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      Moderate Hypoxia Increases Heat Shock Protein 90 Expression in Excised Rat Aorta

      ,

      Journal of Vascular Research

      S. Karger AG

      Vascular smooth muscle, Immunohistochemistry, Western blotting, Vimentin, α-Actin

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          Abstract

          We hypothesized that heat shock protein 90 (HSP90) expression would be increased in vascular tissue exposed to a hypoxic stress that resulted in altered contractile function. We tested this hypothesis by subjecting excised rat aortic rings to a hypoxic stress that has been shown to reduce contractile force induced by arginine vasopressin (PO<sub>2</sub> ≈50 mm Hg for 1 h) and determining the effect on HSP90 expression. Concentration-response curves were determined for control and hypoxic excised rat aortic rings exposed to norepinephrine (n = 8) or KCl (n = 8). Hypoxia reduced the force generated in response to the highest concentration of each agonist. HSP90 expression was evaluated by immunoblotting (n = 6) and immunohistochemistry (n = 7). Both methods documented increased expression of HSP90 in hypoxic aortae as compared to controls. HSP90 expression was increased within the cytoplasm and in conjunction with the nucleus of vascular smooth muscle cells in the tunica media and also within vascular myointimal cells. We conclude that a hypoxic stress sufficient to induce contractile dysfunction increases HSP90 expression in rat aortic smooth muscle cells.

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          Most cited references 3

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          The role of the hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase.

           Gregory Pratt (1996)
          The multicomponent heat-shock protein (hsp) 90-based chaperone system is an ubiquitous protein-folding system in the cytoplasm of eukaryotes. Several signal transduction systems utilize an interaction with hsp90 as an essential component of the signaling pathway. The steroid and dioxin receptors are bound to hsp90 through their hormone-binding domains, and several of them must be bound to hsp90 in order to have a ligand-binding site. The binding of ligands to these receptors promotes their dissociation from hsp90, an event that is the first step in their signaling pathways. Several protein kinases, including the Src and Raf components of the MAP kinase system, are also bound to hsp90. Genetic studies in yeast have demonstrated that hsp90 is required for normal signaling via steroid and dioxin receptors and for the activity of Src in vivo. The hsp90-based chaperone system has been reconstituted from purified components, permitting detailed analysis of the molecular basis of the chaperone's role in signal transduction.
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            Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90

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              • Abstract: found
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              Vasoconstrictor and vasodilator effects of hypoxia.

              Hypoxia has marked effects on artery calibre, which reflects important physiological control mechanisms that are altered in disease states. Hypoxia modifies the release of mediators, especially from the endothelium, and influences smooth muscle membrane potential and Ca2+ regulation. In this review, Roger Wadsworth evaluates the vasoconstrictor and vasodilator effects of hypoxia studied in vitro. In the future, drugs developed to act on the mediators or smooth muscle may be beneficial in the therapy of, for example, pulmonary hypertension or coronary vasospasm.
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                Author and article information

                Journal
                JVR
                J Vasc Res
                10.1159/issn.1018-1172
                Journal of Vascular Research
                S. Karger AG
                1018-1172
                1423-0135
                1999
                October 1999
                28 October 1999
                : 36
                : 5
                : 363-371
                Affiliations
                Department of Veterinary Biosciences, The Ohio State University, Columbus, Ohio, USA
                Article
                25675 J Vasc Res 1999;36:363–371
                10.1159/000025675
                10559676
                © 1999 S. Karger AG, Basel

                Copyright: All rights reserved. No part of this publication may be translated into other languages, reproduced or utilized in any form or by any means, electronic or mechanical, including photocopying, recording, microcopying, or by any information storage and retrieval system, without permission in writing from the publisher. Drug Dosage: The authors and the publisher have exerted every effort to ensure that drug selection and dosage set forth in this text are in accord with current recommendations and practice at the time of publication. However, in view of ongoing research, changes in government regulations, and the constant flow of information relating to drug therapy and drug reactions, the reader is urged to check the package insert for each drug for any changes in indications and dosage and for added warnings and precautions. This is particularly important when the recommended agent is a new and/or infrequently employed drug. Disclaimer: The statements, opinions and data contained in this publication are solely those of the individual authors and contributors and not of the publishers and the editor(s). The appearance of advertisements or/and product references in the publication is not a warranty, endorsement, or approval of the products or services advertised or of their effectiveness, quality or safety. The publisher and the editor(s) disclaim responsibility for any injury to persons or property resulting from any ideas, methods, instructions or products referred to in the content or advertisements.

                Page count
                Figures: 8, Tables: 3, References: 25, Pages: 9
                Categories
                Research Paper

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