NAD(P)H Oxidases in Rat Basilar Arterial Endothelial Cells
- 1 May 2005
- journal article
- research article
- Published by Ovid Technologies (Wolters Kluwer Health) in Stroke
- Vol. 36 (5), 1040-1046
- https://doi.org/10.1161/01.str.0000163111.05825.0b
Abstract
Background and Purpose— Reactive oxygen species (ROS) may play a critical role in the regulation of vascular tone and development of vascular diseases, such as stroke. NAD(P)H oxidase is a major source of ROS in vascular cells, including endothelial cells. It has been considered that Nox2 and Nox4 are exclusively expressed among Nox homologues in the endothelial cells of noncerebral blood vessels. However, the precise molecular identity of the NAD(P)H oxidase in the endothelial cells of the cerebral arteries is not fully understood. We examined the expression of Nox homologues and their activation mechanism in the endothelial cells of the cerebral arteries. Methods— We isolated and cultured basilar artery endothelial cells (BAECs) of Sprague-Dawley rats. Expression of NAD(P)H oxidase was examined by reverse-transcription-polymerase chain reaction (RT-PCR) and immunohistological staining. Results— RT-PCR disclosed abundant expression of Nox4 with marginal Nox2 in BAEC. In addition, Nox1 was expressed highly both at mRNA and protein levels in BAECs. Immunohistological staining also showed the prominent expression of Nox1 in the endothelial cells of the basilar artery. With respect to the cytosolic components of NAD(P)H oxidases, BAECs expressed p67 phox and, to a lesser extent, p47 phox , Noxo1, and Noxa1. Both NADH and NADPH induced superoxide production of the BAEC membranes. The phagocyte-type cytosolic components, p47 phox and p67 phox , significantly enhanced the NADH-induced superoxide production of the BAEC membranes, whereas the components failed to increase the NADPH-induced superoxide production. Conclusions— Nox1 is highly expressed in the endothelial cells of the cerebral arteries along with Nox2 and Nox4, and the endothelial NAD(P)H oxidase of the cerebral arteries may have a unique activation mechanism by the phagocyte-type cytosolic components.This publication has 21 references indexed in Scilit:
- Distinct Subcellular Localizations of Nox1 and Nox4 in Vascular Smooth Muscle CellsArteriosclerosis, Thrombosis, and Vascular Biology, 2004
- NOX enzymes and the biology of reactive oxygenNature Reviews Immunology, 2004
- Increased NADPH-Oxidase Activity and Nox4 Expression During Chronic Hypertension Is Associated With Enhanced Cerebral Vasodilatation to NADPH In VivoStroke, 2004
- Nox4 as the Major Catalytic Component of an Endothelial NAD(P)H OxidaseCirculation, 2004
- Association of gp91phox homolog Nox1 with anchorage-independent growth and MAP kinase-activation of transformed human keratinocytesOncogene, 2003
- Novel Human Homologues of p47 and p67 Participate in Activation of Superoxide-producing NADPH OxidasesOnline Journal of Public Health Informatics, 2003
- Proteins Homologous to p47 and p67 Support Superoxide Production by NAD(P)H Oxidase 1 in Colon Epithelial CellsPublished by Elsevier BV ,2003
- Expression of a Functionally Active gp91phox-Containing Neutrophil-Type NAD(P)H Oxidase in Smooth Muscle Cells From Human Resistance ArteriesCirculation Research, 2002
- Intracellular Localization and Preassembly of the NADPH Oxidase Complex in Cultured Endothelial CellsOnline Journal of Public Health Informatics, 2002
- The PX Domain as a Novel Phosphoinositide- Binding ModuleBiochemical and Biophysical Research Communications, 2001