Enhancement of smooth muscle contraction with protein phosphatase inhibitor 1: Activation of inhibitor 1 by cGMP-dependent protein kinase

Toshiya Tokui; Frank Brozovich; Shoji Ando; Mitsuo Ikebe

doi:10.1006/bbrc.1996.0480

Enhancement of smooth muscle contraction with protein phosphatase inhibitor 1: Activation of inhibitor 1 by cGMP-dependent protein kinase

Toshiya Tokui, Frank Brozovich, Shoji Ando, Mitsuo Ikebe

Cardiovascular Medicine

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

Abstract

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 β-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.

Original language	English (US)
Pages (from-to)	777-783
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	220
Issue number	3
DOIs	https://doi.org/10.1006/bbrc.1996.0480
State	Published - Mar 27 1996

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "Enhancement of smooth muscle contraction with protein phosphatase inhibitor 1: Activation of inhibitor 1 by cGMP-dependent protein kinase",

abstract = "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 β-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.",

author = "Toshiya Tokui and Frank Brozovich and Shoji Ando and Mitsuo Ikebe",

note = "Funding Information: 1This work was supported by National Institute of Health Grant HL37117, HL47530, AR41653 (to MI) and HL44181 (toFB) and is also supported by American Heart Association Grant in Aid (toMI). FB is an Established Investigator of American Heart Association. 2Present address: Department of Thoracic and Cardiovascular Surgery, Mie University School of Medicine, 2-174 Edobashi, Tsu, Mie 514 Japan. 3Present address: Lab. Chemistry, Saga Medical School, 5-1-1 Nabeshima, Saga 849, Japan. 4To whom correspondence should be addressed. Fax: (508)-856-5997. Abbreviations: PMSF, phenylmethylsulfonyl fluoride; PP1, protein phosphatase 1; PP2A, protein phosphatase 2A; PP2B,",

year = "1996",

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doi = "10.1006/bbrc.1996.0480",

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AU - Brozovich, Frank

AU - Ando, Shoji

AU - Ikebe, Mitsuo

N1 - Funding Information: 1This work was supported by National Institute of Health Grant HL37117, HL47530, AR41653 (to MI) and HL44181 (toFB) and is also supported by American Heart Association Grant in Aid (toMI). FB is an Established Investigator of American Heart Association. 2Present address: Department of Thoracic and Cardiovascular Surgery, Mie University School of Medicine, 2-174 Edobashi, Tsu, Mie 514 Japan. 3Present address: Lab. Chemistry, Saga Medical School, 5-1-1 Nabeshima, Saga 849, Japan. 4To whom correspondence should be addressed. Fax: (508)-856-5997. Abbreviations: PMSF, phenylmethylsulfonyl fluoride; PP1, protein phosphatase 1; PP2A, protein phosphatase 2A; PP2B,

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Enhancement of smooth muscle contraction with protein phosphatase inhibitor 1: Activation of inhibitor 1 by cGMP-dependent protein kinase

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