Myosin light chain phosphorylation associated with contraction in arterial smooth muscle

• Published in: The American journal of physiology Vol. 240; no. 5; pp. C222 - C233
• Main Authors: Driska, S P, Aksoy, M O, Murphy, R A
• Format: Journal Article
• Language: English
• Published: United States 01-05-1981
• Subjects: Actomyosin - metabolism; Animals; Calcium - physiology; Carotid Arteries - metabolism; Electrophoresis, Polyacrylamide Gel; In Vitro Techniques; Isoelectric Focusing; Muscle Contraction; Muscle, Smooth - metabolism; Muscle, Smooth - physiology; Muscle, Smooth, Vascular - metabolism; Myosins - metabolism; Peptide Fragments; Phosphorylation; Swine
• ISSN: 0002-9513
• DOI: 10.1152/ajpcell.1981.240.5.c222

The hypothesis that Ca2+ initiates contraction in smooth muscle by activating an endogenous myosin light chain kinase (MLCK) that phosphorylates the 20,000 dalton light chain (LC 20) of myosin was tested in tissues prepared from the media of swine carotid arteries. Unstimulated tissues with low levels of tone exhibited low levels of phosphorylated LC 20. On stimulation with a high-K+ physiological salt solution containing 1.6 mM CaCl2, LC 20 phosphorylation increased to 0.6 mol P/mol LC 20 within 30 s. This increase preceded force development, which required 2-4 min to attain a maximum steady-state value of 3.34 +/- 0.15 (SE) X 10(5) N/m2. These results support the hypothesis, as the stimulus was submaximal for the preparation. However, LC 20 phosphorylation declined significantly from its peak value before steady-state force was attained, reaching near control levels after 10 min of stimulation. The results suggest that Ca2+-stimulated LC 20 phosphorylation is an important physiological control mechanism but that additional factors are involved in the maintenance of tonic isometric force.