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      Call for Papers: Green Renal Replacement Therapy: Caring for the Environment

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      About Blood Purification: 2.2 Impact Factor I 5.8 CiteScore I 0.782 Scimago Journal & Country Rank (SJR)

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      Induction and Coexpression of Latent Transforming Growth Factor β-Binding Protein-1 and Fibrillin-1 in Experimental Glomerulonephritis

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          Abstract

          Background: Latent transforming growth factor-β-binding protein 1 (LTBP-1) and fibrillin-1 were shown to colocalize and interact in the extracellular matrix of the skin and vasculature. This interaction may regulate transforming growth factor-β (TGF-β) activity. TGF-β is an important progression factor for glomerular diseases. We hypothesized that LTBP-1 and fibrillin-1 are coexpressed in the glomerulus and upregulated during glomerulonephritis. Methods: Acute anti-Thy1.1 glomerulonephritis was induced with a single intravenous injection (1 mg/kg body weight) of a monoclonal anti-Thy1.1 antibody in rats. Real-time RT-PCR and immunohistochemical analyses for LTBP-1 and fibrillin-1 were performed. Results: Induction of glomerular LTBP-1 mRNA was detected on day 2 of disease, while mRNA for fibrillin-1 was already upregulated 1 day after induction of disease. Both LTBP-1 and fibrillin-1 showed a mesangial distribution. An expansion of the LTBP-1 and fibrillin-1-positive mesangial area was seen on day 6 of disease, when transient matrix accumulation was most prominent. On day 12 of disease, glomerular LTBP-1 and fibrillin-1 immunoreactivities had returned to control levels. In serial sections, some colocalization of LTBP-1 and fibrillin-1 was detected in control as well as in nephritic glomeruli. Conclusion: Mesangial expression of LTBP-1 and fibrillin-1 is induced early in experimental nephritis and LTBP-1 and fibrillin-1 are partially colocalized in the nephritic glomerulus. An interaction of these molecules could stabilize latent TGF-β complexes and thus attenuate the activation of TGF-β during this self-limited glomerular disease.

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          TGF-β–dependent pathogenesis of mitral valve prolapse in a mouse model of Marfan syndrome

          Connie M Ng, Alan Cheng, Loretha Myers … (2004)
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            Role of transforming growth factor-beta1 and its latent form binding protein in pseudoexfoliation syndrome.

            U Schlötzer-Schrehardt, M Zenkel, M Küchle … (2001)
            Pseudoexfoliation (PEX) syndrome is a common and clinically important systemic condition characterized by the pathologic production and accumulation of an abnormal fibrillar extracellular material in many intra- and extraocular tissues. Recent evidence suggests that it is a type of elastosis associated with the excess synthesis of elastic microfibrillar components such as fibrillin-1. Since transforming growth factor (TGF)-beta is a major modulator of extracellular matrix formation, the potential involvement of TGF-beta and its latent form binding protein (LTBP) in this aberrant matrix process was investigated. The expression of various isoforms of TGF-beta and LTBP was investigated in the anterior segment tissues of PEX and control eyes on the protein and mRNA level by light and electron microscopic immunohistochemistry, in situ hybridization, and semiquantitative RT-PCR. TGF-beta1 and TGF-beta2 levels were measured in aqueous humor and serum of PEX and control patients by ELISA. Cultures of Tenon's capsule fibroblasts were established to study the effect of TGF-beta1 on fibrillin-1 mRNA expression by Northern blot analysis. Significantly increased concentrations of both total and active TGF-beta1 were measured in the aqueous humor of PEX eyes without and with glaucoma as compared to control eyes, whereas levels of TGF-beta2 were not significantly different. The expression of TGF-beta1, LTBP-1, and LTBP-2, but not TGF-beta2, was markedly increased in anterior segment tissues of PEX eyes, particularly in the non-pigmented epithelium of the ciliary body, on both the mRNA and the protein level. Latent TGF-beta1 staining was consistently associated with PEX material deposits and could be released by proteolytic processing. Double immunolabeling revealed clear co-localization of LTBP-1 and -2 with latent TGF-beta1 and with fibrillin-1 on PEX fibrils. The expression of mRNA coding for fibrillin-1 was up-regulated in vitro by TGF-beta1. This study provides evidence for a significant role of TGF-beta1 and the LTBPs 1 and 2 in PEX syndrome. The results suggest that increased levels of latent and active TGF-beta1 in the aqueous humor of PEX patients, derived from enhanced local synthesis and activation, promote the buildup of the abnormal extracellular elastic material characteristic of PEX syndrome. They further support a dual role for LTBPs, both as integral structural components of PEX fibers and as a means of matrix anchorage of latent TGF-beta1, representing one possible mechanism for the regulation of TGF-beta1 activity in PEX eyes. Future therapeutic strategies might focus on TGF-beta1 antagonistic approaches. Copyright 2001 Academic Press.
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              Interactions of fibrillin-1 with heparin/heparan sulfate, implications for microfibrillar assembly.

              B Bätge, Jan Reinhardt, K. Müller … (2001)
              Fibrillin-1 is a major constituent of the 10-12 nm extracellular microfibrils. Here we identify, characterize, and localize heparin/heparan sulfate-binding sites in fibrillin-1 and report on the role of such glycosaminoglycans in the assembly of fibrillin-1. By using different binding assays, we localize two calcium-independent heparin-binding sites to the N-terminal (Arg(45)-Thr(450)) and C-terminal (Asp(1528)-Arg(2731)) domains of fibrillin-1. A calcium-dependent-binding site was localized to the central (Asp(1028)-Thr(1486)) region of fibrillin-1. Heparin binding to these sites can be inhibited by a highly sulfated and iduronated form of heparan sulfate but not by chondroitin 4-sulfate, chondroitin 6-sulfate, and dermatan sulfate, demonstrating that the heparin binding regions represent binding domains for heparan sulfate. When heparin or heparan sulfate was added to cultures of skin fibroblasts, the assembly of fibrillin-1 into a microfibrillar network was significantly reduced. Western blot analysis demonstrated that this effect was not due to a reduced amount of fibrillin-1 secreted into the culture medium. Inhibition of the attachment of glycosaminoglycans to core proteins of proteoglycans by beta-d-xylosides resulted in a significant reduction of the fibrillin-1 network. These studies suggest that binding of fibrillin-1 to proteoglycan-associated heparan sulfate chains is an important step in the assembly of microfibrils.
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                Author and article information

                Journal
                Journal ID (publisher-id): NEE
                Journal ID (nlm-ta): Nephron Exp Nephrol
                Journal ID (doi): 10.1159/issn.1660-2129
                Title: Cardiorenal Medicine
                Publisher: S. Karger AG
                ISSN (Electronic): 1660-2129
                Publication date Subscription-year: 2006
                Publication date (Print): February 2006
                Publication date (Electronic): 11 November 2005
                Volume: 102
                Issue: 3-4
                Pages: e99-e104
                Affiliations
                aChildren’s Hospital and bDepartment of Medicine IV, University of Erlangen-Nuremberg, Erlangen, cDepartment of Nephrology, University of Kiel, Kiel, Germany; dDepartment of Anatomy and Cell Biology and Faculty of Dentistry, McGill University, Montreal, Canada
                Article
                Publisher ID: 89688 Other ID: Nephron Exp Nephrol 2006;102:e99–e104
                DOI: 10.1159/000089688
                PubMed ID: 16282705
                SO-VID: 9f8503cb-67a5-4ad2-8121-0f5696e022f6
                Copyright © © 2006 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 : 10 March 2005
                Date accepted : 08 August 2005
                Page count
                Figures: 3, References: 17, Pages: 1
                Categories
                Subject: Original Paper

                ScienceOpen disciplines: Cardiovascular Medicine,Nephrology
                Keywords: Anti-Thy1.1 nephritis,Transforming growth factor-β,Microfibrillar proteins,Glomerulus,Extracellular matrix,Mesangial cells
                Data availability:
                ScienceOpen disciplines: Cardiovascular Medicine, Nephrology
                Keywords: Anti-Thy1.1 nephritis, Transforming growth factor-β, Microfibrillar proteins, Glomerulus, Extracellular matrix, Mesangial cells

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