title: Force-generating capacity and contractile protein content of arterial smooth muscle.
abstract: After correction for extracellular space (40%) determined from electron micrographs, the maximum isometric force developed by strips prepared from the media of the hog carotid artery (2.2 x 10(6) dyn/cm(2)) can be extrapolated to give a value of 3.7 x 10(6) dyn/cm(2) for the smooth muscle component of the strip. Three independent estimates of the myosin content of the smooth muscle cells were made based on (a) exhaustive extraction and purification with estimates of preparative losses, (b) the myosin catalyzed ATPase activity of media homogenates, and (c) quantitative densitometry of the peaks containing myosin, actin, and tropomyosin after disk electrophoresis of sodium dodecyl sulfate-treated media homogenates. The results were consistent and gave a myosin content of 5-10 mg/g media, or 8-17 mg/g cell. Method (c) gave myosin:actin:tropomyosin weight ratios of 1:3.2:0.8. Although measured force developed by the smooth muscle cell exceeds that of mammalian striated muscle, the myosin content in smooth muscle is about five times lower. The actin content of smooth muscle is relatively high. The actin and myosin contents are consistent with thick and thin filament ratios observed in electron micrographs of vascular smooth muscle.
mesh_terms: D000199:Actins / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D002339:Carotid Arteries; D003720:Densitometry; D004548:Elasticity; D004589:Electrophoresis, Disc; D009124:Muscle Proteins / Q000378:metabolism*; D009130:Muscle, Smooth / Q000201:enzymology / Q000378:metabolism / Q000502:physiology*; D009218:Myosins / Q000378:metabolism; D013552:Swine
chemical_list: D000199:Actins; D009124:Muscle Proteins; D000251:Adenosine Triphosphatases; D009218:Myosins