The internal region leucine-rich repeat 6 of decorin interacts with low density lipoprotein receptor-related protein-1, modulates transforming growth factor (TGF)-β-dependent signaling, and inhibits TGF-β-dependent fibrotic response in skeletal muscles

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dc.catalogadoraba
dc.contributor.authorCabello Verrugio, C.
dc.contributor.authorSantander, C.
dc.contributor.authorCofré, C.
dc.contributor.authorAcuña, M. J.
dc.contributor.authorMelo Ledermann, Francisco Javier
dc.contributor.authorBrandan, Enrique
dc.date.accessioned2025-02-06T20:08:04Z
dc.date.available2025-02-06T20:08:04Z
dc.date.issued2012
dc.description.abstractDecorin is a small proteoglycan, composed of 12 leucine-rich repeats (LRRs) that modulates the activity of transforming growth factor type β (TGF-β) and other growth factors, and thereby influences proliferation and differentiation in a wide array of physiological and pathological processes, such as fibrosis, in several tissues and organs. Previously we described two novel modulators of the TGF-β-dependent signaling pathway: LDL receptor-related protein (LRP-1) and decorin. Here we have determined the regions in decorin that are responsible for interaction with LRP-1 and are involved in TGF-β-dependent binding and signaling. Specifically, we used decorin deletion mutants, as well as peptides derived from internal LRR regions, to determine the LRRs responsible for these decorin functions. Our results indicate that LRR6 and LRR5 participate in the interaction with LRP-1 and TGF-β as well as in its dependent signaling. Furthermore, the internal region (LRR6i), composed of 11 amino acids, is responsible for decorin binding to LRP-1 and subsequent TGF-β-dependent signaling. Furthermore, using an in vivo approach, we also demonstrate that the LRR6 region of decorin can inhibit TGF-β mediated action in response to skeletal muscle injury.
dc.format.extent15 páginas
dc.fuente.origenSIPA
dc.identifier.doi10.1074/jbc.M111.312488
dc.identifier.eissn1083-351X
dc.identifier.issn0021-9258
dc.identifier.pubmedid22203668
dc.identifier.pubmedidPMC3307262
dc.identifier.urihttps://doi.org/10.1074/jbc.M111.312488
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/102197
dc.identifier.wosidWOS:000300791800063
dc.information.autorucFacultad de Ciencias Biológicas; Melo Ledermann, Francisco Javier; 0000-0002-0424-5991; 82342
dc.information.autorucFacultad de Ciencias Biológicas; Brandan, Enrique; 0000-0002-6820-5059; 52075
dc.issue.numero9
dc.language.isoen
dc.nota.accesocontenido completo
dc.pagina.final6787
dc.pagina.inicio6773
dc.revistaThe Journal of biological chemistry
dc.rightsacceso abierto
dc.rights.licenseAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subject.ddc570
dc.subject.deweyBiologíaes_ES
dc.subject.ods03 Good health and well-being
dc.subject.odspa03 Salud y bienestar
dc.titleThe internal region leucine-rich repeat 6 of decorin interacts with low density lipoprotein receptor-related protein-1, modulates transforming growth factor (TGF)-β-dependent signaling, and inhibits TGF-β-dependent fibrotic response in skeletal muscles
dc.typeartículo
dc.volumen287
sipa.codpersvinculados82342
sipa.codpersvinculados52075
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