Novel mastoparan analogs induce differential secretion from mast cells.
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Abstract
Cationic amphiphilic peptides stimulate secretion via a receptor-independent action upon G proteins. We have previously utilized chimeric analogs of mastoparan (MP), including galparan (galanin(1-13)-MP ), as molecular probes of secretion. Here, we further resolve the structure-activity relationship of peptidyl secretagogs, including rationally designed chimeric MP analogs. The secretory efficacies of 10 MP analogs were significantly higher than 45 unrelated basic peptides. Comparative studies identified MP analogs that are differential secretagogs for 5-hydroxytryptamine (5-HT) and beta-hexosaminidase. Peptide-induced activation of phospholipase D (PLD), an enzyme intimately involved in regulated exocytosis [5], correlated with the secretion of beta-hexosaminidase but not 5-HT. Thus, these data indicate that different mechanisms are responsible for the exocytosis of 5-HT and beta-hexosaminidase, respectively. Moreover, mastoparan analogs are novel tools for probing the molecular details of exocytosis and other biological phenomena.Citation
Chemistry & Biology, 9(1): 63-70Publisher
Elsevier Science B.VType
Journal articleLanguage
enDescription
Metadata onlyISSN
10745521ae974a485f413a2113503eed53cd6c53
10.1016/S1074-5521(01)00098-9