Role of contractile protein activation in the length-dependent modulation of tracheal smooth muscle force

• Published in: The American journal of physiology Vol. 270; no. 1 Pt 1; p. C243
• Main Authors: Mehta, D, Wu, M F, Gunst, S J
• Format: Journal Article
• Language: English
• Published: United States 01.01.1996
• Subjects: Acetylcholine - pharmacology; Animals; Calcium - metabolism; Contractile Proteins - physiology; Dogs; In Vitro Techniques; Intracellular Membranes - metabolism; Isometric Contraction; Muscle Contraction - physiology; Muscle, Smooth - drug effects; Muscle, Smooth - physiology; Myosin Light Chains - metabolism; Osmolar Concentration; Phosphorylation; Potassium Chloride - pharmacology; Trachea - drug effects; Trachea - physiology
• ISSN: 0002-9513; 2163-5773
• DOI: 10.1152/ajpcell.1996.270.1.c243

The active isometric force developed by a muscle decreases at muscle lengths below an optimal length (Lo). However, when the length of an actively contracting muscle is abruptly decreased, a lower level of isometric force is reached during force redevelopment than when the contraction is initiated at the shorter length. This has been attributed to a deactivation of contractile proteins caused by shortening. In this study, intracellular Ca2+ and myosin light chain (MLC) phosphorylation were measured to assess the mechanisms for the modulation of isometric force caused by changing smooth muscle length before or during isometric contraction. The decline in isometric force between Lo and 0.5Lo was associated with decreases in MLC phosphorylation and intracellular Ca2+ during contractions elicited by acetylcholine or 60 mM KCl. Quick release of the muscle during contraction depressed force redevelopment at the shorter length but not MLC phosphorylation. We conclude that decreases in Ca(2+)-calmodulin-dependent MLC phosphorylation contribute significantly to the decline in isometric force at lengths below Lo, but the depression of contractility associated with the quick release of actively contracted smooth muscle is not caused by a shortening-induced deactivation of contractile proteins.