Phosphorylation-dependent Autoinhibition of Myosin Light Chain Phosphatase Accounts for Ca Sensitization Force of Smooth Muscle Contraction*
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چکیده
Alexander Khromov, Nandini Choudhury, Andra S. Stevenson, Avril V. Somlyo, and Masumi Eto From the Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, Virginia 22908 and the Department of Molecular Physiology and Biophysics and Kimmel Cancer Center, Thomas Jefferson University, Jefferson Medical College, Philadelphia, Pennsylvania 19107
منابع مشابه
Phosphorylation-dependent autoinhibition of myosin light chain phosphatase accounts for Ca2+ sensitization force of smooth muscle contraction.
The reversible regulation of myosin light chain phosphatase (MLCP) in response to agonist stimulation and cAMP/cGMP signals plays an important role in the regulation of smooth muscle (SM) tone. Here, we investigated the mechanism underlying the inhibition of MLCP induced by the phosphorylation of myosin phosphatase targeting subunit (MYPT1), a regulatory subunit of MLCP, at Thr-696 and Thr-853 ...
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Intracellular calcium concentration ([Ca2+]i)-dependent activation of myosin light chain kinase and its phosphorylation of the 20-kd light chain of myosin is generally considered the primary mechanism responsible for regulation of contractile force in arterial smooth muscle. However, recent data suggest that the relation between [Ca2+]i and myosin light chain phosphorylation is variable and dep...
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An increase in intracellular Ca(2+) is the primary trigger of contraction of gastrointestinal (GI) smooth muscles. However, increasing the Ca(2+) sensitivity of the myofilaments by elevating myosin light chain phosphorylation also plays an essential role. Inhibiting myosin light chain phosphatase activity with protein kinase C-potentiated phosphatase inhibitor protein-17 kDa (CPI-17) and myosin...
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تاریخ انتشار 2009