G-protein-mediated Ca2+ sensitization of smooth muscle contraction through myosin light chain phosphorylation
نویسندگان
چکیده
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 ...
متن کاملZipper-interacting protein kinase induces Ca(2+)-free smooth muscle contraction via myosin light chain phosphorylation.
The inhibition of myosin phosphatase evokes smooth muscle contraction in the absence of Ca(2+), yet the underlying mechanisms are not understood. To this end, we have cloned smooth muscle zipper-interacting protein (ZIP) kinase cDNA. ZIP kinase is present in various smooth muscle tissues including arteries. Triton X-100 skinning did not diminish ZIP kinase content, suggesting that ZIP kinase as...
متن کاملZipper-interacting Protein Kinase Induces Ca-free Smooth Muscle Contraction via Myosin Light Chain Phosphorylation*
The inhibition of myosin phosphatase evokes smooth muscle contraction in the absence of Ca, yet the underlying mechanisms are not understood. To this end, we have cloned smooth muscle zipper-interacting protein (ZIP) kinase cDNA. ZIP kinase is present in various smooth muscle tissues including arteries. Triton X-100 skinning did not diminish ZIP kinase content, suggesting that ZIP kinase associ...
متن کاملPhosphorylation-dependent Autoinhibition of Myosin Light Chain Phosphatase Accounts for Ca Sensitization Force of Smooth Muscle Contraction*
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, Pennsylvan...
متن کاملEffect of lithium on smooth muscle contraction and phosphorylation of myosin light chain by MLCK.
The aims of our study were to investigate into the effect of lithium on smooth muscle contraction and phosphorylation of myosin light chain (MLC20) by MLCK and to find out the clue of its mechanism. Isolated rabbit duodenum smooth muscle strips were used to study the effects of lithium on their contractile activity under the condition of Krebs' solution by means of HW-400S constant temperature ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1991
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)52353-x