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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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Book ChapterDOI
01 Jan 1980
TL;DR: The segregation of the proteoglycans into a separate category is based on a few specific characteristics, including the fact that the d-glucuronic-acid-containing repeating disaccharide of chondroitin, N-acetylchondrosine, has recently been identified as a component of thyroglobulin.
Abstract: With the possible exception of hyaluronic acid, the connective tissue polysaccharides are all synthesized by their parent cells as components of proteoglycans. In these substances, a number of polysaccharide chains are covalently linked to a protein core; e.g., in the proteoglycan of bovine nasal cartilage, which is the prototype of molecules of this kind, close to 100 chondroitin sulfate chains, with a molecular weight of approximately 20,000, and slightly fewer keratan sulfate chains are linked to a core protein (mol. wt. 200,000) which constitutes 7–8% of the entire molecule. In many respects, the proteoglycans are similar to other protein-bound complex carbohydrates, and the conspicuous polysaccharide component per se does not distinguish the proteoglycans from the class of glycoproteins; e.g., there are members of the glycoprotein class, such as the blood group substances, which have a high relative content of carbohydrate consisting of a substantial number of monosaccharide units. Rather, the segregation of the proteoglycans into a separate category is based on a few specific characteristics: (1) each polysaccharide consists of repeating disaccharide units in which a hexosamine, d-glucosamine, or d-galactosamine is always present; (2) all connective tissue polysaccharides except keratan sulfate contain a uronic acid, either d-glucuronic acid or its 5-epimer, l-iduronic acid, or both; (3) ester sulfate groups are present in all members of the group except in hyaluronic acid; in addition, N-sulfate groups are found in heparin and heparan sulfate. Although certain other bipolymers are known to contain ester sulfate, e.g., some epithelial mucins (Horowitz, 1977), these compounds are clearly distinguishable from the connective tissue polysaccharides by the other criteria indicated above. It may also be mentioned that the d-glucuronic-acid-containing repeating disaccharide of chondroitin, N-acetylchondrosine, has recently been identified as a component of thyroglobulin (Spiro, 1977); however, since the disaccharide is present as a single unit, thyroglobulin may not be considered a proteoglycan.

393 citations

Journal ArticleDOI
TL;DR: The data suggest that keratan sulfate, alone or in combination with other molecules expressed by the roof plate, may be responsible, in part, for the inhibition of axon elongation through the roof Plate in the embryonic spinal cord.

391 citations

Journal ArticleDOI
TL;DR: The 1/20/5-D-4 monoclonal antibody appears to recognize a common determinant in their polysaccharide moieties, consistent with several biochemical analyses showing the absence of keratan sulfate in proteoglycan synthesised by this tissue.

385 citations

Journal ArticleDOI
TL;DR: Findings have served to expand the concept of what keratan sulfate is and the potential roles it may play in the cellular biology of diverse tissues.
Abstract: The last 5 years have seen a marked increase in research on keratan sulfate (KS) and a concomitant increase in our understanding of the range of molecules that carry this adaptable polysaccharide. More than 15 KS-linked proteins have been identified and many of the genes encoding these have been cloned. KS-containing molecules have been identified in numerous epithelial and neural tissues in which KS expression responds to embryonic development, physiological variations, and to wound healing. A corneal cell culture system has been developed in which long-term KS biosynthesis is maintained. Progress has been made toward identification of the glycosyl- and sulfotransferases responsible for KS biosynthesis. A mouse knockout of a corneal KS-proteoglycan has provided the first experimental support for the role of KS in corneal transparency. Evidence has also been presented supporting functional roles of KS in cellular recognition of protein ligands, axonal guidance, cell motility, and in embryo implantation. These findings have served to expand the concept of what keratan sulfate is and the potential roles it may play in the cellular biology of diverse tissues.

376 citations

Journal ArticleDOI
TL;DR: The largest in size and most abundant by weight is aggrecan, a proteoglycan that possesses over 100 chondroitin sulfate and keratan sulfate chains that provides cartilage with its osmotic properties, which give articular cartilage its ability to resist compressive loads.
Abstract: Hyaline cartilage contains five well-characterized proteoglycans in its extracellular matrix, and it is likely that others exist. The largest in size and most abundant by weight is aggrecan, a proteoglycan that possesses over 100 chondroitin sulfate and keratan sulfate chains. Aggrecan is also characterized by its ability to interact with hyaluronic acid to form large proteoglycan aggregates. Both the high anionic charge on the individual aggrecan molecules endowed by the sulfated glycosaminoglycan chains and the localization within the matrix endowed by aggregate formation are essential for aggrecan function. The molecule provides cartilage with its osmotic properties, which give articular cartilage its ability to resist compressive loads. The other proteoglycans are characterized by their ability to interact with collagen. They are much smaller than aggrecan in size but may be present in similar molar amounts. Decorin, biglycan, and fibromodulin are closely related in protein structure but differ in glycosaminoglycan composition and function. Decorin and biglycan possess one and two dermatan sulfate chains, respectively, whereas fibromodulin bears several keratan sulfate chains. Decorin and fibromodulin both interact with the type II collagen fibrils in the matrix and may play a role in fibrillogenesis and interfibril interactions. Biglycan is preferentially localized in the pericellular matrix, where it may interact with type VI collagen. Finally, type IX collagen can also be considered as a proteoglycan, as its α2(IX) chain may bear a glycosaminoglycan chain. It may serve as a bridge between the collagen fibrils or with the interspersed aggrecan network. © 1994 Wiley-Liss, Inc.

350 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
202310
202222
20217
20209
201912
201812