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The maximal velocity of vascular smooth muscle shortening is independent of the expression of calponin

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Abstract

In smooth muscle, the phosphorylation/dephosphorylation of the 20-kDa regulatory light chain of myosin (MLC20) is known to regulate actomyosin interaction and force. However, a thin filament based regulatory system for actomyosin interaction has been suggested to exist in parallel to MLC20 phosphorylation. Calponin is a thin filament associated protein that in vitro inhibits actomyosin interaction, and has been suggested to reduce maximal shortening velocity (v max). Using antibodies to h1- and h2-calponin, we demonstrated that calponin was present in smooth muscle from Sprague Dawley (SD) rats, while calponin was not detectable in the smooth muscle from Wistar Kyoto (WKY) rats. v max determined from the force vs. velocity relationship at maximal Ca2+ activation was not different for either the aorta or the portal vein of SD vs. WKY rats. These results suggest that physiological levels of calponin do not contribute to a thin filament-based secondary regulation to inhibit smooth muscle contraction.

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Authors and Affiliations

  1. Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH, 44106-4970, USA

    Carie Facemire, Frank V. Brozovich & Jian-Ping Jin

  2. Department of Medicine (Cardiology), Case Western Reserve University, Cleveland, OH, 44106-4970, USA

    Frank V. Brozovich

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  1. Carie Facemire
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  2. Frank V. Brozovich
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  3. Jian-Ping Jin
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Facemire, C., Brozovich, F.V. & Jin, JP. The maximal velocity of vascular smooth muscle shortening is independent of the expression of calponin. J Muscle Res Cell Motil 21, 367–373 (2000). https://doi.org/10.1023/A:1005680614296

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