Molecular cloning and characterization of a Ca2+/calmodulin-insensitive adenylyl cyclase from rat brain

Paul G. Feinstein, Karen A. Schrader, Heather A. Bakalyar, Wei Jen Tang, John Krupinski, Alfred G. Gilman, Randall R. Reed

Research output: Contribution to journalArticle

219 Scopus citations

Abstract

Biochemical, immunological, and molecular cloning studies have suggested the existence of multiple forms of adenylyl cyclase (EC 4.6.1.1). An adenylyl cyclase cDNA clone (type II) was isolated from a rat brain library and found to encode a protein of 1090 amino acids that was homologous to but distinct from the previously described Ca2+ / calmodulin-stimulated adenylyl cyclase from bovine brain. Expression of the type II cDNA in an insect cell line resulted in an increased level of adenylyl cyclase activity that was insensitive to Ca2+ / calmodulin. Addition of activated G protein to type II-containing membranes increased enzyme activity. The mRNA encoding the type II protein was expressed at high levels in brain tissue and at low levels in olfactory epithelium and lung. The existence of multiple adenylyl cyclase enzymes may provide for complex and distinct modes of biochemical regulation of cAMP levels in the brain. (.

Original languageEnglish (US)
Pages (from-to)10173-10177
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume88
Issue number22
DOIs
StatePublished - Jan 1 1991

Keywords

  • Cyclic AMP
  • Guanine nucleotide-binding protein
  • Signal transduction

ASJC Scopus subject areas

  • General

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