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Phosphorylation of caldesmon by mitogen‐activated protein kinase with no effect on Ca2+ sensitivity in rabbit smooth muscle.
77
Citations
19
References
1995
Year
Muscle FunctionRelaxed Smooth MuscleMechanotransductionBiomedical EngineeringTonic Smooth MuscleCellular PhysiologyMuscle PhysiologyCa2+ SensitivityCell SignalingHealth SciencesMolecular PhysiologyBiochemistryMitogen‐activated Protein KinaseVascular PharmacologyIon ChannelsVascular BiologyProtein PhosphorylationSignal TransductionPhysiologyCardiovascular PhysiologyRabbit Smooth MuscleCellular BiochemistryTriton X-100Medicine
1. Recombinant, activated mitogen-activated protein kinase (3.3 microM; p42mapk) phosphorylated caldesmon in phasic (rabbit portal vein) and tonic (rabbit femoral artery) smooth muscle strips permeabilized with Triton X-100. 2. Phosphorylation of caldesmon by p42mapk neither induced contraction of relaxed smooth muscle nor affected the Ca2+ sensitivity of submaximally contracted permeabilized phasic or tonic smooth muscle.
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