Interaction of calcium-binding proteins with calmodulin-dependent guanylate cyclase in Tetrahymena plasma membrane

Comp Biochem Physiol B. 1985;80(3):495-8. doi: 10.1016/0305-0491(85)90279-2.

Abstract

Addition of bovine brain calmodulin and S-100 inhibited Tetrahymena calmodulin-induced stimulation of guanylate cyclase, but they did not affect enzymatic activity in the presence of calcium alone. Troponin C shows little effect on the cyclase activity regardless of the presence or absence of Tetrahymena calmodulin. The inhibitory effects of brain calmodulin and S-100 were overcome by the addition of Tetrahymena calmodulin, but not by calcium. Both calmodulins from Tetrahymena and bovine brain elicited stimulation of heart phosphodiesterase, while troponin C and S-100 did not affect the phosphodiesterase activity in the presence and absence of Tetrahymena calmodulin.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Brain Chemistry
  • Calcium / pharmacology
  • Calcium-Binding Proteins / pharmacology
  • Calmodulin / pharmacology*
  • Cattle
  • Cell Membrane / enzymology
  • Guanylate Cyclase / antagonists & inhibitors
  • Guanylate Cyclase / metabolism*
  • S100 Proteins / pharmacology
  • Tetrahymena pyriformis / enzymology*
  • Troponin / pharmacology
  • Troponin C

Substances

  • Calcium-Binding Proteins
  • Calmodulin
  • S100 Proteins
  • Troponin
  • Troponin C
  • Guanylate Cyclase
  • Calcium