ACTH-induced lipolysis in rat adipocytes: structure-activity relationships.
The lipolytic action of natural porcine ACTH1(-39) and of a number of highly purified synthetic ACTH peptide fragments was studied using rat adipocytes. Of the analogues tested, only ACTH1(-24) exhibited full lipolytic activity with respect to intrinsic activity and affinity. Several shorter fragments appeared to be full agonists but had lower affinity. Fragments ACTH5(-10) and ACTH7(-10) were inactive. No antagonistic effects against the lipolytic action of ACTH could be demonstrated with substimulatory doses of ACTH1(-16), ACTH1(-10), ACTH7(-24) and ACTH11(-24). Based on the relative potency derived from dose-response curves, a more refined model with respect to the active centers being encoded in various sequences of the hormone, is proposed.
D000273:Adipose Tissue / Q000187:drug effects / Q000378:metabolism*; D000324:Adrenocorticotropic Hormone / Q000031:analogs & derivatives / Q000494:pharmacology*; D000818:Animals; D066298:In Vitro Techniques; D050356:Lipid Metabolism; D008297:Male; D010446:Peptide Fragments / Q000494:pharmacology; D051381:Rats; D013329:Structure-Activity Relationship
D010446:Peptide Fragments; D000324:Adrenocorticotropic Hormone