Cellular thin filament protein contents and force generation in porcine arteries and veins.
We estimated the cellular myosin, actin, and tropomyosin contents of vascular smooth muscle from (1) seven major arteries, (2) seven large veins, and (3) the first through third order branches of the uterine vasculature to determine whether variations in the contractile apparatus contribute to the functional diversity of vascular smooth muscle. We obtained the estimates by quantitative densitometry of stained polyacrylamide gels after electrophoresis of sodium dodecyl sulfate-treated tissue homogenates. No differences in cellular myosin content were found (18.7 +/- 1.0 mg/g cell wet weight in arteries vs. 17.2 +/- 0.7 in veins). However, the actin and tropomyosin contents were higher in arteries (49.7 +/- 2.9 and 13.1 +/- 0.8 mg/g cell, respectively) than in veins (25.5 +/- 1.4 and 7.0 +/- 0.3 mg/g cell). These differences persisted in the smaller uterine vessels. The higher contents of thin filament proteins in arteries, compared with veins and several other smooth muscle tissues previously studied, may underlie the high force generating capacity of arterial smooth muscle.
D000199:Actins; D000818:Animals; D001158:Arteries / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D009124:Muscle Proteins; D009130:Muscle, Smooth / Q000032:analysis / Q000166:cytology*; D009218:Myosins; D013552:Swine; D014335:Tropomyosin; D014599:Uterus / Q000098:blood supply; D014680:Veins / Q000032:analysis
D000199:Actins; D009124:Muscle Proteins; D014335:Tropomyosin; D009218:Myosins