American Journal of Physiology-Cell Physiology · 1986 · 154 citations · 31 references
Life SciencesPharmacologyPhysiologyCell SignalingMolecular PhysiologySignal TransductionMechanotransductionMuscle MechanicsMuscle MechanobiologyMuscle PhysiologyMuscle TissueTissue MechanicsCalcium Signaling In Muscle CellsMuscle Contractile FunctionMuscle ContractionMuscle Contraction MechanicsSkeletal Muscle ContractionSkeletal Muscle PhysiologySmooth Muscle ContractionVascular Smooth Muscle Regulation
We studied the contractile response to phorbol esters and its relationship to myosin light chain phosphorylation in intact and Triton X-100-skinned porcine carotid preparations. Muscle contraction was activated by phorbol 12,13-dibutyrate (PDBu) and phorbol 12,13-didecanoate (PDD). Dose-dependent contractions to PDBu were obtained both in the intact and skinned preparations. The maximal values of stress in response to PDBu were 1.11 +/- 0.10 X 10(5) N/m2 (n = 7) in the intact and 5.72 +/- 0.59 X 10(4) N/m2 (n = 10) in the skinned muscles. The skinned tissues responded to PDD, which has been shown to activate protein kinase C, but not to the inactive isomer 4 alpha-PDD, thus ruling out nonspecific phorbol effects. The phorbol ester response exhibited a Ca2+ dependence. High stresses in the skinned muscles (5.53 +/- 0.69 X 10(4) N/m2, n = 8) were associated with low values of myosin light chain phosphorylation (0.18 +/- 0.01 mol Pi/mol light chain, n = 8). Thus phorbol esters can contract vascular smooth muscle by a mechanism that is not proportional to myosin light chain phosphorylation and that may involve activation of protein kinase C.
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