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C2  -  complement component 2

Rattus norvegicus

 
 
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High impact information on C2

  • However, Ca2+ titrations monitored via intrinsic tryptophan fluorescence revealed that all three C2 domains bound Ca2+ in the absence of phospholipids with a high apparent affinity (EC50 of approximately 1.3-2.3 microM) [1].
  • All MCTP C2 domains except for the second C2 domain of MCTP2 include a perfect Ca2+/phospholipid-binding consensus sequence [1].
  • By contrast, however, some C2 domains do not exhibit Ca2+ binding activity because of amino acid substitutions at Ca2+ -binding sites, and their physiological meanings remain largely unknown [2].
  • The C2 domain was originally defined as a homologous domain to the C2 regulatory region of Ca2+ -dependent protein kinase C and has been identified in more than 50 different signaling molecules [2].
  • The original C2 domain of protein kinase Calpha functions as a Ca2+ binding module, and the Ca2+ binding to the C2 domain allows translocation of proteins to phospholipid membranes [2].
 

Biological context of C2

  • The presence of C1- and C2-domains in these proteins and the phenotype of the C. elegans mutants raise the possibility that Munc13s may have an essential signaling role during neurotransmitter release [3].
  • Rat prostatic binding protein: the complete sequence of the C2 gene and its flanking regions [4].
  • Domain formation in a fluid mixed lipid bilayer modulated through binding of the C2 protein motif [5].
  • In some areas (e.g., the substantia nigra), [3H]rauwolscine binding sites were detected even though alpha C2 messenger RNA expression was absent [6].
  • In the rat brain, four C-terminal variants of the NR1 subunit (NR1-1 to NR1-4) are encoded by a single gene, and are generated by alternative splicing of the C1 and C2 exon cassettes, while four different genes encode the NR2 subunits (NR2 A-D) [7].
 

Anatomical context of C2

  • Here, we investigated the regulation of protease (cathepsin B, cathepsin D, proteasome C2 subunit and m-calpain) mRNA concentrations by Dex in cultured L8 muscle cells [8].
  • CONCLUSION: EPA supplement decreased skeletal muscle E2(14k), E3alpha, and hepatic C2 mRNA levels compared with the isocaloric, isonitrogenous corn oil supplement, supporting a treatment-specific effect [9].
  • On day 29, tumor volume (TV) was determined; liver and quadriceps muscles were also excised to determine gene expression of C2, C3, E2(14k), and E3alpha by reverse transcription-polymerase chain reaction (RT-PCR) [9].
 

Associations of C2 with chemical compounds

  • Munc13s are large, brain-specific proteins with divergent N termini but conserved C termini containing C1- and C2-domains [3].
  • The complete sequence (2879 bp) of the androgen-controlled rat prostatic binding protein C2 gene and 1023 bp of the 5'- and 2127 bp of the 3'-flanking regions have been determined [4].
  • Addition of the C2 protein motif (a structural domain found in proteins implicated in eukaryotic signal transduction and cellular trafficking processes) to the bilayer first increases and then decreases the excimer/monomer ratio of the pyrene fluorescence [5].
  • Three protein-DNA complexes (C1, C2, and C3) were detected in band-shift assays [10].
  • The specific radioactivity of biliary cholesterol, as compared to liver cholesterol, was 12 times higher for C2 and five times higher for MCFA [11].
 

Other interactions of C2

  • Proteasome C2 mRNA was unaffected by Dex and Dex reduced alpha-tubulin mRNA [8].
 

Analytical, diagnostic and therapeutic context of C2

  • Semiquantitative reverse transcription-polymerase chain reaction (RT-PCR) revealed approximately twofold lower proteasome C2 mRNA levels in the lesion group as compared with the sham-operated group [12].
  • The proteins forming complexes C2 and C3 have been purified by DNA-affinity chromatography and their molecular masses (75-80 kDa and 35-40 kDa, respectively) have been determined by ultraviolet cross-linking to radio-labelled DNA and SDS/PAGE [10].

References

  1. Evolutionarily conserved multiple C2 domain proteins with two transmembrane regions (MCTPs) and unusual Ca2+ binding properties. Shin, O.H., Han, W., Wang, Y., Südhof, T.C. J. Biol. Chem. (2005) [Pubmed]
  2. The C2A domain of double C2 protein gamma contains a functional nuclear localization signal. Fukuda, M., Saegusa, C., Kanno, E., Mikoshiba, K. J. Biol. Chem. (2001) [Pubmed]
  3. Mammalian homologues of Caenorhabditis elegans unc-13 gene define novel family of C2-domain proteins. Brose, N., Hofmann, K., Hata, Y., Südhof, T.C. J. Biol. Chem. (1995) [Pubmed]
  4. Rat prostatic binding protein: the complete sequence of the C2 gene and its flanking regions. Delaey, B., Dirckx, L., Decourt, J.L., Claessens, F., Peeters, B., Rombauts, W. Nucleic Acids Res. (1987) [Pubmed]
  5. Domain formation in a fluid mixed lipid bilayer modulated through binding of the C2 protein motif. Hinderliter, A., Almeida, P.F., Creutz, C.E., Biltonen, R.L. Biochemistry (2001) [Pubmed]
  6. Expression of alpha 2 adrenoceptors during rat brain development--II. Alpha 2C messenger RNA expression and [3H]rauwolscine binding. Winzer-Serhan, U.H., Raymon, H.K., Broide, R.S., Chen, Y., Leslie, F.M. Neuroscience (1997) [Pubmed]
  7. Differential interaction of the tSXV motifs of the NR1 and NR2A NMDA receptor subunits with PSD-95 and SAP97. Bassand, P., Bernard, A., Rafiki, A., Gayet, D., Khrestchatisky, M. Eur. J. Neurosci. (1999) [Pubmed]
  8. Effects of dexamethasone on protein degradation and protease gene expression in rat L8 myotube cultures. Hong, D.H., Forsberg, N.E. Mol. Cell. Endocrinol. (1995) [Pubmed]
  9. Modulation of the ubiquitin-proteasome proteolytic pathway by eicosapentaenoic acid supplementation in a model of progressive malignancy. Mikhail, A.T., Babcock, T.A., Jho, D.H., Helton, W.S., Brodsky, I.G., Espat, N.J. JPEN. Journal of parenteral and enteral nutrition. (2003) [Pubmed]
  10. Characterization of the nuclear proteins binding the CACCC element of a glucocorticoid-responsive enhancer in the tyrosine aminotransferase gene. DeVack, C., Lupp, B., Nichols, M., Kowenz-Leutz, E., Schmid, W., Schütz, G. Eur. J. Biochem. (1993) [Pubmed]
  11. The incorporation of fatty acids of different chain length into liver and biliary lipids in the perfused rat liver. Rubin, M., Pakula, R., Gilat, T., Tietz, A. Lipids (1999) [Pubmed]
  12. Suppression of proteasome C2 contralateral to ischemic lesions in rat brain. Keyvani, K., Reinecke, S., Abts, H.F., Paulus, W., Witte, O.W. Brain Res. (2000) [Pubmed]
 
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