O-Aminobenzoyl-S-Nitrosoglutathione: a Fluorogenic, Cell Permeable, Pseudo-Substrate for S-Nitrosoglutathione Reductase.

O-Aminobenzoyl-S-Nitrosoglutathione: a Fluorogenic, Cell Permeable, Pseudo-Substrate for S-Nitrosoglutathione Reductase. Free Radic Biol Med. 2017 Apr 15;: Authors: Sun BL, Palmer L, Alam SR, Adekoya I, Brown-Steinke K, Periasamy A, Mutus B Abstract S-nitrosoglutathione reductase (GSNOR) is a multifunctional enzyme. It can catalyze NADH-dependent reduction of S-nitrosoglutathione (GSNO); as well as NAD(+)-dependent oxidation of hydroxymethylglutathione (HMGSH; an adduct formed by the spontaneous reaction between formaldehyde and glutathione). While initially recognized as the enzyme that is involved in formaldehyde detoxification, increasing amount of research evidence has shown that GSNOR also plays a significant role in nitric oxide mediated signaling through its modulation of protein S-nitrosothiol abundance via transnitrosation reactions with GSNO. In humans, GSNOR/S-nitrosothiols have been implicated in the etiology of several diseases including lung cancer, cystic fibrosis, asthma, pulmonary hypertension, and neuronal dysfunction. Currently, it is not possible to monitor the activity of GSNOR in live cells. In this article, we present a new compound, O-aminobenzoyl-S-nitrosoglutathione (OAbz-GSNO), which acts as a fluorogenic pseudo-substrate for GSNOR with an estimated Km value of 320µM. The weak OAbz-GSNO fluorescence increases by approximately 14 fold upon reduction of its S-NO moiety. In live cell imaging studies, OAbz-GSN...
Source: Free Radical Biology and Medicine - Category: Biology Authors: Tags: Free Radic Biol Med Source Type: research