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: The data indicate that the different cells of the adult human kidney are characterized by a distinct expression pattern of the four small proteoglycans, which may have distinct pathophysiological roles depending upon whether they are expressed by mesangial cells, endothelial cells, epithelial cells and collecting ducts, or cells ofThe tubulointerstitium.
99 citations
TL;DR: The role of all the identified PG family members (CS, HS, HEP, DS, KS and HA) in normal CNS function and in the context of pathology are discussed.
99 citations
TL;DR: The data suggest that stage 23 to 24 mesenchyme cells undergo normal chondrogenic maturation in culture in the presence of xylosides even though most of the polysaccharides are synthesized onto the exogenously supplied xylOSide substrate and released into the medium, which is abnormal in general morphology.
99 citations
01 Jan 2002
TL;DR: Bone matrix proteoglycans and glycoproteins are proportionally the most abundant constituents of the noncollagenous proteins in bone matrix and exhibit a broad array of functions ranging from control of cell proliferation, cell-matrix interactions, and mediation of hydroxyapatite deposition.
Abstract: Publisher Summary Bone matrix proteoglycans and glycoproteins are proportionally the most abundant constituents of the noncollagenous proteins in bone matrix. Proteoglycan are characterized by the covalent attachment of long chain polysaccharides (glycosaminoglycans, GAGs) to core protein molecules. GAGs are composed of repeating carbohydrate units that are sulfated to varying degrees, and include chondroitin sulfate (CS), dermatan sulfate (DS), keratan sulfate (KS), and heparin sulfate (HS). Different subclasses of proteoglycan are generally characterized by the structure of the core protein and by the nature of the GAG. Proteoglycans with protein cores composed of the leucine-rich repeat sequences such as decorin, biglycan, fibromodulin, and osteoadherin, are the predominant form found in mineralized matrix, although hyaluronan-binding forms are present during early stages of osteogenesis. They participate in matrix organization and in regulating growth factor activity. Glycoproteins, such as alkaline phosphatase, osteonectin, RGD-containing proteins (osteoadherin, thrombospondin, fibronectin, vitronectin, osteopontin, bone sialoprotein), fibrillin, and tetranectin are produced at different stages of osteoblastic maturation. They exhibit a broad array of functions ranging from control of cell proliferation, cell-matrix interactions, and mediation of hydroxyapatite deposition. The ectopic expression of bone matrix proteins may also play a significant role in pathological states such as bone metastasis in certain forms of cancer and atherosclerosis.
98 citations
TL;DR: It is concluded that isolated chondrons are rich in proteoglycan monomer, which is particularly concentrated in the tail and interconnecting segments of the chondron where it could function to protect and stabilize the chONDrocyte.
Abstract: Chondrons have recently been extracted from adult articular cartilages and techniques developed to study their structure and composition in isolation. This study introduces methods to immobilize isolated canine chondrons in thin layers of agarose gel for immunohistochemistry and future in vitro studies. An antibody to Type VI collagen which stained the chondron in suspension was used to successfully validate the system and its feasibility for immunoelectron microscopy. Monoclonal and polyclonal antibodies to a variety of epitopes on the proteoglycan molecule were tested on fresh and fixed plugs cored from chondron-agarose gels. Plugs were immunolabeled with peroxidase-diaminobenzidine before or after digestion with testicular hyaluronidase or chondroitinase ABC. Trypsin/chymotrypsin were used to challenge epitopes of the core protein. The results indicate that epitopes to keratan sulfate, chondroitin sulfate, hyaluronate binding region, and core protein are localized in the chondron. Consistent staining was found in the tail and interconnecting segments between chondrons, whereas staining of the pericellular matrix and capsule adjacent to the chondrocyte varied according to the enzyme pre-treatment employed. We conclude that isolated chondrons are rich in proteoglycan monomer, which is particularly concentrated in the tail and interconnecting segments of the chondron where it could function to protect and stabilize the chondrocyte.
98 citations