{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,20]],"date-time":"2026-09-20T07:03:34Z","timestamp":1789887814452,"version":"4.0.1"},"reference-count":94,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2006,5,18]],"date-time":"2006-05-18T00:00:00Z","timestamp":1147910400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Diabetes Obesity Metabolism"],"published-print":{"date-parts":[[2006,11]]},"abstract":"<jats:p>\n                    Chromogranins or secretogranins (granins), present in secretory granules of virtually all neuroendocrine cells and neurones, are structurally related proteins encoded by different genetic loci: chromogranins A and B, and secretogranins II through VI. Compelling evidence supports both intracellular and extracellular functions for this protein family. Within the cells of origin, a granulogenic or sorting role in the regulated pathway of hormone or neurotransmitter secretion has been documented, especially for chromogranin A (CHGA). Granins also function as pro\u2010hormones, giving rise by proteolytic processing to an array of peptide fragments for which diverse autocrine, paracrine, and endocrine activities have been demonstrated. CHGA measurements yield insight into the pathogenesis of such human diseases as essential hypertension, in which deficiency of the catecholamine release\u2010inhibitory CHGA fragment catestatin may trigger sympathoadrenal overactivity as an aetiologic culprit in the syndrome. The CHGA dysglycaemic fragment pancreastatin is functional in humans\n                    <jats:italic>in vivo<\/jats:italic>\n                    , affecting both carbohydrate (glucose) and lipid (fatty acid) metabolism. Pancreastatin is cleaved from CHGA in hormone storage granules\n                    <jats:italic>in vivo<\/jats:italic>\n                    , and its plasma concentration varies in human disease. The pancreastatin region of CHGA gives rise to three naturally occurring human variants, one of which (Gly297Ser) occurs in the functionally important carboxy\u2010terminus of the peptide, and substantially\n                    <jats:italic>increases<\/jats:italic>\n                    the peptide\u2019s potency to inhibit cellular glucose uptake. These observations establish a role for pancreastatin in human intermediary metabolism and disease, and suggest that qualitative hereditary alterations in pancreastatin\u2019s primary structure may give rise to interindividual differences in glucose disposition.\n                  <\/jats:p>","DOI":"10.1111\/j.1463-1326.2006.00575.x","type":"journal-article","created":{"date-parts":[[2006,5,18]],"date-time":"2006-05-18T11:14:22Z","timestamp":1147950862000},"page":"621-633","source":"Crossref","is-referenced-by-count":29,"title":["Catecholamine storage vesicles and the metabolic syndrome: the role of the chromogranin A fragment pancreastatin"],"prefix":"10.1111","volume":"8","author":[{"given":"Kuixing","family":"Zhang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fangwen","family":"Rao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gen","family":"Wen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rany M.","family":"Salem","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sucheta","family":"Vaingankar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Manjula","family":"Mahata","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nitish R.","family":"Mahapatra","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elizabeth O.","family":"Lillie","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter E.","family":"Cadman","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ryan S.","family":"Friese","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bruce A.","family":"Hamilton","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vivian Y.","family":"Hook","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sushil K.","family":"Mahata","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laurent","family":"Taupenot","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel T.","family":"O\u2019Connor","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2006,5,18]]},"reference":[{"key":"e_1_2_12_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/0306-4522(80)90031-7"},{"key":"e_1_2_12_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/0306-4522(76)90001-4"},{"key":"e_1_2_12_4_2","doi-asserted-by":"publisher","DOI":"10.1097\/00004872-198803000-00002"},{"key":"e_1_2_12_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)50695-0"},{"key":"e_1_2_12_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/0024-3205(83)90721-X"},{"issue":"5","key":"e_1_2_12_7_2","doi-asserted-by":"crossref","first-page":"3237","DOI":"10.1016\/S0021-9258(17)43286-8","article-title":"Chromogranin A, the major catecholamine storage vesicle soluble protein. 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