{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,20]],"date-time":"2026-02-20T22:48:25Z","timestamp":1771627705069,"version":"3.50.1"},"reference-count":0,"publisher":"American Diabetes Association","issue":"5","content-domain":{"domain":["diabetesjournals.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1991,5,1]]},"abstract":"<jats:p>We examined the in vivo mechanisms of amylin-induced resistance in concious rats (n = 18). During 180-min euglycemic insulin-clamp (21.5 pmol \u00b7 kg\u22121 \u00b7 min\u22121) studies, amylin (50, 200, or 500 pmol \u00b7 kg\u22121 \u00b7 min\u22121; plasma concentration from 3 \u00d7 10\u221210 to 9 \u00d7 10\u22129 M) infusion determined a 19\u201327% reduction in glucose uptake (117.8 \u00b1 7.0 vs. 145.8 \u00b1 11.0, 107.1 \u00b1 9.2 vs. 145.1 \u00b1 6.7, and 105.0 \u00b1 7.2 vs. 144.4 \u00b1 7.0 \u03bcmol \u00b7 kg\u22121 \u00b7 min\u22121 at 50, 200, or 500 pmol \u00b7 kg\u22121 \u00b7 min\u22121, respectively, P &amp;lt; 0.01) versus insulin alone, whereas 10-pmol \u00b7 kg\u22121 \u00b7 min\u22121 amylin infusion (plasma concn 5 \u00d7 10\u221211 M) failed to affect insulin-mediated glucose disposal. After amylin infusion, the contribution of whole-body glycolysis to overall glucose disposal increased from 43\u201348 to 62\u201379%, whereas muscle glycogen synthesis decreased significantly at all peptide concentrations &amp;gt;3 \u00d7 10\u221210 M, completely accounting for the decrease in glucose uptake. Skeletal muscle glucose-6-phosphate concentration rose from 0.219 \u00b1 0.038 \u03bcmol\/g (insulin alone) to 0.350 \u00b1 0.018, 0.440 \u00b1 0.020, and 0.505 \u00b1 0.035 \u03bcmol\/g (insulin plus amylin at 50, 200, or 500 pmol \u00b7 kg\u22121 \u00b7 min\u22121, P &amp;lt; 0.01). Suppression of hepatic glucose production by insulin was unaffected by a 50-pmol \u00b7 kg\u22121 \u00b7 min\u22121 amylin infusion (18.5 \u00b1 4.3 vs. 21.7 \u00b1 2.9 \u03bcmol \u00b7 kg\u22121 \u00b7 min\u22121), whereas it was slightly but significantly impaired by amylin infusion at 200 pmol \u00b7 kg\u22121 \u00b7 min\u22121 (17.8 \u00b1 3.9 vs. 24.7 \u00b1 4.5 \u03bcmol \u00b7 kg\u22121 \u00b7 min\u22121, P &amp;lt; 0.05). whereas peripheral glucose uptake and muscle glycogen synthesis were not further reduced. Our results suggest that amylin antagonizes the ability of insulin to promote total-body glucose uptake primarily by decreasing muscle glycogen synthesis, which, in turn, determines an increase in muscle glucose-6-phosphate levels and glycolysis and a reduction in glucose transport\/phosphorylation.<\/jats:p>","DOI":"10.2337\/diab.40.5.568","type":"journal-article","created":{"date-parts":[[2013,9,19]],"date-time":"2013-09-19T17:22:06Z","timestamp":1379611326000},"page":"568-573","update-policy":"https:\/\/doi.org\/10.2337\/ada-journal-policies","source":"Crossref","is-referenced-by-count":75,"title":["In Vivo Insulin Resistance Induced by Amylin Primarily Through Inhibition of Insulin-Stimulated Glycogen Synthesis in Skeletal Muscle"],"prefix":"10.2337","volume":"40","author":[{"given":"Simona","family":"Frontoni","sequence":"first","affiliation":[{"name":"Department of Medicine, University of Texas Health Science Center\u2008San Antonio, Texas"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Soo Bong","family":"Choi","sequence":"additional","affiliation":[{"name":"Department of Medicine, University of Texas Health Science Center\u2008San Antonio, Texas"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Donna","family":"Banduch","sequence":"additional","affiliation":[{"name":"Department of Medicine, University of Texas Health Science Center\u2008San Antonio, Texas"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Luciano","family":"Rossetti","sequence":"additional","affiliation":[{"name":"Department of Medicine, University of Texas Health Science Center\u2008San Antonio, Texas"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1167","container-title":["Diabetes"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.org\/diabetes\/diabetes\/article-pdf\/40\/5\/568\/336643\/40-5-568.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/diabetesjournals.org\/diabetes\/article-pdf\/40\/5\/568\/336643\/40-5-568.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,11,2]],"date-time":"2022-11-02T16:18:41Z","timestamp":1667405921000},"score":1,"resource":{"primary":{"URL":"https:\/\/diabetesjournals.org\/diabetes\/article\/40\/5\/568\/7641\/In-Vivo-Insulin-Resistance-Induced-by-Amylin"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1991,5,1]]},"references-count":0,"journal-issue":{"issue":"5","published-print":{"date-parts":[[1991,5,1]]}},"URL":"https:\/\/doi.org\/10.2337\/diab.40.5.568","relation":{},"ISSN":["0012-1797","1939-327X"],"issn-type":[{"value":"0012-1797","type":"print"},{"value":"1939-327X","type":"electronic"}],"subject":[],"published":{"date-parts":[[1991,5,1]]}}}