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pubmed-article:8607841pubmed:abstractTextNew 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.lld:pubmed
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pubmed-article:8607841pubmed:articleTitleEnhancement of smooth muscle contraction with protein phosphatase inhibitor 1: activation of inhibitor 1 by cGMP-dependent protein kinase.lld:pubmed
pubmed-article:8607841pubmed:affiliationDepartment of Physiology and Biophysics, Case Western Reserve University, School of Medicine, Cleveland, Ohio 44106, USA.lld:pubmed
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pubmed-article:8607841pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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