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Nitric Oxide Regulates Prolidase Activity by Serine/threonine Phosphorylation by Arkadiusz Surazynski; Yongmin Liu; Wojciech Miltyk; James M. Phang is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract Prolidase [E.C. 3.4.13.9], a member of the matrix metalloproteinase (MMP) family, is a manganese‐dependent cytosolic exopeptidase that cleaves imidodipeptides containing C‐terminal proline or hydroxyproline. It plays an important role in collagen metabolism, matrix remodeling and cell growth. Nitric oxide (NO), a versatile signaling molecule, regulates many processes including collagen synthesis and matrix remodeling and, thereby, may modulate angiogenesis, tumor invasiveness, and metastasis. Thus, we considered that prolidase may be an important target of NO regulation. In our study, SIN I and DETA/NO were used as NO donors. Both donors increased prolidase activity in a time‐dependent and dose‐dependent manner. Prolidase activity increased not only with NO donors but also with endogenous NO in cells transfected with iNOS. The effect of iNOS was abolished by treatment with S‐methylisothiourea (SMT), a selective inhibitor of iNOS. However, with either exogenous or endogenous sources of NO, the increase in prolidase activity was not accompanied by increased prolidase expression. Therefore, we suspected phosphorylation of prolidase as a potential mechanism regulating enzym

Who reads Nitric Oxide Regulates Prolidase Activity by Serine/threonine Phosphorylation?

Author

Arkadiusz Surazynski; Yongmin Liu; Wojciech Miltyk; James M. Phang

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0730-2312)

Published

2005

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)