Selective activation and inhibition of calmodulin-dependent enzymes by a calmodulin-like protein found in human epithelial cells

Eur J Biochem. 1994 Dec 1;226(2):725-30. doi: 10.1111/j.1432-1033.1994.tb20101.x.

Abstract

A calmodulin-like protein, which is identical in size and 85% identical to vertebrate calmodulin, was recently identified by 'subtractive hybridization' comparison of transcripts expressed in normal versus transformed human mammary epithelial cells. Unlike the ubiquitous distribution of calmodulin, calmodulin-like protein expression is restricted to certain epithelial cells, and appears to be modulated during differentiation. In addition, calmodulin-like protein levels are often significantly reduced in malignant tumor cells as compared to corresponding normal epithelial cells. The current studies compare calmodulin-like protein functions with those of calmodulin. We find that calmodulin-like protein activation of multifunctional Ca2+/calmodulin-dependent protein kinase II (calmodulin kinase II) is equivalent to activation by calmodulin, but that four other calmodulin-dependent enzymes, cGMP phosphodiesterase, calcineurin, nitric-oxide synthase, and myosin-light-chain kinase, display much weaker activation by calmodulin-like protein than by calmodulin. In the case of myosin-light-chain kinase, calmodulin-like protein competitively inhibits calmodulin activation of the enzyme with a Ki value of 170 nM. Thus, calmodulin-like protein may have evolved to function as a specific agonist of certain calmodulin-dependent enzymes, and/or as a specific competitive antagonist of other calmodulin-dependent enzymes.

Publication types

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

MeSH terms

  • 3',5'-Cyclic-GMP Phosphodiesterases / antagonists & inhibitors
  • 3',5'-Cyclic-GMP Phosphodiesterases / metabolism
  • Amino Acid Oxidoreductases / antagonists & inhibitors
  • Amino Acid Oxidoreductases / metabolism
  • Amino Acid Sequence
  • Binding, Competitive
  • Breast
  • Calcineurin
  • Calcium-Binding Proteins / chemistry
  • Calcium-Binding Proteins / metabolism
  • Calcium-Binding Proteins / pharmacology*
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2
  • Calcium-Calmodulin-Dependent Protein Kinases / antagonists & inhibitors
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism
  • Calmodulin / chemistry
  • Calmodulin / metabolism
  • Calmodulin / pharmacology*
  • Calmodulin-Binding Proteins / antagonists & inhibitors
  • Calmodulin-Binding Proteins / metabolism
  • Cells, Cultured
  • Chromatography, Affinity
  • Enzyme Activation / drug effects*
  • Enzyme Inhibitors*
  • Epithelium / chemistry
  • Female
  • Humans
  • Molecular Sequence Data
  • Myosin-Light-Chain Kinase / antagonists & inhibitors
  • Myosin-Light-Chain Kinase / metabolism
  • Nitric Oxide Synthase
  • Phosphoprotein Phosphatases / antagonists & inhibitors
  • Phosphoprotein Phosphatases / metabolism

Substances

  • Calcium-Binding Proteins
  • Calmodulin
  • Calmodulin-Binding Proteins
  • Enzyme Inhibitors
  • Nitric Oxide Synthase
  • Amino Acid Oxidoreductases
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Myosin-Light-Chain Kinase
  • Calcineurin
  • Phosphoprotein Phosphatases
  • 3',5'-Cyclic-GMP Phosphodiesterases