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: Results indicate that the repeated use of IA MPA leads to a potentially harmful inhibition of procollagen II synthesis and an increased release of degradation products of the PG aggrecan from articular cartilage.
54 citations
TL;DR: A larger size, a greater overall hydrophobicity and an absence of O-linked oligosaccharides argue that this core protein is a distinct gene product from the core protein of the dermatan sulfate proteoglycan.
53 citations
Journal Article•
TL;DR: Corneas with macular dystrophy still contained abundant intra- and extracellular material with the histochemical attributes of nonextracted pathologic corneas, and this correlated with concentrations ofNonextracted isotope as shown by autoradiography.
53 citations
TL;DR: An important role for BGN is suggested in dentin formation and mineralization in predentin, an effect possibly attributable to the deglycosylation action of stromelysin-1.
Abstract: Small leucine-rich proteoglycans (SLRPs) regulate extracellular matrix organization. In order to investigate the distribution and potential functions of decorin, biglycan (BGN), and fibromodulin (3 SLRPs, potentially related to dentinogenesis), we performed light and electron immunochemistry on teeth from rats, and on wild-type and biglycan knockout mice (BGN KO). Immunohistochemical data demonstrate that chondroitin sulfate/dermatan sulfate (CS/DS) and keratan sulfate (KS) distributions displayed reverse gradients in predentin. The decrease of CS/DS labeling from the proximal to the distal predentin contrasted with the sharp decorin increase observed in the distal predentin near the predentin/dentin transition, an effect possibly attributable to the deglycosylation action of stromelysin-1. In contrast, BGN concentration was apparently constant throughout the whole predentin. Additional immunolabelings showed, for the first time, the presence of fibromodulin in predentin. Compared with the wild-type mouse...
53 citations
TL;DR: Tissue contents of small, easily extracted, proteoglycans, relatively poor in keratan sulphate, were compared in normal and osteoarthrotic cartilage and some proteoglyCans in the diseased cartilage were much more readily extracted than those in the normal tissue.
Abstract: Tissue contents of small, easily extracted, proteoglycans, relatively poor in keratan sulphate, were compared in normal and osteoarthrotic cartilage. Although the amounts of small proteoglycans were similar in each tissue, as were the collagen contents, some proteoglycans in the diseased cartilage were much more readily extracted than those in the normal tissue.
53 citations