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The purpose of this study was to test the hypothesis that the mechanical response of coronary smooth muscle following adrenergic receptor stimulation was mediated by changes in cyclic AMP content. Dibutyryl cyclic AMP caused relaxation of coronary artery strips. Aminophyline caused relaxation and a 254% elevation of cyclic AMP content (P less than 0.005). Phenylephrine caused contraction but no significant change in cyclic AMP content (P greater than 0.4). Epinephrine alone caused contraction and a 99% elevation of cyclic AMP content (P less than 0.001). The alpha blocker, phentolamine, reversed the mechanicaal response to epinephrine, but it did not significantly (P greater than 0.15) reduce the effect of epinephrine on cyclic AMP content. Propranolol enhanced the contractile response to epinephrine and attenuated the epinephrine-induced increase in cyclic AMP content. These results suggest that the contraction of coronary arteries associated with alpha-receptor stimulation is not mediated by changes in cyclic AMP content; however, relaxation associated with beta-receptor stimulation may be mediated by an increase in cyclic AMP content.

The purpose of this work was to test the hypothesis that stress relaxation (SR) in vascular smooth muscle is related to the amount of contractile activity (developed stress) and perhaps a property of the contractile element (CE). Using medial-intimal strips from the hog carotid artery, a strain (delta 1/l0, where l0 equals optimal length for force development) of 2% was applied at two different rates in the presence of various levels of developed or passive stress. Developed stress was altered either by changing the extracellular K-ion concentration with the strip length equal to l0 or by stimulating with a salt solution containing 30 mM KCl at various strip lengths. Passive stress was altered by varying strip length. At each level of developed or passive stress the magnitude of the increment in stress due to the strain (induced stress) and the SR were noted. SR varied directly with the magnitude of the developed stress, but there was a small and relatively unchanging amount of SR when passive stress was varied. At a given level of developed stress, the magnitude of SR was greater at a strain rate of 0.016 than at 0.001 l0/sec. When developed stress was altered, the magnitude of SR was essentially equal to the amount of induced stress; however, when passive stress was varied, SR was always less than induced stress. These observations are consistent with the hypothesis that, in the presence of developed stress, a large fraction of the SR represents the lengthening of the CE. This increased CE length allows a reequilibration of stress between the series elastic element and the contractile element. In the absence of developed stress, SR may represent a passive, physical property of this heterogeneous tissue.

Previous studies have shown that smooth muscle myosin consists of two heavy chains (MHCs) of unequal molecular weight; however, it is not clear whether there are intermuscle, inter- and intraspecies differences in the MHCs. The purpose of these experiments was to quantitatively and qualitatively compare MHCs in different smooth muscles. Extracts of bovine aorta (BAo), dog saphenous vein (dSV) and femoral artery (dFA), and rat aorta (rAo), femoral artery (rFA), carotid artery (rCA), ileum (rGI) and uterus (rUt) were electrophoresed on 5% polyacrylamide-1% SDS gels. All tissues exhibited two MHCs with molecular weights of 207,000 (MHC1) and 204,000 (MHC2) daltons. In all cases the proportion of total MHC made up by MHC1 was greater than that by MHC2. Based on their relative proportions (MHC1:MHC2), the tissues fell into one of three groups: (1) 55:45 - rAo, rCA, dFA; (2) 60:40 - dSV, BAo, rGI; and (3) 65:35 - rUt, rFA. Group 1 differed significantly from group 3 in the proportion of each MHC. One dimensional peptide maps indicated that BAo, dSV and dFA were similar while subtle differences existed between rUt and rAo. Differences between rUt and rAo were also observed in their cross-reactivity to a monoclonal antibody to smooth muscle MHC, confirming the differences seen on peptide maps. These results indicate that there are intertissue and inter- and intraspecies differences in smooth muscle MHCs. The significance of these differences to muscle function remains to be determined.