Adenosine and divalent cation effects on S-91 melanoma adenylate cyclase

Marvin D. Bregman, Tomi K. Sawyer, Mac E. Hadley, Victor J. Hruby

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

Adenosine inhibits S-91 melanoma membrane adenylate cyclase. This inhibition is observed with all activators tested; α-melanocyte-stimulating hormone, [norleucine4]α-melanocyte-stimulating hormone, prostaglandin-E2, and fluoride ion. This inhibition is also observed with the ribose modified adenosine analog adenine-9-β-d-arabinofuranoside. However, "R" site (stringent for the ribose moiety) analogs such as 2-chloroadenosine and 6-methyladenosine were without effect. Addition of manganous ion (Mn2+), a potent activator of adenylate cyclase, markedly enhances the inhibition by adenosine. The nucleoside specificity, Mn2+ requirement, and lack of reversal by the potent R-site antagonist, 3-isobutyl-1-methylxanthine, suggest that the S-91 melanoma membrane adenylate cyclase system contains only P-type (stringent for purine moiety) receptor sites.

Original languageEnglish (US)
Pages (from-to)1-7
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume201
Issue number1
DOIs
StatePublished - Apr 15 1980

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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