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Interactions between Phosphatidylinositol 3-Kinase and Nitric Oxide: Explaining the Paradox

Wright, Karen L. and Ward, Stephen G. (2000) Interactions between Phosphatidylinositol 3-Kinase and Nitric Oxide: Explaining the Paradox. Molecular Cell Biology Research Communications, 4 (3). pp. 137-143. ISSN 1522-4724

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Abstract

Nitric oxide (NO) and the many derivatives and reactive oxygen intermediates thereof are all molecules that are utilised by mammalian cells in the war against microbial pathogens and tumours. They are potentially toxic molecules and, with damage control being crucial, the production and metabolism of nitric oxide is a tightly regulated process. The duality of NO is well documented. On the one hand, beneficial effects include normal healing in the skin and intestinal mucosa, killing of certain bacteria, regulating T cell proliferation and differentiation (Th1 vs Th2), and regulating leukocyte recruitment, by affecting adhesion molecule expression. On the other hand, persistent high levels of NO can lead to the production of toxic metabolites (peroxynitrite and hydroxyls), which can have detrimental effects, such as increased microvascular and epithelial permeability, increased oxidative stress (which can damage DNA), and damage to iron–sulphur proteins in mitochondria. NO has been reported to modulate its own production and the mechanisms involved in this self-regulation are being hotly pursued. The purpose of this review is to update recent intriguing advances in our understanding of the interaction of the phosphatidylinositol (PI) 3-kinase-dependent signal transduction pathway in regulating the activity of the enzymes that generate NO, namely, the nitric oxide synthases.

Item Type: Article
Journal or Publication Title: Molecular Cell Biology Research Communications
Uncontrolled Keywords: nitric oxide ; nitric oxide synthase ; phosphatidylinositol 3-kinase ; protein kinase B
Subjects: R Medicine > RM Therapeutics. Pharmacology
Departments: Faculty of Health and Medicine > Biomedical & Life Sciences
ID Code: 40896
Deposited By: Mr Richard Ingham
Deposited On: 16 Jun 2011 11:19
Refereed?: Yes
Published?: Published
Last Modified: 26 Jul 2012 18:06
Identification Number:
URI: http://eprints.lancs.ac.uk/id/eprint/40896

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