Changes with age in the structure of fibromodulin in human articular cartilage.
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TLDR
Fibromodulin is present in human articular cartilage at all ages, but the extracted molecules only appear to exist in a proteoglycan form possessing keratan sulfate chains in the juvenile and young adult, and the size of these chains decreases with age.About:
This article is published in Osteoarthritis and Cartilage.The article was published on 1996-09-01 and is currently open access. It has received 68 citations till now. The article focuses on the topics: Keratan sulfate & Proteoglycan.read more
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The family of the small leucine-rich proteoglycans: key regulators of matrix assembly and cellular growth.
TL;DR: These proteoglycans are tissue organizers, orienting and ordering collagen fibrils during ontogeny and in pathological processes such as wound healing, tissue repair, and tumor stroma formation, and three-dimensional modeling of their prototype protein core proposes a flexible, arch-shaped binding surface suitable for strong and distinctive interactions with ligand proteins.
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Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon.
TL;DR: In this paper, the authors show that mice lacking a functional fibromodulin gene exhibit an altered morphological phenotype in tail tendon with fewer and abnormal collagen fiber bundles, and they demonstrate that the orchestrated action of several leucine-rich repeat glycoproteins/proteoglycans influence the architecture of collagen matrices.
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The structure and function of cartilage proteoglycans.
TL;DR: The structure/function relationships of the cartilage proteoglycans are discussed, and the manner in which perturbations in proteoglycan structure or abundance can adversely affect tissue function is discussed.
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Articular cartilage and changes in arthritis: noncollagenous proteins and proteoglycans in the extracellular matrix of cartilage.
TL;DR: A selective survey of noncollagenous proteins in its extracellular matrix, including proteoglycans, is provided and discusses their structure, function, and involvement in inherited and arthritic disorders.
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SLRP interaction can protect collagen fibrils from cleavage by collagenases.
TL;DR: Interaction with either recombinant decorin, fibromodulin or lumican results in decreased collagenase cleavage of both fibril types, thus SLRP interaction can help protect collagen fibrils from cleavage by collagenases.
References
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Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.
TL;DR: A method has been devised for the electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets that results in quantitative transfer of ribosomal proteins from gels containing urea.
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Polypeptides of the tail fibres of bacteriophage T4
Jonathan King,Ulrich K. Laemmli +1 more
TL;DR: The products of four of the six genes involved in bacteriophage T4 tail fibre assembly by sodium dodecyl sulphate-acrylamide gel electrophoresis of tail fibre mutant lysates and particles purified from them are identified, allowing the formulation in greater detail of the early stages of the fibre assembly pathway.
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Deduced protein sequence of bone small proteoglycan I (biglycan) shows homology with proteoglycan II (decorin) and several nonconnective tissue proteins in a variety of species.
TL;DR: The derived protein sequence of PG I showed sufficient homology with the PG II sequence to strongly suggest that the two proteins were the result of a gene duplication, and it is suggested that PG I be called biglycan.
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Proteoglycan-fibrillar collagen interactions
TL;DR: Interactions in connective tissues, including those between the proteoglycans and collagens are especially piquant, evolutionarily conserved and physiologically significant, and methods for diagnosing interactions are developed.
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Interaction of Biglycan with Type I Collagen
TL;DR: Recombinant biglycan and decorin were characterized by lower dissociation constants compared with the glycanated forms, suggesting that, because of its trivalency,biglycan could have a special organizing function on the assembly of the extracellular matrix.
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