S100 alpha, CAPL, and CACY: molecular cloning and expression analysis of three calcium-binding proteins from human

D Engelkamp1, B W Schäfer, P Erne

  • 1Department of Pediatrics, University of Zurich, Switzerland.

Biochemistry
|October 27, 1992
PubMed

Insights

Researchers identified three S100 family calcium-binding proteins (S100 alpha, CACY, and CAPL) in the human heart. Their expression patterns in human tissues differ from those in rodents, offering insights into myocardial dysfunction.

Area of Science:

  • Molecular biology
  • Cardiology
  • Biochemistry

Background:

  • Elevated intracellular calcium levels contribute to myocardial dysfunction.
  • S100 proteins are a family of EF-hand calcium-binding proteins implicated in cellular processes.

Purpose of the Study:

  • To identify potential mediators of deregulated calcium in the heart.
  • To investigate the expression patterns of S100 family proteins in human tissues.

Main Methods:

  • Polymerase Chain Reaction (PCR) technology to identify S100 family members.
  • Cloning of complementary DNAs (cDNAs).
  • Northern blot analysis to examine mRNA expression levels in various human tissues.

Main Results:

  • Three S100 family members (S100 alpha, CACY, and CAPL) were identified in the human heart.
  • All three proteins were found at high levels in the human heart.
  • CACY and CAPL mRNAs showed ubiquitous expression, while S100 alpha mRNA was restricted to heart, skeletal muscle, and brain.
  • Significant differences were observed in the expression patterns of these proteins between human and rodent tissues.

Conclusions:

  • S100 alpha, CACY, and CAPL are expressed in the human heart.
  • The distinct tissue distribution of these proteins, particularly S100 alpha, may play a role in cardiac function.
  • Human and rodent S100 protein expression patterns diverge, highlighting species-specific regulation relevant to cardiovascular research.