Topic
Keratan sulfate
About: Keratan sulfate is a research topic. Over the lifetime, 1253 publications have been published within this topic receiving 57984 citations. The topic is also known as: keratan sulfate & KS.
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TL;DR: It appears that the role of the squid sulfotransferase is to synthesize so-called chondroitin sulfate E where over 50% of the interior hexosamine units are 4,6-bis-sulfated.
20 citations
TL;DR: A simple procedure using human basic fibroblast growth factor (FGF) was utilized for the selection of COS cell mutants with defects in the biosynthesis or expression of heparan sulfate proteoglycan (HSPG) based on the strong binding affinity exhibited by COS cells to basic FGF that had been adsorbed to plastic dishes.
20 citations
TL;DR: Fragments of large monomers containing keratan sulfate and hyaluronic acid binding region are the major component of similar fractions from old cartilage.
Abstract: Proteoglycans extracted from articular cartilage of large joints of humans aged 4, 11, 70 and 75, were fractionated on associative density gradients. The top fraction (A3) was purified by ion-exchange chromatography and subsequent gel filtration on Sepharose CL 4B in 4 M GuCl, 0.5% Triton x 100. Proteoglycans from young cartilages yielded a narrow rapid migrating band on gel electrophoresis, had a Kav of 0.43 and 0.44 on Sepharose CL 4B, a glucosamine/galactosamine ratio of 0.11 and 0.12 and a glycoprotein core rich in aspartic acid and leucine with a Mr of about 47,000. Proteoglycans from old cartilages gave a wider and slower migrating band on gel electrophoresis, had a wide peak with a Kav of 0.38 and 0.40 on Sepharose CL 4B, a glucosamine/galactosamine ratio of 5.1 and 3.2, a glycoprotein core rich in glutamic acid and glycine, and with a Mr of about 170,000-180,000. Analysis using monoclonal antibodies detected epitopes of keratarn sulfate and of hyaluronic acid binding region in the fractions from old but not in those from young cartilages. Small proteoglycans not derived from the large monomers are the major component of low-buoyant-density fractions of proteoglycans from young cartilages. Fragments of large monomers containing keratan sulfate and hyaluronic acid binding region are the major component of similar fractions from old cartilage.
19 citations
TL;DR: In chronic IgG-induced immune synovitis, anti-proteoglycan antibodies elicited are heterogeneous with regard to specificity, but a relatively large proportion predominantly recognized a portion of the proteoglycan molecule containing core protein and associated keratan sulfate.
Abstract: This study details the immune response to cartilage proteoglycan in experimental chronic IgG-induced immune synovitis. Antibodies reactive with purified rabbit proteoglycan monomer were observed in nine of nine rabbits with immune synovitis. IgG-immunized but nonsynovitic control animals with no pathology showed no antibody response. A panel of murine monoclonal antibodies with defined specificity towards rabbit proteoglycan were utilized to characterize the epitope specificity of the immune synovitis polyclonal anti-proteoglycan response. One murine monoclonal antibody, 6C11, inhibited the binding of the polyclonal antisera to proteoglycan in all nine animals with significant (greater than 40%) inhibition in six of nine rabbits. Further inhibition studies utilizing DEAE-cellulose-resolved proteoglycan tryptic peptides revealed that peptides poor in chondroitin sulfate were strong inhibitors of binding of the polyclonal antibodies to the proteoglycan substrate. In particular, keratan sulfate-containing tryptic peptides were most inhibitory on a per weight basis. These results indicate that, in chronic IgG-induced immune synovitis, anti-proteoglycan antibodies elicited are heterogeneous with regard to specificity, but a relatively large proportion predominantly recognized a portion of the proteoglycan molecule containing core protein and associated keratan sulfate.
19 citations
TL;DR: The preliminary analyses showed that the chondroitin sulphate from the acetabular cartilage contained exclusively 6-sulphated disaccharide units and there was some heterogeneity in keratan sulphate.
Abstract: The distribution of glycosaminoglycans (GAGs) in different functional regions (weight-bearing and nonweight-bearing portions) of the human hip joint cartilage was studied. The results obtained were as follows: (1) Weight-bearing cartilage contains larger amounts of GAGs than nonweight-bearing, cartilage. (2) Weight-bearing cartilage contains keratan sulphate in higher ratio to chondroitin sulphate than nonweight-bearing cartilage. (3) The differences in content and composition of GAGs between the weight-bearing and nonweight-bearing portions are more pronounced in the femoral head than in the acetabulum. The preliminary analyses showed that the chondroitin sulphate from the acetabular cartilage contained exclusively 6-sulphated disaccharide units and there was some heterogeneity in keratan sulphate.
19 citations