Effect of 67 kDa calcimedin on caldesmon functioning

Natalia V. Bogatcheva, Michail P. Panaiotov, Alexander V. Vorotnikov, Nikolai B. Gusev

Research output: Contribution to journalArticle

8 Scopus citations


Interaction of smooth muscle caldesmon with calmodulin, troponin C, S-100 protein and 67 kDa calcimedin was analyzed. Native gel electrophoresis and crosslinking revealed the complex formation between caldesmon and three EF-hand Ca-binding proteins, whereas calcimedin did not interact with caldesmon. In the presence of Ca2+, calcimedin binds to actin-tropomyosin without affecting the interaction of caldesmon with this complex. Although calcimedin reversed the inhibitory action of caldesmon on the actomyosin ATPase activity at a lower concentration than three other Ca-binding proteins, this effect only slightly depends on Ca2+ and was observed at the concentration of calcimedin comparable to that of actin. It is concluded that calcimedin itself cannot be responsible for Ca-dependent regulation of caldesmon functioning, but actin bundling induced by calcimedin (or by other actin binding proteins) decreases the inhibitory action of caldesmon on the actomyosin ATPase activity.

Original languageEnglish (US)
Pages (from-to)193-197
Number of pages5
JournalFEBS Letters
Issue number2
StatePublished - Dec 6 1993


  • Calcimedin
  • Caldesmon
  • Calmodulin
  • S-100
  • Troponin C

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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