Endothelial argininosuccinate synthetase 1 (ASS1) regulates the provision of l-arginine to
nitric oxide synthase 3 (NOS3). Previous studies demonstrated that endothelial ASS1 …

Increases in arginase activity have been reported in a variety of disease conditions
characterized by vascular dysfunction. Arginase competes with NO synthase for their …

Increased arginase activity has been reported in a variety of disease conditions
characterized by vascular dysfunction. In the present study, the potentially protective effect of …

Arginine (L-arginine), is an amino acid involved in a number of biological processes,
including the biosynthesis of proteins, host immune response, urea cycle, and nitric oxide …

Aims Increased matrix metalloproteinases activity and reduced nitric oxide (NO)
bioavailability contributes to development of hypertension and this may be associated with a …

Endothelial function is impaired in aging because of a decrease in NO bioavailability. This
may be, in part, attributable to increased arginase activity, which reciprocally regulates NO …

Impaired production or biological activity of nitric oxide (NO) released from vascular
endothelium is a central mechanism of endothelial dysfunction. 1 Large number of …

Arginase-2 counteracts endothelial nitric oxide synthase (eNOS) activity in human
endothelium, and its expression is negatively controlled by histone deacetylase (HDAC2) …

Arginase shares a common substrate, L‐arginine, with nitric oxide (NO) synthase (NOS). It is
thought that arginase, if it is expressed in the endothelium, might play a pivotal role in the …

The objectives of this study were to determine whether rat aortic smooth muscle cells
(RASMC) express arginase and to elucidate the possible mechanisms involved in the …