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      Call for Papers: Novel Methods in Vascular and Lymphatic Physiology

      Submit here before June 30, 2025

      About Journal of Vascular Research: 1.8 Impact Factor I 3.4 CiteScore I 0.486 Scimago Journal & Country Rank (SJR)

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      Transglutaminases in Vascular Biology: Relevance for Vascular Remodeling and Atherosclerosis

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          Abstract

          The transglutaminase (Tgase) family consists of nine known members of whom at least three are expressed in the vascular system: type 1 Tgase, type 2 Tgase and factor XIII. The cross-linking of proteins is a characteristic feature of Tgases, of well-known importance for stabilizing the blood clot and providing mechanical strength to tissues. However, recent data suggest that Tgases play a role in several other processes in vascular biology. These newly discovered areas include endothelial barrier function, small artery remodeling, and atherosclerosis.

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          Transglutaminases: crosslinking enzymes with pleiotropic functions.

          Laszlo Lorand, Robert Graham (2003)
          Blood coagulation, skin-barrier formation, hardening of the fertilization envelope, extracellular-matrix assembly and other important biological processes are dependent on the rapid generation of covalent crosslinks between proteins. These reactions--which are catalysed by transglutaminases--endow the resulting supramolecular structure with extra rigidity and resistance against proteolytic degradation. Some transglutaminases function as molecular switches in cytoskeletal scaffolding and modulate protein-protein interactions. Having knowledge of these enzymes is essential for understanding the aetiologies of diverse hereditary diseases of the blood and skin, and various autoimmune, inflammatory and degenerative conditions.
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            Tissue Transglutaminase Is an Integrin-Binding Adhesion Coreceptor for Fibronectin

            Sergey S. Akimov, Dmitry Krylov, Laurie F. Fleischman … (2000)
            The protein cross-linking enzyme tissue transglutaminase binds in vitro with high affinity to fibronectin via its 42-kD gelatin-binding domain. Here we report that cell surface transglutaminase mediates adhesion and spreading of cells on the 42-kD fibronectin fragment, which lacks integrin-binding motifs. Overexpression of tissue transglutaminase increases its amount on the cell surface, enhances adhesion and spreading on fibronectin and its 42-kD fragment, enlarges focal adhesions, and amplifies adhesion-dependent phosphorylation of focal adhesion kinase. These effects are specific for tissue transglutaminase and are not shared by its functional homologue, a catalytic subunit of factor XIII. Adhesive function of tissue transglutaminase does not require its cross-linking activity but depends on its stable noncovalent association with integrins. Transglutaminase interacts directly with multiple integrins of β1 and β3 subfamilies, but not with β2 integrins. Complexes of transglutaminase with integrins are formed inside the cell during biosynthesis and accumulate on the surface and in focal adhesions. Together our results demonstrate that tissue transglutaminase mediates the interaction of integrins with fibronectin, thereby acting as an integrin-associated coreceptor to promote cell adhesion and spreading.
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              Gh: a GTP-binding protein with transglutaminase activity and receptor signaling function.

              Kate Im, D. Campora Perez, Basma F. A. Husain … (1994)
              The alpha 1-adrenergic receptors activate a phospholipase C enzyme by coupling to members of the large molecular size (approximately 74 to 80 kilodaltons) G alpha h family of guanosine triphosphate (GTP)-binding proteins. Rat liver G alpha h is now shown to be a tissue transglutaminase type II (TGase II). The transglutaminase activity of rat liver TGase II expressed in COS-1 cells was inhibited by the nonhydrolyzable GTP analog guanosine 5'-O-(3-thiotriphosphate) or by alpha 1-adrenergic receptor activation. Rat liver TGase II also mediated alpha 1-adrenergic receptor stimulation of phospholipase C activity. Thus, G alpha h represents a new class of GTP-binding proteins that participate in receptor signaling and may be a component of a complex regulatory network in which receptor-stimulated GTP binding switches the function of G alpha h from transglutamination to receptor signaling.
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                Author and article information

                Journal
                Journal ID (publisher-id): JVR
                Journal ID (nlm-ta): J Vasc Res
                Journal ID (doi): 10.1159/issn.1018-1172
                Title: Journal of Vascular Research
                Publisher: S. Karger AG
                ISSN (Print): 1018-1172
                ISSN (Electronic): 1423-0135
                Publication date Subscription-year: 2008
                Publication date (Print): June 2008
                Publication date (Electronic): 22 January 2008
                Volume: 45
                Issue: 4
                Pages: 271-278
                Affiliations
                Department of Medical Physics, Academic Medical Center, Amsterdam, The Netherlands
                Article
                Publisher ID: 113599 Other ID: J Vasc Res 2008;45:271–278
                DOI: 10.1159/000113599
                PubMed ID: 18212504
                SO-VID: 91c28d82-7ddd-412e-aeae-9ef55dbd6618
                Copyright © © 2008 S. Karger AG, Basel
                License:

                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.

                History
                Date received : 22 June 2007
                Date accepted : 26 November 2007
                Page count
                Figures: 3, References: 75, Pages: 8
                Categories
                Subject: Review

                ScienceOpen disciplines: General medicine,Neurology,Cardiovascular Medicine,Internal medicine,Nephrology
                Keywords: Transglutaminase,Atherosclerosis,Factor XIII,Vascular remodeling
                Data availability:
                ScienceOpen disciplines: General medicine, Neurology, Cardiovascular Medicine, Internal medicine, Nephrology
                Keywords: Transglutaminase, Atherosclerosis, Factor XIII, Vascular remodeling

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