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- W2262621849 abstract "The most defining feature of differentiated vascular smooth muscle is the ability to contract and relax by the process of excitation-contraction coupling.There is enormous heterogeneity in the molecular and cellular physiology of vascular smooth muscle that is evident in different vascular beds and in conduit compared to resistance arteries.Thin filaments are composed of actin, tropomyosin, and specific thin filament-binding proteins caldesmon and calponin.Caldesmon and calponin are negative modulators; thus, when inhibited by vasoconstrictor-induced phosphorylation, these proteins will increase contractile force.Binding of Ca2+-calmodulin to myosin light chain kinase activates the kinase that, in turn, phosphorylates the regulatory light chains of myosin.Independent regulation of myosin light chain kinase and myosin phosphatase by different contractile agonists is a mechanism for modulating the Ca2+ sensitivity of vascular muscle tone.Ca2+-induced Ca2+ release (CICR) does not elicit increases in global Ca2+ in vascular smooth muscle; however, CICR is essential for localized Ca2+ gradients, “Ca2+ sparks,” which most profoundly activate K+ channels in the form of spontaneous transient outward currents (STOCs).The earlier concept of global cytoplasmic Ca2+ being a regulator of contraction and other cellular functions has undergone a transformation to the concept that localized Ca2+ signaling is the main regulator of many functions of the differentiated vascular myocyte.Pharmacomechanical coupling is contraction in the absence of a change in membrane potential and can occur via inositol-1,4,5-triphosphate (IP3)-mediated Ca2+ release or Ca2+ influx through ligand-gated channels.Vascular smooth muscle contains a rhoA-regulated rhokinase that phosphorylates and inactivates myosin phosphatase, thereby increasing contractile force." @default.
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- W2262621849 date "2007-01-01" @default.
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- W2262621849 title "Molecular and Cellular Physiology of Differentiated Vascular Smooth Muscle" @default.
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- W2262621849 doi "https://doi.org/10.1007/978-1-84628-715-2_72" @default.
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