Document Detail


Decorin core protein fragment Leu155-Val260 interacts with TGF-beta but does not compete for decorin binding to type I collagen.
MedLine Citation:
PMID:  9675033     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
It has been shown that small proteoglycans containing leucine-rich repeats in their core proteins can form complexes with TGF-beta. Decorin, a ubiquitously found molecule of the extracellular matrix, is the best-studied example. Therefore, binding domains on its core protein were investigated using recombinant decorin fragments generated as fusion proteins in prokaryotes. The peptide Leu155-Val260 immobilized by the polyhistidine tag on a nickel chelate column bound TGF-beta1 and -beta2 almost as effectively as the largest fragment (Asp45-Lys359) studied. Other peptides were less effective. For the two peptides Asp45-Lys359 and Leu155-Val260 dissociation constants in the nanomolar range for high-affinity binding sites were calculated in a solid-phase assay with immobilized TGF-beta2. Peptide Asp45-Lys359 also contained a lower affinity binding site. Domains with lower affinity were also found in peptides Asp45-Leu155 and Arg63-Gly190. Peptide Leu155-Val260 also formed complexes with TGF-beta in the liquid phase as determined by equilibrium gel filtration. Furthermore, F(ab') fragments of polyclonal antibodies against peptide Leu155-Val260 interfered with TGF-beta binding to peptide Asp45-Lys359 in a dose-dependent manner. Peptide Leu155-Val260, however, is only a weak competitor of the binding of wild-type decorin to reconstituted type I collagen fibrils. Therefore, independent binding sites of decorin for TGF-beta and type I collagen should exist. In support of this hypothesis saturable binding of TGF-beta1 and TGF-beta2 to collagen-bound native decorin could be demonstrated. The bound cytokine could be released in a biologically active form by collagenase treatment. Thus, decorin may play a biological role in storing this cytokine temporarily in the extracellular matrix and in thereby modulating an interaction of TGF-beta with its signaling receptors.
Authors:
E Schönherr; M Broszat; E Brandan; P Bruckner; H Kresse
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Archives of biochemistry and biophysics     Volume:  355     ISSN:  0003-9861     ISO Abbreviation:  Arch. Biochem. Biophys.     Publication Date:  1998 Jul 
Date Detail:
Created Date:  1998-08-18     Completed Date:  1998-08-18     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0372430     Medline TA:  Arch Biochem Biophys     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  241-8     Citation Subset:  IM    
Copyright Information:
Copyright 1998 Academic Press.
Affiliation:
Institute of Physiological Chemistry and Pathobiochemistry, University of Münster, Waldeyerstrasse 15, Münster, D-48149, Germany. schonhe@uni-muenster.de
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MeSH Terms
Descriptor/Qualifier:
Binding Sites
Binding, Competitive
Chromatography, Gel
Collagen / metabolism*
Extracellular Matrix Proteins
Humans
Immune Sera / pharmacology
Immunoglobulin Fab Fragments / metabolism,  pharmacology
Leucine / metabolism
Monocytes
Peptide Fragments / immunology,  metabolism
Protein Binding
Proteoglycans / genetics,  metabolism*
Recombinant Proteins / metabolism
Transforming Growth Factor beta / metabolism*
Tumor Cells, Cultured
Valine / metabolism
Chemical
Reg. No./Substance:
0/Extracellular Matrix Proteins; 0/Immune Sera; 0/Immunoglobulin Fab Fragments; 0/Peptide Fragments; 0/Proteoglycans; 0/Recombinant Proteins; 0/Transforming Growth Factor beta; 0/decorin; 61-90-5/Leucine; 7004-03-7/Valine; 9007-34-5/Collagen

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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