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Bayraktutan, Ulvi, Blayney, Lynda and Shah, Ajay (2000) Molecular Characterization and Localization of the NAD(P)H Oxidase Components gp91-phox and p22-phox in Endothelial Cells. Arteriosclerosis thrombosis and vascular biology, 20 . pp. 1903-1911.

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Abstract

The production of reactive oxygen species (ROS) within endothelial cells may have several effects, including

alterations in the activity of paracrine factors, gene expression, apoptosis, and cellular injury. Recent studies indicate that

a phagocyte-type NAD(P)H oxidase is a major source of endothelial ROS. In contrast to the high-output phagocytic

oxidase, the endothelial enzyme has much lower biochemical activity and a different substrate specificity

(NADH.NADPH). In the present study, we (1) cloned and characterized the cDNA and predicted amino acid structures

of the 2 major subunits of rat coronary microvascular endothelial cell NAD(P)H oxidase, gp91-phox and p22-phox;

(2) undertook a detailed comparison with phagocytic NADPH oxidase sequences; and (3) studied the subcellular

location of these subunits in endothelial cells. Although these studies revealed an overall high degree of homology

(.90%) between the endothelial and phagocytic oxidase subunits, the endothelial gp91-phox sequence has potentially

important differences in a putative NADPH-binding domain and in putative glycosylation sites. In addition, the

subcellular location of the endothelial gp91-phox and p22-phox subunits is significantly different from that reported for

the neutrophil oxidase, in that they are predominantly intracellular and collocated in the vicinity of the endoplasmic

reticulum. This first detailed characterization of gp91-phox and p22-phox structure and location in endothelial cells

provides new data that may account, in part, for the differences in function between the phagocytic and endothelial

NAD(P)H oxidases.

Item Type:	Article
RIS ID:	https://nottingham-repository.worktribe.com/output/1023593
Keywords:	endothelium n NADPH oxidase n reactive oxygen species n cDNA
Schools/Departments:	University of Nottingham, UK > Faculty of Medicine and Health Sciences > School of Medicine > Division of Medical Sciences and Graduate Entry Medicine
Related URLs:	URL URL Type http://atvb.ahajournals.org/ Publisher
Depositing User:	Sayers, Hazel
Date Deposited:	26 Oct 2006
Last Modified:	04 May 2020 20:32
URI:	https://eprints.nottingham.ac.uk/id/eprint/427

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