Melanophore pigment dispersion responses to agonists show two patterns of sensitivity to inhibitors of cAMP-dependent protein kinase and protein kinase C

Timothy S. Mcclintock, Joshua P. Rising, Michael R. Lerner

Research output: Contribution to journalArticlepeer-review

27 Scopus citations

Abstract

Melanophore pigment dispersion is a sensitive bioassay for activation of the adenylyl cyclase and phospholipase C second-messenger pathways. The necessity of protein kinase activation in causing pigment dispersion was confirmed for eight agonists of endogenous melanophore receptors and for two transfected receptors. All agonists and receptors previously shown to elevate intracellular cAMP in melanophores-melanocyte stimulating hormone, light, (-) norepinephrine, 5-hydroxytryptamine, and the β2-adrenergic receptor - were able to stimulate pigment dispersion in the presence of Ro31-8220, a potent inhibitor of protein kinase C, but were blocked in the presence of H89, an inhibitor of cAMP-dependent protein kinase. The bombesin receptor, which elevates intracellular IP3 in melanophores, was unable to stimulate pigment dispersion in the presence of Ro31-8220 or H89. Agonists whose mechanism of activation of pigment dispersion are unknown were also tested. Endothelin 3 responses were blocked by both H89 and Ro31-8220, predicting coupling to phospholipase C. Vasoactive intestinal polypeptide, oxytocin, and calcitonin gene-related peptide β responses were blocked only by H89, predicting coupling to adenylyl cyclase.

Original languageEnglish
Pages (from-to)1-7
Number of pages7
JournalJournal of Cellular Physiology
Volume167
Issue number1
DOIs
StatePublished - Apr 1996

ASJC Scopus subject areas

  • Physiology
  • Clinical Biochemistry
  • Cell Biology

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