Decorin core protein fragment Leu155-Val260 interacts with TGF-β but does not compete for decorin binding to type I collagen

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dc.contributor.authorSchönherr, E
dc.contributor.authorBroszat, M
dc.contributor.authorBrandan, E
dc.contributor.authorBruckner, P
dc.contributor.authorKresse, H
dc.date.accessioned2025-01-21T01:32:35Z
dc.date.available2025-01-21T01:32:35Z
dc.date.issued1998
dc.description.abstractIt 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-beta 1 and -beta 2 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-beta 2. 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-beta 1 and TGF-beta 2 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. (C) 1998 Academic Press.
dc.fuente.origenWOS
dc.identifier.issn0003-9861
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/97286
dc.identifier.wosidWOS:000075269600016
dc.issue.numero2
dc.language.isoen
dc.pagina.final248
dc.pagina.inicio241
dc.revistaArchives of biochemistry and biophysics
dc.rightsacceso restringido
dc.subjectdecorin
dc.subjectTGF-beta
dc.subjectcore protein
dc.subjectproteoglycan
dc.subjectinteraction
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleDecorin core protein fragment Leu155-Val260 interacts with TGF-β but does not compete for decorin binding to type I collagen
dc.typeartículo
dc.volumen355
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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