The effect of NO on phosphotyrosine protein phosphatases (PTPases) has
been investigated in vivo. NO production is induced in interferon-gam
ma and lipopolyaccharide stimulated RAW-263.7 macrophages as indicated
by the increase of NO2- in the medium, Our results demonstrate an inh
ibition of p-nitrophenylphosphatase activity as a consequence of macro
phages activation, Under the described experimental conditions, most o
f the hydrolysis of p-nitrophenylphosphate can be ascribed to the acti
on of cellular PTPases. The presence of N-G-monomethyl-L-arginine, a s
pecific inhibitor of NO synthase decreases the inactivation rate of bo
th membrane-bound and soluble PTPases. This evidence further confirms
the ability of NO to inactivate PTPases and suggests a possible role o
f NO in the regulation of cellular processes involving this class of p
hosphatases.