Interaction of smooth muscle calponin and desmin.

Interaction of smooth-muscle calponin and desmin was analyzed by means of ultracentrifugation, fluorescent spectroscopy and affinity chromatography. At low and intermediate ionic strength (30-50 mM NaCl) calponin is cosedimented with desmin with an apparent dissociation constant 3-15 microM and stoichiometry of 1 calponin/4-6 desmin. Calmodulin decreases the quantity of calponin bound to desmin. Increase of ionic strength up to 150 mM weakens calponin-desmin interaction, but even at this ionic strength part of calponin remains bound to desmin. Calponin increases the rate and extent of fluorescence quenching induced by polymerization of 5-iodoacetamidofluorescein-labeled desmin. Affinity chromatography data indicate that desmin-binding sites are located in the N-terminal 22 kDa fragment of calponin. Since calponin interacts with desmin with an affinity comparable with that of, e.g., tropomyosin and myosin we suppose that calponin-desmin interaction may be important for cytoskeleton organization.