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Interaction between calponin and smooth muscle myosin
Author(s) -
Szymanski Pawel T.,
Tao Terence
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80348-x
Subject(s) - calponin , myosin , tropomyosin , actin , calmodulin , meromyosin , caldesmon , contractility , biophysics , chemistry , myosin light chain kinase , microbiology and biotechnology , muscle contraction , biology , myosin head , biochemistry , anatomy , endocrinology , enzyme
Calponin is a thin filament‐associated protein in smooth muscle that has been shown to bind actin, tropomyosin and calmodulin, and has been implicated to play a role in regulation of smooth muscle contractility. Using a centrifugation assay we found that calponin interacts with unphosphorylated filamentous smooth muscle myosin. We found that this calponin‐myosin interaction is reversed by Ca 2+ ‐CaM, and depends on ionic strength. At 50 mM NaCI the binding constant and the stoichiometry of this interaction were estimated to be 2 × 10 6 M −1 , and 1.2–2.4 calponin per myosin, respectively. We suggest that the calponin‐myosin interaction could be involved in regulation of smooth muscle contractility by anchoring myosin to actin.