The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

CHGA  -  chromogranin A (parathyroid secretory...

Bos taurus

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of CHGA

  • Plasma CgA concentration in 2 dogs with insulinoma (0.9, 1.0 ng/ml) exceeded the reference range established for 10 clinically normal control dogs (0.50 +/- 0.16 ng/ml) [1].
  • Increase in plasma CgA concentration may be useful diagnostically for animals with suspected neuroendocrine tumors [1].

High impact information on CHGA

  • Adrenal medulla, brain, pituitary and parathyroid are all sites of synthesis of chromogranin A. The primary structure of chromogranin A, and the presence of chromogranin mRNA in the parathyroid, indicate that chromogranin A and SP-I are identical [2].
  • Peptides generated by plasmin-mediated cleavage of CgA significantly inhibited nicotinic cholinergic stimulation of catecholamine release from PC12 cells and primary bovine adrenal chromaffin cells [3].
  • Chromogranin A (CgA) is the major soluble protein in the core of catecholamine-storage vesicles and is also distributed widely in secretory vesicles throughout the neuroendocrine system [3].
  • Occupancy of cell surface binding sites promoted the cleavage of CgA by plasmin [3].
  • We show here that the major fibrinolytic enzyme, plasmin, can cleave CgA to form a series of large fragments as well as small trichloroacetic acid-soluble peptides [3].

Biological context of CHGA

  • The nucleotide sequences of the pituitary SP-I cDNA and adrenal medullary SP-I cDNAs are nearly identical [4].
  • Unlike CgA, another granin protein CgB could not substitute for the role of CgA in secretory granule biogenesis [5].
  • In 32P-labeled bovine adrenal medullary cells, 56 mM K+ increased the phosphorylation of CgA and catecholamine secretion in similar time- and concentration-dependent manners, both of which were inhibited by 20 mM MgSO4, an inhibitor of voltage-dependent Ca2+ channels [6].
  • These studies, therefore, explain the lack of quantitative correspondence between 1,25-(OH)2D3-induced CgA gene transcription and CgA protein levels by revealing a previously unsuspected level of regulation of mRNA translation in the parathyroid cell [7].
  • Furthermore, 1,25-(OH)2D3 had no effect on CgA mRNA stability [8].

Anatomical context of CHGA

  • Secretory protein I (SP-I), also referred to as chromogranin A, is an acidic glycoprotein that has been found in every tissue of endocrine and neuroendocrine origin examined but never in exocrine or epithelial cells [4].
  • Catestatin is an active 21-residue peptide derived from the chromogranin A (CgA) precursor, and catestatin is secreted from neuroendocrine chromaffin cells as an autocrine regulator of nicotine-stimulated catecholamine release [9].
  • Chromogranin A (CgA), an acidic granule protein of the regulated secretory pathway in the diffuse neuroendocrine system, is postulated to serve as a prohormone for regulatory peptides [10].
  • Thus, the betagranin peptide rCgA(7-57) and the two bovine chromofungin-containing peptides, highly homologous to the corresponding sequence (rCgA(47-66)), affected the rat cerebral artery without vasodilator effects, indicating significant species differences in vasoactivity of the N-terminal domain of CgA [10].
  • Using immunohistochemical techniques on paraffin-embedded tissue we have successfully shown that CgA is selectively expressed in ciliated cells of the bovine oviduct [11].

Associations of CHGA with chemical compounds

  • Results also demonstrated the presence of 54-56 and 50 kDa catestatin intermediates that contain the NH(2) terminus of CgA [9].
  • Partially purified CgA was phosphorylated by cyclic AMP-dependent protein kinase and protein kinase C as well as CaM kinase II [6].
  • However, that for CgA was doubled in the presence of 1,25-(OH)2D3 [7].
  • Thus, parathyroid CgA synthesis is regulated by the vitamin D sterol at the level of peptide chain elongation [7].
  • Therefore, we examined the effect of 1,25-(OH)2D3 on the polyribosome profile of CgA mRNA analyzed by sucrose density gradients [7].

Other interactions of CHGA

  • The IP(3)R/Ca(2+) channel was shown to directly interact with CgA and CgB at the intragranular pH 5.5, and this coupling led to modulation of the IP(3)R/Ca(2+) channel activity by the coupled chromogranins [12].

Analytical, diagnostic and therapeutic context of CHGA

  • Radioimmunoassay of the bacterial lysates with SP-I antiserum yielded parallel displacement curves of 125I-labeled SP-I by the SP4B lysate and authentic SP-I [4].
  • Catestatin-containing polypeptides, demonstrated by anti-catestatin western blots, of 54-56, 50, 32, and 17 kDa contained NH(2)-terminal peptide sequences that indicated proteolytic cleavages of the CgA precursor at KK downward arrow, KR downward arrow, R downward arrow, and KR downward arrow basic residue sites, respectively [9].
  • Protein sequencing and immunoblotting revealed that the 70-kDa protein is chromogranin A (CgA) or a closely related protein [6].
  • In the present study, immunoprecipitation of extracts of bovine parathyroid cells that had been pulse chased with [35S]methionine revealed that 1,25-(OH)2D3 had no effect on the disappearance time of intracellular CgA [7].
  • HPLC separation of tryptic digests of Ch A (72,000 Da) and SP-I (72,000 Da) also resulted in elution profiles that were very similar to each other [13].


  1. Chromogranin A plasma concentration and expression in pancreatic islet cell tumors of dogs and cats. Myers, N.C., Andrews, G.A., Chard-Bergstrom, C. Am. J. Vet. Res. (1997) [Pubmed]
  2. Bovine chromogranin A sequence and distribution of its messenger RNA in endocrine tissues. Iacangelo, A., Affolter, H.U., Eiden, L.E., Herbert, E., Grimes, M. Nature (1986) [Pubmed]
  3. Processing of chromogranin A by plasmin provides a novel mechanism for regulating catecholamine secretion. Parmer, R.J., Mahata, M., Gong, Y., Mahata, S.K., Jiang, Q., O'Connor, D.T., Xi, X.P., Miles, L.A. J. Clin. Invest. (2000) [Pubmed]
  4. Primary structure of bovine pituitary secretory protein I (chromogranin A) deduced from the cDNA sequence. Ahn, T.G., Cohn, D.V., Gorr, S.U., Ornstein, D.L., Kashdan, M.A., Levine, M.A. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  5. Large dense-core secretory granule biogenesis is under the control of chromogranin A in neuroendocrine cells. Kim, T., Tao-Cheng, J.H., Eiden, L.E., Loh, Y.P. Ann. N. Y. Acad. Sci. (2002) [Pubmed]
  6. Phosphorylation of chromogranin A and catecholamine secretion stimulated by elevation of intracellular Ca2+ in cultured bovine adrenal medullary cells. Yanagihara, N., Oishi, Y., Yamamoto, H., Tsutsui, M., Kondoh, J., Sugiura, T., Miyamoto, E., Izumi, F. J. Biol. Chem. (1996) [Pubmed]
  7. 1,25-Dihydroxycholecalciferol regulates chromogranin-A translatability in bovine parathyroid cells. Mouland, A.J., Hendy, G.N. Mol. Endocrinol. (1992) [Pubmed]
  8. Regulation of synthesis and secretion of chromogranin-A by calcium and 1,25-dihydroxycholecalciferol in cultured bovine parathyroid cells. Mouland, A.J., Hendy, G.N. Endocrinology (1991) [Pubmed]
  9. Primary sequence characterization of catestatin intermediates and peptides defines proteolytic cleavage sites utilized for converting chromogranin a into active catestatin secreted from neuroendocrine chromaffin cells. Lee, J.C., Taylor, C.V., Gaucher, S.P., Toneff, T., Taupenot, L., Yasothornsrikul, S., Mahata, S.K., Sei, C., Parmer, R.J., Neveu, J.M., Lane, W.S., Gibson, B.W., O'Connor, D.T., Hook, V.Y. Biochemistry (2003) [Pubmed]
  10. Chromogranin A-derived peptides: interaction with the rat posterior cerebral artery. Mandalà, M., Brekke, J.F., Serck-Hanssen, G., Metz-Boutigue, M.H., Helle, K.B. Regul. Pept. (2005) [Pubmed]
  11. Colocalization of chromogranin A and inositol 1,4,5-trisphosphate receptor in ciliated cells of the bovine oviduct. Steffl, M., Schweiger, M., Amselgruber, W.M. Ann. Anat. (2003) [Pubmed]
  12. Inositol 1,4,5-trisphosphate receptor/Ca(2+) channel modulatory role of chromogranins A and B. Yoo, S.H., So, S.H., Huh, Y.H., Park, H.Y. Ann. N. Y. Acad. Sci. (2002) [Pubmed]
  13. Structural characterization of adrenal chromogranin A and parathyroid secretory protein-I as homologs. Hamilton, J.W., Chu, L.L., Rouse, J.B., Reddig, K., MacGregor, R.R. Arch. Biochem. Biophys. (1986) [Pubmed]
WikiGenes - Universities