Mechanism of cerebral vasospasm--contractile proteins in smooth muscle of bovine cerebral artery.

Understanding of the pathogenesis of cerebral vasospasm requires basic study of the contraction mechanism of cerebral arteries. In this study, the morphological and biochemical properties of actomyosin from bovine cerebral arteries were examined. Arrays of thick and thin filaments were clearly seen on electron micrographs of a cross section of a muscle strip stretched to 1.5 times its normal length in Krebs-Ringer solution. The diameters of the thick and thin filaments were 110.0 ± 19.9 A and 51.0 ± 8.0 A, respectively. The average ratio of thick to thin filaments was about 1:15 to 1:16. The gel pattern of Ca2+-sensitive actomyosin extracted from bovine cerebral arteries revealed the presence of myosin, actin, and tropomyosin, but not skeletal troponin. The Mg-ATPase activity of actomyosin was greatly enhanced in the presence of Ca2+. Rapid superprecipitation occurred after the clearing phase, when 1 mM Mg-ATP was added to a suspension of actomyosin with 10-5 M Ca2+. This superprecipitation did not occur with a lower Ca2+ concentration of 10-8 M. Intracellular free Ca2+ appears to play a crucial role in the regulation of contraction and relaxation of cerebral arterial smooth muscle.