slp gene. In contrast, the regions between the first exon and the middle of the ninth exon of the three hybrid genes showed a mosaic structure of C4-like and Slp-like sequences. Moreover, the boundaries of the C4-like and Slp-like sequences were quite different among the three hybrid genes. The pattern of nucleotide sequence diversity in this region among the five C4-related sequences could be mainly explained not by point mutations but by gene conversions or unequal crossovers. These results suggest that multiple genetic recombinational events between two homologous sequences played an important role in the generation and diversification of the extra copies of the C4/Slp gene in the H-2 w7 mouse.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00241638
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  • 5
    Electronic Resource
    Electronic Resource
    Post-transcriptional regulation of complement C4 in low C4-producing strain of mouse (1990)
    Springer
    Immunogenetics 31 (1990), S. 361-367 
    Details
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The expression of the fourth component of complement (C4) of the mouse can differ 20-fold and is determined byC4-high (C4 h ) orC4-low (C4 l ) alleles. To investigate the molecular mechanisms underlying the differences in C4 expression, we compared the transcriptional activity of theC4 genes between high and low C4-producer strains of mice (B10 and FM vs B10.BR) using nuclear transcriptional and chloramphenicol acetyltransferase (CAT) assays. We also compared the level of C4-specific RNA in total and nuclear RNA of the liver. The results revealed no significant difference in transcriptional activity betweenC4 h andC4 l genes. However, the steady-state levels of C4 mRNA are ten times lower inC4 l strains than inC4 h strains, suggesting that the major regulation of C4 plasma levels occurs at the post-transcriptional level.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02115011
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  • 6
    Electronic Resource
    Electronic Resource
    Fourth component of Xenopus laevis complement: cDNA cloning and linkage analysis of the frog MHC (1996)
    Springer
    Immunogenetics 43 (1996), S. 360-369 
    Details
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract ComplementC4 shows extensive structural and functional similarity to complementC3, hence these components are believed to have originated by gene duplication from a common ancestor. Although to dateC3 cDNA clones have been isolated from all major classes of extant vertebrates includingXenopus, C4 cDNA clones have been isolated from mammalian species only. We describe here the molecular cloning and structural analysis ofXenopus C4 cDNA. The cDNA sequence encoding the thioester region ofXenopus C4 was amplified by reverse transcriptase-polymerase chain reaction usingXenopus liver mRNA as a template, and then used to screen a liver cDNA library. The amino acid sequence ofXenopus C4 deduced from a clone containing the entire protein-coding sequence showed 39%, 30%, 25%, and 20% overall identity with those of human C4, C3, C5, and α2-macroglobulin, respectively. The predicted amino acid sequence consisted of a 22-residue putative signal peptide, a 634-residue β chain, a 732-residue α chain, and a 287-residue γ chain. Of 30 cysteine residues, 27 were found in exactly the same positions as in humanC4. Genomic Southern blotting analysis indicated thatC4 is a single copy gene inXenopus and is part of the frog MHC cluster. These results clearly demonstrate thatC3/C4 gene duplication and linkage between theC4 gene and the major histocompatibility complex predate mammalian/amphibian divergence.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02199804
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  • 7
    Electronic Resource
    Electronic Resource
    Fourth component of Xenopus laevis complement: cDNA cloning and linkage analysis of the frog MHC (1996)
    Springer
    Immunogenetics 43 (1996), S. 360-369 
    Details
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract   Complement C4 shows extensive structural and functional similarity to complement C3, hence these components are believed to have originated by gene duplication from a common ancestor. Although to date C3 cDNA clones have been isolated from all major classes of extant vertebrates including Xenopus, C4 cDNA clones have been isolated from mammalian species only. We describe here the molecular cloning and structural analysis of Xenopus C4 cDNA. The cDNA sequence encoding the thioester region of Xenopus C4 was amplified by reverse transcriptase-polymerase chain reaction using Xenopus liver mRNA as a template, and then used to screen a liver cDNA library. The amino acid sequence of Xenopus C4 deduced from a clone containing the entire protein-coding sequence showed 39%, 30%, 25%, and 20% overall identity with those of human C4, C3, C5, and α2-macroglobulin, respectively. The predicted amino acid sequence consisted of a 22-residue putative signal peptide, a 634-residue β chain, a 732-residue α chain, and a 287-residue γ chain. Of 30 cysteine residues, 27 were found in exactly the same positions as in human C4. Genomic Southern blotting analysis indicated that C4 is a single copy gene in Xenopus and is part of the frog MHC cluster. These results clearly demonstrate that C3/C4 gene duplication and linkage between the C4 gene and the major histocompatibility complex predate mammalian/amphibian divergence.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002510050076
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