PMID: 9439972Jan 24, 1998Paper

Nitric oxide synthase activity in tissues of the bovine eye

Graefe's Archive for Clinical and Experimental Ophthalmology = Albrecht Von Graefes Archiv Für Klinische Und Experimentelle Ophthalmologie
O GeyerT Mittag

Abstract

Nitric oxide synthase (NOS) is present in many ocular tissues where it may have different physiological functions. This warrants a thorough characterization of NOS activity in the eye. NOS distribution and its biochemical properties were determined in the retina, choroid, ciliary processes (CP), and trabecular meshwork (TM). Retinal NOS required NADPH (diphenylene-iodonium, a flavoprotein inhibitor, which inhibited enzyme activity with an IC50 of 0.36 microM, FAD (40 microM), FMN (40 microM), and BH4 (4 microM) as cofactors for optimal activity. Ocular NOS appeared to be regulated by free divalent cations, since its activity was inhibited by EDTA (slopes > 3.0 and IC50 values of 12.8, 19.7, and 53 microM, respectively). Ocular NOS required calmodulin, since NOS activity was inhibited by trifluoperazine (calmodulin inhibitor, IC50 = 41 microM). NOS activity is widely distributed in the eye, (choroid > retina > CP > TM) and is mainly cytosolic (70-95%). L-Arginine analogs inhibited NOS in the retina, choroid, and TM. In all three tissues, NG-methyl-L-arginine displayed the highest affinity for inhibition (IC50 = 0.2-0.7 microM) followed by canavanine (IC50 = 13-33 microM), while aminoguanidine only weakly inhibited NOS (IC50 = 93...Continue Reading

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Citations

Mar 31, 2004·Experimental Eye Research·Karl-Georg SchmidtT W Mittag
Sep 27, 2000·American Journal of Ophthalmology·G YilmazN Kociek
Jul 1, 1998·Clinical Biochemistry·G EllisS K Makela
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Mar 7, 2021·Antioxidants·Marc Herb, Michael Schramm
Dec 1, 2020·Progress in Retinal and Eye Research·Ester Reina-TorresW Daniel Stamer

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