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SCG2  -  secretogranin II

Bos taurus

 
 
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Disease relevance of SCG2

  • We investigated the proteolytic processing of secretogranin II by prohormone convertases in vivo in a cellular system using the vaccinia virus system [1].
 

High impact information on SCG2

 

Biological context of SCG2

 

Anatomical context of SCG2

 

Associations of SCG2 with chemical compounds

  • The effect of PACAP on SgII mRNA levels, like the effect of the PKC stimulator 12-O-tetradecanoylphorbol-13-acetate (TPA), was not affected by cycloheximide, whereas the effects of the PKA stimulator forskolin or cell-depolarization by high K(+) were significantly reduced by the protein synthesis inhibitor [5].
  • The cytosolic calcium chelator BAPTA-AM and the nonselective calcium channel antagonist NiCl(2) equally inhibited both secretion of the peptide and transcription of the SgII gene, indicating a major contribution of calcium influx in PACAP-induced SN biosynthesis and release in chromaffin cells [5].
  • 5. Secretogranin II also underwent acidic pH- and Ca(2+)-dependent aggregation, and it was approximately 8-fold more sensitive than CGA to Ca(2+) in its pH-dependent aggregation but was 8-fold less sensitive than CGB [6].
  • Nicotine and prostaglandin E2 elevated secretogranin II mRNA and protein up to three-fold [8].
  • Proteolytic processing of chromogranin A and secretogranin II was higher in noradrenaline cells which was paralleled by a higher content of the prohormone convertase PC2 [9].
 

Other interactions of SCG2

 

Analytical, diagnostic and therapeutic context of SCG2

References

  1. Processing of secretogranin II by prohormone convertases: importance of PC1 in generation of secretoneurin. Hoflehner, J., Eder, U., Laslop, A., Seidah, N.G., Fischer-Colbrie, R., Winkler, H. FEBS Lett. (1995) [Pubmed]
  2. Sorting of three secretory proteins to distinct secretory granules in acidophilic cells of cow anterior pituitary. Hashimoto, S., Fumagalli, G., Zanini, A., Meldolesi, J. J. Cell Biol. (1987) [Pubmed]
  3. Histamine induces a gene-specific synthesis regulation of secretogranin II but not of chromogranin A and B in chromaffin cells in a calcium-dependent manner. Bauer, J.W., Kirchmair, R., Egger, C., Fischer-Colbrie, R. J. Biol. Chem. (1993) [Pubmed]
  4. Sequence analysis, tissue distribution and regulation by cell depolarization, and second messengers of bovine secretogranin II (chromogranin C) mRNA. Fischer-Colbrie, R., Gutierrez, J., Hsu, C.M., Iacangelo, A., Eiden, L.E. J. Biol. Chem. (1990) [Pubmed]
  5. Pituitary adenylate cyclase-activating polypeptide stimulates secretoneurin release and secretogranin II gene transcription in bovine adrenochromaffin cells through multiple signaling pathways and increased binding of pre-existing activator protein-1-like transcription factors. Turquier, V., Yon, L., Grumolato, L., Alexandre, D., Fournier, A., Vaudry, H., Anouar, Y. Mol. Pharmacol. (2001) [Pubmed]
  6. Purification, pH-dependent conformational change, aggregation, and secretory granule membrane binding property of secretogranin II (chromogranin C). Park, H.Y., So, S.H., Lee, W.B., You, S.H., Yoo, S.H. Biochemistry (2002) [Pubmed]
  7. Chromogranin C: a third component of the acidic proteins in chromaffin granules. Fischer-Colbrie, R., Hagn, C., Kilpatrick, L., Winkler, H. J. Neurochem. (1986) [Pubmed]
  8. Nicotine and prostaglandin E induce secretogranin II levels in bovine chromaffin cells. Wolkersdorfer, M., Egger, C., Laslop, A., Fischer-Colbrie, R. Brain Res. Mol. Brain Res. (1996) [Pubmed]
  9. Differences in the composition of chromaffin granules in adrenaline and noradrenaline containing cells of bovine adrenal medulla. Weiss, C., Cahill, A.L., Laslop, A., Fischer-Colbrie, R., Perlman, R.L., Winkler, H. Neurosci. Lett. (1996) [Pubmed]
  10. The proinflammatory cytokines tumor necrosis factor-alpha and interleukin-1 stimulate neuropeptide gene transcription and secretion in adrenochromaffin cells via activation of extracellularly regulated kinase 1/2 and p38 protein kinases, and activator protein-1 transcription factors. Ait-Ali, D., Turquier, V., Grumolato, L., Yon, L., Jourdain, M., Alexandre, D., Eiden, L.E., Vaudry, H., Anouar, Y. Mol. Endocrinol. (2004) [Pubmed]
  11. Processing of chromogranins in chromaffin cell culture: effects of reserpine and alpha-methyl-p-tyrosine. Wolkersdorfer, M., Laslop, A., Lazure, C., Fischer-Colbrie, R., Winkler, H. Biochem. J. (1996) [Pubmed]
  12. Immunodetection of secretogranin II in animal and human tissues by new monoclonal antibodies. Pelagi, M., Zanini, A., Gasparri, A., Ermellino, L., Giudici, A.M., Ferrero, S., Siccardi, A.G., Buffa, R. Regul. Pept. (1992) [Pubmed]
  13. Immunological characterization of chromogranins A and B and secretogranin II in the bovine pancreatic islet. Yoshie, S., Hagn, C., Ehrhart, M., Fischer-Colbrie, R., Grube, D., Winkler, H., Gratzl, M. Histochemistry (1987) [Pubmed]
 
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