New insights into granin-derived peptides: evolution and endocrine roles
Centre for Advanced Research in Environmental Genomics, Department of Biology, University of Ottawa, 30 Marie Curie, Ottawa, ON, Canada.General and Comparative Endocrinology (Impact Factor: 2.47). 02/2009; 164(2-3):161-74. DOI: 10.1016/j.ygcen.2009.01.011
The granin protein family is composed of two chromogranin and five secretogranin members that are acidic, heat-stable proteins in secretory granules in cells of the nervous and endocrine systems. We report that there is little evidence for evolutionary relationships among the granins except for the chromogranin group. The main granin members, including chromogranin A and B, and secretogranin II are moderately conserved in the vertebrates. Several small bioactive peptides can be generated by proteolysis from those homologous domains existing within the granin precursors, reflecting the conservation of biological activities in different vertebrates. In this context, we focus on reviewing the distribution and function of the major granin-derived peptides, including vasostatin, bovine CgB(1-41) and secretoneurin in vertebrate endocrine systems, especially those associated with growth, glucose metabolism and reproduction.
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- "CgA is currently the best available biomarker for the diagnosis of neuroendocrine tumors [17, 22, 55]. The granin family comprises nine members including CgA and CgB, secretogranin (Sg) II, III, IV (HISL-19), V (7B2), VI (NESP55), VII (VGF), and proSAAS [15, 16, 18, 56]. Potential utility of CgB, SgII, and VGF nerve growth factor-inducible protein (VGF) as biomarkers of neurological and psychiatric disorders has been described . "
ABSTRACT: We used mass spectrometry-based protein identification to determine the presence of granins and other proteins in the mouse neuroblastoma secretome. We detected polypeptides derived from four members of the granin family: chromogranin A, chromogranin B, secretogranin III, and VGF. Many of them are derived from previously described biologically active regions; however, for VGF and CgB, we detected peptides not related to known bioactivities. Along with granins, we identified 115 other proteins secreted by mouse neuroblastoma cells, belonging to different functional categories. Fifty-six out of 119 detected proteins possess the signal fragments required for translocation into endoplasmic reticulum. Sequences of remaining 63 proteins were analyzed using SecretomeP algorithm to determine probability of nonclassical secretion. Identified proteins are involved in the regulation of cell cycle, proliferation, apoptosis, angiogenesis, proteolysis, and cell adhesion.
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