Conclusion
Up to now, investigations on the function of chromogranins have been conducted mainly in mammalian species. Although much has been learned from these studies on the structure, properties and distribution of chromogranins, their physiological function is still a matter of debate. Studies in distant vertebrate species will bring novel information that may help to solve the enigma of chromogranin function. From the cloning of the frog SgII and CGA proteins, we could learn that evolutionary pressure has acted to conserve the sequence of specific amino acid stretches within these proteins. The fact that some of these conserved regions have been characterized as free peptides such as SN or vasostatin for which biological activities have been described, strongly suggests that one of the functions of chromogranins is to serve as precursors to biologically active peptides. This notion still needs further support, for example by characterization of the receptors for these peptides. On the other hand, chromogranins exhibit a high content of acidic amino acids in all species studied to date, suggesting that this property is probably important for their function. It is conceivable that before chromogranins are released from the cells to act as neuropeptides or hormones, they may participate in the intracellular events leading to secretory granule formation as has been previously suggested (Huttner and Natori 1995). Their highly acidic nature could be the basis for such a complementary role.
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References
Aardal, S., and Helle, K.B., 1992, The vasoinhibitory activity of bovine chromogranin A fragment (vasostatin) and its independence of extracellular calcium in isolated segments of human blood vessels. Regul. Pept. 41: 9–18.
Aardal, S., Helle, K.B., Elsayed, S., Reed, R.K., and Serck-Hanssen, G., 1993, Vasostatins, comprising the N-terminal domain of chromogranin A, suppress tension in isolated human blood vessel segments. J. Neuroendocrinol. 5: 405–412.
Anouar, Y., Benie, T., De Monti, M., Counis, R., and Duval, J., 1991, Estradiol negatively regulates secretogranin II and chromogranin A messenger ribonucleic acid levels in the female rat pituitary but not in the adrenal. Endocrinology 129: 2393–2399.
Anouar, Y., Desmoucelles, C., Yon, L., Leprince, J., Breault, L., Gallo-Payet, N., and Vaudry, H., 1998, Identification of a novel secretogranin II-derived peptide (SgII(187–252)) in adult and fetal human adrenal glands using antibodies raised against the human recombinant peptide. J. Clin. Endocrinol. Metab. 83: 2944–2951.
Anouar, Y., Jegou, S., Alexandre, D., Lihrmann, I., Conlon, J.M., and Vaudry, H., 1996, Molecular cloning of frog secretogranin II reveals the occurrence of several highly conserved potential regulatory peptides. FEBS Lett. 394: 295–299.
Ayoubi, T.A., Jenks, B.G., Roubos, E.W., and Martens, G.J., 1992, Transcriptional and posttranscriptional regulation of the proopiomelanocortin gene in the pars intermedia of the pituitary gland of Xenopus laevis. Endocrinology 130: 3560–3566.
Benedum, U.M., Baeuerle, P.A., Konecki, D.S., Frank, R., Powell, J., Mallet, J., and Huttner, W.B., 1986, The primary structure of bovine chromogranin A a representative of a class of acidic secretory proteins common to a variety of peptidergic cells. EMBO J. 5: 1495–1502.
Blazquez, M., Bosma, P.T., Chang, J.P., Docherty, K., and Trudeau, V.L., 1998, Gamma-aminobutync acid up-regulates the expression of a novel secretogranin-II messenger ribonucleic acid in the goldfish pituitary. Endocrinology 139: 4870–4880.
Conlon, J.M., Hamberger, B., and Grimelius, L., 1992, Isolation of peptides arising from the specific posttranslational processing of chromogranin A and chromogranin B from human pheochromocytoma tissue. Peptides 13: 639–644.
Curry, W.J., Shaw, C., Johnston, C.F., Thim, L., and Buchanan, K.D., 1992, Isolation and primary structure of a novel chromogranin A-derived peptide, WE-14, from a human midgut carcinoid tumour. FEBS Lett. 301: 319–321.
Eiden, L.E., 1987, Is chromogranin a prohormone? Nature (London) 325: 301.
Fasciotto, B.H., Gorr, S.U., DeFranco, D.J., Levine, M.A., and Cohn, D.V., 1989, Pancreastatin, a presumed product of chromogranin-A (secretory protein-I) processing, inhibits secretion from porcine parathyroid cells in culture. Endocrinology 125: 1617–1622.
Fischer-Colbrie, R., Wohlfarter, T., Schmid, K.W., Grimes, M., and Winkler, H., 1989, Dexamethasone induces an increased biosynthesis of chromogranin A in rat pituitary gland. J. Endocrinol. 121: 487–494.
Holthuis, J.C., and Martens, G.J., 1996, The neuroendocrine proteins secretogranin II and III are regionally conserved and coordinately expressed with proopiomelanocortin in Xenopus intermediate pituitary. J. Neurochem. 66: 2248–2256.
Huttner, W.B., and Benedum, U.M., 1987, Chromogranin A and pancreastatin. Nature (London) 325: 305.
Huttner, W.B., and Natori, S., 1995, Regulated secretion. Helper proteins for neuroendocrine secretion. Curr. Biol. 5: 242–245.
Hutton, J.C., Davidson, H.W., Grimaldi, K.A., and Peshavaria, M., 1987, Biosynthesis of betagranin in pancreatic beta-cells. Identification of a chromogranin A-like precursor and its parallel processing with proinsulin. Biochem. J. 244: 449–456.
Iacangelo, A.L., and Eiden, L.E., 1995, Chromogranin A current status as a precursor for bioactive peptides and a granulogenic/sorting factor in the regulated secretory pathway. Regul. Pept. 58: 65–88.
Iacangelo, A.L., Fischer-Colbrie, R., Koller, K.J., Brownstein, M.J., and Eiden, L.E., 1988, The sequence of porcine chromogranin A messenger RNA demonstrates chromogranin A can serve as the precursor for the biologically active hormone, pancreastatin. Endocrinology 122: 2339–2341.
Kong, C., Gill, B.M., Rahimpour, R., Xu, L., Feldman, R.D., Xiao, Q., McDonald, T.J., Taupenot, L., Mahata, S.K., Singh, B., O’Connor, D.T., and Kelvin, D.J., 1998, Secretoneurin and chemoattractant receptor interactions. J. Neuroimmunol. 88: 91–98.
Mahata, S.K., O’Connor, D.T., Mahata, M., Yoo, S.H., Taupenot, L., Wu, H., Gill, B.M., and Parmer, R.J., 1997, Novel autocrine feedback control of catecholamine release. A discrete chromogranin a fragment is a noncompetitive nicotinic cholinergic antagonist. J. Clin. Invest. 100: 1623–1633.
Parker, D.B., Power, M.E., Swanson, P., Rivier, J., and Sherwood, N.M., 1997, Exon skipping in the gene encoding pituitary adenylate cyclase-activating polypeptide in salmon alters the expression of two hormones that stimulate growth hormone release. Endocrinology 138: 414–423.
Reinecke, M., and Maake, C., 1993, A phylogenetic survey of pancreastatin and chromogranin immunoreactivity in chromaffin (TH-, DBH-, and PNMT-immunoreactive) cells of the adrenal organ of vertebrates. Gen.Comp.Endocrinol. 90: 251–265.
Reinisch, N., Kirchmair, R., Kahler, C.M., Hogue-Angeletti, R., Fischer-Colbrie, R., Winkler, H., and Wiedermann, C.J., 1993, Attraction of human monocytes by the neuropeptide secretoneurin. FEBS Lett. 334: 41–44.
Saria, A., Troger, J., Kirchmair, R., Fischer-Colbrie, R., Hogue-Angeletti, R., and Winkler, H., 1993, Secretoneurin releases dopamine from rat striatal slices: a biological effect of a peptide derived from secretogranin II (chromogranin C). Neuroscience 54: 1–4.
Schneitler, C., Kahler, C., Wiedermann, C.J., Hogue-Angeletti, R., and Fischer-Colbrie, R., 1998, Specific binding of a 1251-secretoneurin analogue to a human monocytic cell line. J. Neuroimmunol. 86: 87–91.
Simon, J.P., and Aunis, D., 1989, Biochemistry of the chromogranin A protein family. Biochem. J. 262: 1–13.
Tatemoto, K., Efendic, S., Mutt, V., Makk, G., Feistner, G.J., and Barchas, J.D., 1986, Pancreastatin, a novel pancreatic peptide that inhibits insulin secretion. Nature (London) 324: 476–478.
Turquier, V., Vaudry, H., Jegou, S., and Houar, Y., 1999, Frog chromogranin A messenger ribonucleic acid encodes three highly conserved peptides. Coordinate regulation of proopiomelanocortin and chromogranin A gene expression in the pars intermedia of the pituitary during background color adaptation. Endocrinology 140: 4104–4112.
Van Horssen, A.M., and Martens, G.J., 1999, Biosynthesis of secretogranin II in Xenopus intermediate pituitary. Mol. Cell. Endocrinol. 147: 57–64.
Vaudry, H., and Conlon, J.M., 1991, Identification of a peptide arising from the specific post-translation processing of secretogranin II. FEBS Lett. 284: 31–33.
Winkler, H., and Fischer-Colbrie, R., 1992, The chromogranins A and B: the first 25 years and future perspectives. Neuroscience 49: 497–528.
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Turquier, V., Vaudry, H., Montéro, M., Yon, L., Anouar, Y. (2002). Characterization of Chromogranins in the Frog Rana ridibunda . In: Helle, K.B., Aunis, D. (eds) Chromogranins. Advances in Experimental Medicine and Biology, vol 482. Springer, Boston, MA. https://doi.org/10.1007/0-306-46837-9_9
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