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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1996-5-20
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pubmed:abstractText |
New method for purification of phosphatase inhibitor 1 (PPI-1) was developed which avoid the phosphorylation of PPI-1 during the purification and provides a high yield of highly pure preparation. Using this preparation, it was shown that PPI-1 was stoichiometrically phosphorylated by cGMP-dependent protein kinase at Thr-35 and the phosphorylated PPI-1 potently inhibited protein phosphatase 1. Addition of the phosphorylated PPI-1 to beta-escin-skinned single smooth muscle cells resulted in force development of the cells at the submaximal pCa2+. The results suggest that the phosphorylation of PPI-1 can be the mechanism for modifying the Ca2+ sensitivity of smooth muscle contractile response.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic GMP-Dependent Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin-Light-Chain Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/protein phosphatase inhibitor-1
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
220
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
777-83
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8607841-Amino Acid Sequence,
pubmed-meshheading:8607841-Animals,
pubmed-meshheading:8607841-Carrier Proteins,
pubmed-meshheading:8607841-Chromatography, Ion Exchange,
pubmed-meshheading:8607841-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:8607841-Cyclic GMP-Dependent Protein Kinases,
pubmed-meshheading:8607841-Enzyme Inhibitors,
pubmed-meshheading:8607841-Gizzard,
pubmed-meshheading:8607841-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:8607841-Kinetics,
pubmed-meshheading:8607841-Molecular Sequence Data,
pubmed-meshheading:8607841-Muscle, Skeletal,
pubmed-meshheading:8607841-Muscle, Smooth, Vascular,
pubmed-meshheading:8607841-Muscle Contraction,
pubmed-meshheading:8607841-Myosin-Light-Chain Kinase,
pubmed-meshheading:8607841-Peptide Fragments,
pubmed-meshheading:8607841-Peptides,
pubmed-meshheading:8607841-Phosphopeptides,
pubmed-meshheading:8607841-Phosphorylation,
pubmed-meshheading:8607841-Portal Vein,
pubmed-meshheading:8607841-Proteins,
pubmed-meshheading:8607841-Rabbits,
pubmed-meshheading:8607841-Turkeys
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pubmed:year |
1996
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pubmed:articleTitle |
Enhancement of smooth muscle contraction with protein phosphatase inhibitor 1: activation of inhibitor 1 by cGMP-dependent protein kinase.
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pubmed:affiliation |
Department of Physiology and Biophysics, Case Western Reserve University, School of Medicine, Cleveland, Ohio 44106, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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