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Gene Review

Chgb  -  chromogranin B

Mus musculus

Synonyms: CgB, Chromogranin-B, Scg-1, Scg1, Secretogranin I, ...
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Disease relevance of Chgb


Psychiatry related information on Chgb


High impact information on Chgb

  • Chromogranin B (CgB, secretogranin I) is a secretory granule matrix protein expressed in a wide variety of endocrine cells and neurons [3].
  • Upon subcellular fractionation of the exocrine pancreas, the distribution of CgB in the various fractions was indistinguishable from that of amylase, an endogenous constituent of zymogen granules [3].
  • Immunogold electron microscopy of pancreatic acinar cells showed co-localization of CgB with zymogens in Golgi cisternae, condensing vacuoles/immature granules and mature zymogen granules; the ratio of immunoreactivity of CgB to zymogens being highest in condensing vacuoles/immature granules [3].
  • Two distinct chromogranin B-derived peptides result from cleavage at Trp-Trp bonds, a site not typically associated with neuropeptide processing [6].
  • The expression of phenylethanolamine N-methyl transferase and chromogranin B mRNA was similar in TH-null and wild-type mice [7].

Biological context of Chgb


Anatomical context of Chgb

  • Recently, secretory granule Ca(2+) storage protein chromogranin B (CGB) was shown to be present in the nucleoplasm proper in a complex structure that consists of the inositol 1,4,5-trisphosphate receptor (IP(3)R)/Ca(2+) channels and the phospholipids [12].
  • In contrast, inhibition of CGA expression in PC12 cells by siRNA treatment decreased the IP(3)-induced Ca(2+) releases in the nucleus by 17%, while inhibition of CGB expression decreased the IP(3)-induced Ca(2+) releases in the nucleus by 55% [12].
  • Peptides found to increase corresponded to fragments of proenkephalin, prothyrotropin-releasing hormone, provasopressin, proSAAS, secretogranin II, chromogranin B, and peptidyl-glycine-alpha-amidating mono-oxygenase in the hypothalamus [13].
  • Chromogranin B-like immunoreactivity in the mouse submandibular salivary gland during postnatal development [14].
  • Recently, we have isolated from bovine chromaffin granules and identified two natural peptides possessing antibacterial activity: secretolytin (chromogranin B 614-626) and enkelytin (proenkephalin-A 209-237) [15].

Associations of Chgb with chemical compounds


Other interactions of Chgb

  • Microinjection of IP(3) into the nucleus of CGB-expressing NIH3T3 cells increased the IP(3)-dependent nuclear Ca(2+) mobilization approximately 3-fold, whereas in CGA-expressing cells it remained the same as that of control cells [12].
  • PC1 appeared to be by far the most active enzyme and converted chromogranin B to several smaller molecules, including the peptide PE-11 [4].
  • Some processing of chromogranin B and formation of free PE-11 were also observed with PC2 and PACE4 [4].
  • Northern and immunoblot analyses, in situ hybridization and immunocytochemistry revealed that the exocrine pancreas was the tissue with the highest level of ectopic CgB expression [3].
  • Proenkephalin mRNA in both saline- and ACTH-treated CRHR1 null mice were higher than in control animals (215.8% P <0.05, 268.9% P <0.01) whereas expression of neuropeptide Y and chromogranin B did not differ [19].

Analytical, diagnostic and therapeutic context of Chgb


  1. Chromogranin A, chromogranin B and secretogranin II mRNAs in the pituitary and adrenal glands of various mammals. Regulation of chromogranin A, chromogranin B and secretogranin II mRNA levels by estrogen. Lloyd, R.V., Hawkins, K., Jin, L., Kulig, E., Fields, K. Lab. Invest. (1992) [Pubmed]
  2. Secretogranin II expression in Ewing's sarcomas and primitive neuroectodermal tumors. Pagani, A., Fischer-Colbrie, R., Sanfilippo, B., Winkler, H., Cerrato, M., Bussolati, G. Diagn. Mol. Pathol. (1992) [Pubmed]
  3. Chromogranin B (secretogranin I), a neuroendocrine-regulated secretory protein, is sorted to exocrine secretory granules in transgenic mice. Natori, S., King, A., Hellwig, A., Weiss, U., Iguchi, H., Tsuchiya, B., Kameya, T., Takayanagi, R., Nawata, H., Huttner, W.B. EMBO J. (1998) [Pubmed]
  4. Proteolytic processing of chromogranin B and secretogranin II by prohormone convertases. Laslop, A., Weiss, C., Savaria, D., Eiter, C., Tooze, S.A., Seidah, N.G., Winkler, H. J. Neurochem. (1998) [Pubmed]
  5. Peptidomics of Cpe fat/fat mouse hypothalamus: effect of food deprivation and exercise on peptide levels. Che, F.Y., Yuan, Q., Kalinina, E., Fricker, L.D. J. Biol. Chem. (2005) [Pubmed]
  6. Identification of peptides from brain and pituitary of Cpe(fat)/Cpe(fat) mice. Che, F.Y., Yan, L., Li, H., Mzhavia, N., Devi, L.A., Fricker, L.D. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  7. Deletion of tyrosine hydroxylase gene reveals functional interdependence of adrenocortical and chromaffin cell system in vivo. Bornstein, S.R., Tian, H., Haidan, A., Böttner, A., Hiroi, N., Eisenhofer, G., McCann, S.M., Chrousos, G.P., Roffler-Tarlov, S. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  8. Structure and function of the chromogranin A gene. Clues to evolution and tissue-specific expression. Wu, H.J., Rozansky, D.J., Parmer, R.J., Gill, B.M., O'Connor, D.T. J. Biol. Chem. (1991) [Pubmed]
  9. Chromogranin B-induced secretory granule biogenesis: comparison with the similar role of chromogranin A. Huh, Y.H., Jeon, S.H., Yoo, S.H. J. Biol. Chem. (2003) [Pubmed]
  10. Genetic dissection of vasculitis, myeloperoxidase-specific antineutrophil cytoplasmic autoantibody production, and related traits in spontaneous crescentic glomerulonephritis-forming/Kinjoh mice. Hamano, Y., Tsukamoto, K., Abe, M., Sun, G.D., Zhang, D., Fujii, H., Matsuoka, S., Tanaka, M., Ishida-Okawara, A., Tachikawa, H., Nishimura, H., Tokunaka, K., Hirose, S., Suzuki, K. J. Immunol. (2006) [Pubmed]
  11. Dense-core granules: a specific hallmark of the neuronal/neurosecretory cell phenotype. Malosio, M.L., Giordano, T., Laslop, A., Meldolesi, J. J. Cell. Sci. (2004) [Pubmed]
  12. Role of nuclear chromogranin B in inositol 1,4,5-trisphosphate-mediated nuclear Ca2+ mobilization. Huh, Y.H., Chu, S.Y., Park, S.Y., Huh, S.K., Yoo, S.H. Biochemistry (2006) [Pubmed]
  13. Quantitative peptidomics in mice: effect of cocaine treatment. Che, F.Y., Vathy, I., Fricker, L.D. J. Mol. Neurosci. (2006) [Pubmed]
  14. Chromogranin B-like immunoreactivity in the mouse submandibular salivary gland during postnatal development. Letić-Gavrilović, A., Abe, K., Mori, M. Acta Histochem. (1990) [Pubmed]
  15. Antibacterial activity of glycosylated and phosphorylated chromogranin A-derived peptide 173-194 from bovine adrenal medullary chromaffin granules. Strub, J.M., Goumon, Y., Lugardon, K., Capon, C., Lopez, M., Moniatte, M., Van Dorsselaer, A., Aunis, D., Metz-Boutigue, M.H. J. Biol. Chem. (1996) [Pubmed]
  16. In vivo expression and stoichiometric sulfation of the artificial protein sulfophilin, a polymer of tyrosine sulfation sites. Niehrs, C., Huttner, W.B., Rüther, U. J. Biol. Chem. (1992) [Pubmed]
  17. A functional interaction between chromogranin B and the inositol 1,4,5-trisphosphate receptor/Ca2+ channel. Thrower, E.C., Choe, C.U., So, S.H., Jeon, S.H., Ehrlich, B.E., Yoo, S.H. J. Biol. Chem. (2003) [Pubmed]
  18. Expression of regulated secretory proteins is sufficient to generate granule-like structures in constitutively secreting cells. Beuret, N., Stettler, H., Renold, A., Rutishauser, J., Spiess, M. J. Biol. Chem. (2004) [Pubmed]
  19. Chromaffin cell function and structure is impaired in corticotropin-releasing hormone receptor type 1-null mice. Yoshida-Hiroi, M., Bradbury, M.J., Eisenhofer, G., Hiroi, N., Vale, W.W., Novotny, G.E., Hartwig, H.G., Scherbaum, W.A., Bornstein, S.R. Mol. Psychiatry (2002) [Pubmed]
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