{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T09:34:03Z","timestamp":1777541643005,"version":"3.51.4"},"reference-count":41,"publisher":"American Physiological Society","issue":"5","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American Journal of Physiology-Gastrointestinal and Liver Physiology"],"published-print":{"date-parts":[[2002,5,1]]},"abstract":"<jats:p>Gastrin requires extensive posttranslational processing for full biological activity. It is presumed that progastrin is cleaved at pairs of basic amino acids by a prohormone convertase to form a glycine-extended intermediate (G-Gly) that serves as a substrate for peptidyl-glycine \u03b1-amidating monooxygenase (PAM), resulting in COOH-terminally amidated gastrin. To confirm the nature of progastrin processing in a primary cell line, we performed [<jats:sup>35<\/jats:sup>S]methionine-labeled pulse-chase biosynthetic experiments in canine antral G cells. Radiolabeled progastrin reached a peak earlier than observed for G-Gly or amidated gastrin. G-Gly radioactivity accumulated in G cells and preceded the appearance of radioactivity in amidated gastrin. The conversion of G-Gly to amidated gastrin was enhanced by the PAM cofactor ascorbic acid. To determine whether one member of the prohormone convertase family (PC2) was responsible for progastrin cleavage, G cells were incubated with PC2 antisense oligonucleotide probes. Cells treated with antisense probes had reduced PC2 expression, an accumulation of radiolabeled progastrin, and a delay in the formation of amidated gastrin. Progastrin in antral G cells is cleaved via PC2 to form G-Gly that is converted to amidated gastrin via the actions of PAM.<\/jats:p>","DOI":"10.1152\/ajpgi.00167.2001","type":"journal-article","created":{"date-parts":[[2015,3,3]],"date-time":"2015-03-03T19:55:15Z","timestamp":1425412515000},"page":"G766-G775","source":"Crossref","is-referenced-by-count":12,"title":["Gastrin biosynthesis in canine G cells"],"prefix":"10.1152","volume":"282","author":[{"given":"Vinzenz","family":"Stepan","sequence":"first","affiliation":[{"name":"Departments of Pediatrics and"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kentaro","family":"Sugano","sequence":"additional","affiliation":[{"name":"Internal Medicine, University of Michigan, Ann Arbor, Michigan 48109-0656;"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tadataka","family":"Yamada","sequence":"additional","affiliation":[{"name":"GlaxoSmithKline, King of Prussia, Pennsylvania 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