The novel catecholamine release-inhibitory peptide catestatin (chromogranin A344-364). Properties and function.
The novel catecholamine release-inhibitory peptide catestatin (chromogranin A344-364). Properties and function.
复制标题
新型儿茶酚胺释放抑制肽儿茶素（嗜铬粒蛋白 A344-364）。
DOI：
10.1007/0-306-46837-9_21
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发表时间：
2000
影响因子：
--
通讯作者：
O'Connor,DT
中科院分区：
文献类型：
--
作者：
Mahata,SK;Mahata,M;LivseyTaylor,CV;Taupenot,L;Parmer,RJ;O'Connor,DT
Chromogranin A (CGA), a highly acidic secretory protein, was initially discovered in catecholamine storage vesicles of the adrenal medulla (Blaschko et al 1967, Huttner et al 1991, Takiyyuddin et al 1990, Winkler and Fischer-Colbrie 1992). It belongs to the chromogranin/secretogranin protein family, which also includes chromogranin B and secretogranin II (Fischer-Colbrie et al 1995, Huttner et al 1991, Winkler and Fischer-Colbrie 1992). These proteins are ubiquitously distributed in endocrine, neuroendocrine, and neuronal cells. CGA is encoded by eight exons with a molecular mass of-48 kDa. The primary structure of this protein reveals conserved pairs of 8-10 dibasic sites, which are potential sites of proteolytic cleavages for the generation of biologically active peptides. These peptides include pancreastatin (porcine CGA240-288), which impairs glucose tolerance by inhibiting glucose-stimulated insulin release from pancreatic islet betacells (Tatemoto et al 1986), and by triggering hepatic glycogenolysis (Sanchez-Margalet 1999), the vasodilator (vascular smooth muscle-relaxing) vasostatin (human CGA1-76)(Aardal et al 1993), parastatin (porcine CGA347-419) which inhibits PTH secretion by parathyroid chief cells (Fasciotto et al
