Effects of nitric oxide on force-generating proteins of skeletal muscle

• Published in: Pflügers Archiv Vol. 434; no. 3; pp. 242 - 245
• Main Authors: Galler, S, Hilber, K, Göbesberger, A
• Format: Journal Article
• Language: English
• Published: Germany Springer Nature B.V 01.07.1997
• Subjects: Adenosine Triphosphatases - antagonists & inhibitors; Animals; Calcium - pharmacology; Enzyme Inhibitors - pharmacology; In Vitro Techniques; Kinetics; Muscle Contraction - drug effects; Muscle Contraction - physiology; Muscle Proteins - physiology; Muscle, Skeletal - drug effects; Muscle, Skeletal - physiology; Muscular system; Myofibrils - drug effects; Myofibrils - enzymology; Nitric Oxide - physiology; Nitroprusside - pharmacology; Penicillamine - analogs & derivatives; Penicillamine - pharmacology; Proteins; Rats; Rodents; S-Nitroso-N-Acetylpenicillamine; Skeletal system; Space life sciences
• ISSN: 0031-6768; 1432-2013
• DOI: 10.1007/s004240050391

Nitric oxide (NO) has recently been identified as a physiologically important intracellular messenger modulating the contractile activity of skeletal muscle [Kobzik L, Reid MB, Bredt DS, Stamler JS (1994) Nature 372: 546-548]. However, the mechanism of action of NO is not yet known. We used skinned (demembranated) muscle fibres to investigate the mechanism of NO function in muscle contraction. Maximally Ca2+-activated single fibres of rat skeletal muscle were exposed to physiologically relevant NO concentrations by adding NO donor molecules into the bath solution. Donor application caused a decline both in the contractile properties and in the myofibrillar adenosine triphosphatase (ATPase) activity. These results reveal a novel molecular mechanism of NO action: a direct inhibition of the force-generating proteins in skeletal muscle.