Interaction between Caveolin-1 and the Reductase Domain of Endothelial Nitric-oxide Synthase CONSEQUENCES FOR CATALYSIS
TLDR
It is proposed that cav-1 binding to eNOS reductase compromises its ability to bind CaM and to donate electrons to the eN OS heme, thereby inhibiting NO synthesis.About:
This article is published in Journal of Biological Chemistry.The article was published on 1998-08-28 and is currently open access. It has received 152 citations till now. The article focuses on the topics: Enos & Nitric oxide synthase.read more
Citations
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Journal ArticleDOI
Nitric oxide synthases: structure, function and inhibition
TL;DR: This review concentrates on advances in nitric oxide synthase (NOS) structure, function and inhibition made in the last seven years, during which time substantial advances have been made in the authors' understanding of this enzyme family.
Journal ArticleDOI
Mammalian nitric oxide synthases.
TL;DR: This report summarizes some of the current information regarding NO synthase structure-function, reaction mechanism, control of catalysis, and protein interactions.
Journal ArticleDOI
Caveolins, liquid-ordered domains, and signal transduction.
Eric J. Smart,Gregory A. Graf,Mark A. McNiven,William C. Sessa,Jeffrey A. Engelman,Philipp E. Scherer,Takashi Okamoto,Michael P. Lisanti +7 more
TL;DR: This review seeks to update the working definition of caveolae, describe the functional roles of the caveolin gene family, and summarize the evidence that supports a role for Caveolae as mediators of a number of cellular signaling processes.
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Molecular mechanisms involved in the regulation of the endothelial nitric oxide synthase
Ingrid Fleming,Rudi Busse +1 more
TL;DR: Simultaneous alterations in the phosphorylation of Ser(1177) and Thr(495) in response to a variety of stimuli are regulated by a number of kinases and phosphatases that continuously associate with and dissociate from the eNOS signaling complex.
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Enzymatic function of nitric oxide synthases.
Penelope Andrew,Bernd Mayer +1 more
TL;DR: The pteridine tetrahydrobiopterin (BH4) is a key feature of NOS, affecting dimerisation and electron transfer, although its full role in catalysis remains to be determined.
References
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Nitric oxide synthases in mammals.
TL;DR: This review will describe the known biochemical mechanisms involved in the synthesis of NO from L-arginine by the NO synthases and will also describe the nature of these enzymes, their inhibition and their molecular characteristics.
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Caveolins, a Family of Scaffolding Proteins for Organizing “Preassembled Signaling Complexes” at the Plasma Membrane
TL;DR: Because the responsibilities assigned to caveolae continue to increase, this review will focus on: (i) caveolin structure/function and (ii) Caveolae-associated signal transduction.
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Cellular and molecular mechanisms of endothelial cell dysfunction.
TL;DR: This Perspective will highlight some of the important new observations, as they relate to the pathology of the endothelial cell L -arginine/NO synthase (NOS) system, which have led to new insights into regulation of vascular tone, redox state, inflammation, growth, and the prothrombotic/antithrombosis properties of the vessel wall.
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Nitric oxide synthases: which, where, how, and why?
Thomas Michel,Olivier Feron +1 more
TL;DR: eNOS, the last of the three mammalian NOS isoforms to be isolated, was originally purified and cloned from vascular endothelium, but has since been discovered in cardiac myocytes, blood platelets, brain (hippocampus), and elsewhere.
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Identification of Peptide and Protein Ligands for the Caveolin-scaffolding Domain IMPLICATIONS FOR THE INTERACTION OF CAVEOLIN WITH CAVEOLAE-ASSOCIATED PROTEINS
TL;DR: The Caveolin-scaffolding domain is used as a receptor to select random peptide ligands from phage display libraries and it is found that the scaffolding domains of caveolins 1 and 3 both recognize the same peptide and protein ligands, whereas the corresponding domain within caveolin-2 fails to recognize these ligands under the same conditions.