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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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Journal ArticleDOI
TL;DR: Molecules bearing carbohydrates recognized by anti-keratan sulfate antibodies appear at developmentally important stages of keratinocyte differentiation, indicating that these carbohydrates may serve as markers for molecules important in the differentiation of human keratinocytes.

26 citations

Journal ArticleDOI
TL;DR: The structure of this oligosaccharide shows that keratan sulphate chains from bovine intervertebral disc have non-reducing termini with N-acetylneuraminic acid linked alpha(2----6) as well as alpha( 2----3) to an unsulphated galactose.
Abstract: Peptido-keratan sulphate fragments were isolated from the nucleus pulposus of bovine intervertebral discs (2-year-old animals) after digestion with chondroitin ABC lyase followed by digestion with diphenylcarbamoyl chloride-treated trypsin of A1D1 proteoglycans and gel-permeation chromatography on Sepharose CL-6B. The peptido-keratan sulphate fragments were subjected to alkaline borohydride reduction. The reduced chains were treated with keratanase in the presence of the sialidase inhibitor 2,3-dehydro-2-deoxy-N-acetylneuraminic acid, and the digest was subjected to alkaline borohydride reduction. This produced oligosaccharides with galactitol at their reducing ends. This reduced digest was chromatographed on a Nucleosil 5 SB anion-exchange column and individual oligosaccharides were isolated. One of these was shown by 600 MHz 1H-n.m.r. spectroscopy to have the following structure: NeuAc alpha 2-6Gal beta 1-4GlcNAc(6-SO4)beta 1-3Gal-ol The structure of this oligosaccharide shows that keratan sulphate chains from bovine intervertebral disc have non-reducing termini with N-acetylneuraminic acid linked alpha(2----6) as well as alpha(2----3) to an unsulphated galactose.

25 citations

Journal ArticleDOI
TL;DR: This is the first report showing the presence of KS in zebra fish eye, and the structural characterization of CS and its localization in the zebrafish retina.
Abstract: The zebrafish Danio rerio (Chordata-Cyprinidae) is a model organism frequently used to study the functions of proteoglycans and their glycosaminoglycan (GAG) chains. Although several studies clearly demonstrate the participation of these polymers in different biological and cellular events that take place during embryonic development, little is known about the GAGs in adult zebrafish. In the present study, the total GAGs were extracted from the whole fish by proteolytic digestion, purified by anion-exchange chromatography and characterized by electrophoresis after degradation with specific enzymes and/or by high-performance liquid chromatography (HPLC) analysis of the disaccharides. Two GAGs were identified: a low-molecular-weight chondroitin sulfate (CS) and keratan sulfate (KS), corresponding to ∼80% and 20% of the total GAGs, respectively. In the fish eye, KS represents ∼ 80% of total GAGs. Surprisingly, no heparinoid was detected, but may be present in the fish at concentrations lower than the limit of the method used. HPLC of the disaccharides formed after chondroitin AC or ABC lyase degradation revealed that the zebrafish CS is composed by ΔUA-1→3-GalNAc(4SO4) (59.4%), ΔUA-1→3-GalNAc(6SO4) (23.1%), and ΔUA-1→3-GalNAc (17.5%) disaccharide units. No disulfated disaccharides were detected. Immunolocalization on sections from zebrafish retina using monoclonal antibodies against CS4- or 6-sulfate showed that in the retina these GAGs are restricted to the outer and inner plexiform layers. This is the first report showing the presence of KS in zebrafish eye, and the structural characterization of CS and its localization in the zebrafish retina. Detailed information about the structure and tissue localization of GAGs is important to understand the functions of these polymers in this model organism.

25 citations

Journal ArticleDOI
TL;DR: The rationale for the contention that this elevation in the rate of proteoglycan turnover precedes clinical evidence of degenerative changes may predispose adult humans to polyarticular osteoarthritis is discussed.

25 citations

Journal ArticleDOI
TL;DR: Increases in sulfation of proteoglycans with advancing age may be correlated with progress of corneal transparency, which begins on Day 14 and continues until hatching, and catabolism of keratan sulfate proteoglycan might be preferentially accelerated during those times.
Abstract: Proteoglycan biosynthesis in developing chicken corneas was studied. Corneas free of scleral rims were prepared from 5- to 18-day-old chick embryos and labeled in vitro with [3H]glucosamine and [35S]sulfate. Then, the labeled medium and corneal proteoglycans were analyzed. Day 5 corneas synthesized mainly chondroitin sulfate/dermatan sulfate proteoglycan and a sudden increase in keratan sulfate proteoglycan synthesis was found on Day 7. Keratan sulfate proteoglycan in Day 7 cornea appeared to be synthesized by fibroblasts which invaded the stroma between Day 5 and Day 7. The proportion of keratan sulfate proteoglycan synthesis increased with advancing embryonic age until Day 14 and declined a little on Day 18. The relative proportion of chondroitin sulfate/dermatan sulfate proteoglycan synthesis changed in a reverse curve during Day 7 to Day 18. Because embryonic cornea begins to become transparent on Day 14, this change in proteoglycan synthesis may be correlated with the onset of transparency. The labeled glycosaminoglycans were isolated from cultured embryonic corneas by pronase digestion, and then digested with chondroitinase ABC or keratanase II. Disaccharides in the enzymatic digests were analyzed by HPLC, and the extents and positions of sulfation of proteoglycans were determined. Sulfation of keratan sulfate proteoglycan continued to increase with advancing age until Day 18. Moreover, it has been shown by HPLC of unsaturated disaccharides of chondroitinase ABC digests that, whereas a comparable amount of non-sulfated "chondroitin sulfate/dermatan sulfate" was synthesized during Day 7 to Day 9, its amount declined during late development (Day 12 to Day 18). Such increases in sulfation of proteoglycans with advancing age may be correlated with progress of corneal transparency, which begins on Day 14 and continues until hatching. Analysis of proteoglycans of the culture medium has shown that most of the medium proteoglycans were keratan sulfate proteoglycan and free keratan sulfate chain (or keratan sulfate chain with a short peptide) during all ages after Day 7, although the major proteoglycan of Day 5 medium was chondroitin sulfate/dermatan sulfate proteoglycan. Sulfation of medium keratan sulfate also increased with advancing age. In addition, the proportion of free keratan sulfate chain in the medium increased during late corneal development, suggesting that catabolism of keratan sulfate proteoglycan might be preferentially accelerated during those times.

25 citations


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