Premium
In vivo inactivation of phosphotyrosine protein phosphatases by nitric oxide
Author(s) -
Caselli Anna,
Chiarugi Paola,
Camici Guido,
Manao Giampaolo,
Ramponi Giampietro
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01120-4
Subject(s) - phosphatase , biochemistry , in vivo , protein tyrosine phosphatase , nitric oxide , enzyme , chemistry , nitric oxide synthase , microbiology and biotechnology , biology , organic chemistry
The effect of NO on phosphotyrosine protein phosphatases (PTPases) has been investigated in vivo. NO production is induced in interferon‐γ and lipopolyaccharide stimulated RAW‐264.7 macrophages as indicated by the increase of NO 2 − in the medium. Our results demonstrate an inhibition of p ‐nitrophenylphosphatase activity as a consequence of macrophages activation. Under the described experimental conditions, most of the hydrolysis of p ‐nitrophenylphosphate can be ascribed to the action of cellular PTPases. The presence of , a specific inhibitor of NO synthase decreases the inactivation rate of both membrane‐bound and soluble PTPases. This evidence further confirms the ability of NO to inactivate PTPases and suggests a possible role of NO in the regulation of cellular processes involving this class of phosphatases.