dc.creatorGomes L.
dc.creatorEsquisatto M.A.M.
dc.creatorBelline P.
dc.creatorPimentel E.R.
dc.date1996
dc.date2015-06-26T17:03:44Z
dc.date2015-11-26T14:19:09Z
dc.date2015-06-26T17:03:44Z
dc.date2015-11-26T14:19:09Z
dc.date.accessioned2018-03-28T21:20:35Z
dc.date.available2018-03-28T21:20:35Z
dc.identifier
dc.identifierBrazilian Journal Of Medical And Biological Research. , v. 29, n. 9, p. 1243 - 1246, 1996.
dc.identifier0100879X
dc.identifier
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-0030224420&partnerID=40&md5=1b5d99e94c40b282cdd80504beef0b4b
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/95641
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/95641
dc.identifier2-s2.0-0030224420
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1243856
dc.descriptionThe small proteoglycans fibromodulin and decorin may play an important role in regulating collagen fibrillogenesis and interactions with growth factors. Here, we describe the presence of these proteoglycans in cartilage submitted to different biomechanical forces. Fibromodulin from chicken and bovine articular cartilage was shown to self-associate. The different states of fibromodulin aggregation due to disulfide bonding demonstrable in different regions of the same joint suggest that the presence of different biomechanical forces results in the differential expression of small proteoglycans. A 250-kDa complex found in chicken tibiotarsal cartilage, which migrates as a 59-kDa component in SDS-PAGE under reducing conditions, and which was recognized by anti-fibromodulin antibodies, was not demonstrable in tarsometatarsal cartilage where a different fibromodulin complex has been recently demonstrated. Biglycan and decorin were not expressed in the same way in different regions of the bovine knee joint, suggesting that there is a relationship between the expression of small proteoglycans and the different biomechanical properties of a tissue.
dc.description29
dc.description9
dc.description1243
dc.description1246
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dc.descriptionHildebrand, A., Romaris, M., Rasmussen, L.H., Heinegård, D., Twardzik, D.R., Border, W.A., Ruoslahti, E., Interactions of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor ß (1994) Biochemical Journal, 302, pp. 527-534
dc.descriptionJohnstone, B., Markopoulos, M., Neame, P., Caterson, B., Identification and characterization of glycanated and non-glycanated forms of biglycan and decorin in the human intervertebral disc (1993) Biochemical Journal, 292, pp. 661-666
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dc.descriptionLiu, J., Laue, T.M., Choi, H.U., Tang, L.H., Rosenberg, L., The self-association of biglycan from bovine articular cartilage (1994) Journal of Biological Chemistry, 269, pp. 28366-28373
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dc.descriptionBidanset, D.J., Guidray, C., Rosenberg, L.C., Choi, H.U., Timpl, R., Hook, M., Binding of the proteoglycan decorin to collagen type VI (1992) Journal of Biological Chemistry, 267, pp. 5250-5256
dc.languageen
dc.publisher
dc.relationBrazilian Journal of Medical and Biological Research
dc.rightsaberto
dc.sourceScopus
dc.titleIs There A Relationship Between The State Of Aggregation Of Small Proteoglycans And The Biomechanical Properties Of Tissues?
dc.typeArtículos de revistas


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