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 keratan sulfate-containing proteoglycans were isolated from fourteen pooled human corneas and showed significantly higher levels of α(1-3)-fucosylated repeat region structures than did the bovine sample, and it is not clear whether this reflects a species or age dependence.
40 citations
TL;DR: Observations show that C6ST could transfer sulfate to position 6 of Gal residue of SLN, suggesting that sulfate moiety attached to adjacent GlcNAc residue may stimulate the transfer of sulfates to Gal residue.
Abstract: We have previously shown that chondroitin 6-sulfotransferase (C6ST) catalyzes transfer of sulfate not only to position 6 of GalNAc residue of chondroitin but also to position 6 of Gal residue of keratan sulfate. In this study, we examined the sulfation of sialyl lactosamine oligosaccharides by C6ST. C6ST catalyzed transfer of sulfate to NeuAc alpha 2-3Gal beta 1-4GlcNAc (SLN), NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-3Gal beta 1-4GlcNAc (SL1L1), NeuAc alpha 2-3Gal beta 1-4(6-sulfo)GlcNAc beta 1-3(6-sulfo)Gal beta 1-4(6-sulfo)GlcNAc (SL2L4), and their desialylated derivatives, but not to NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc (SLe(x)). The sulfated product formed from SLN was degraded with neuraminidase and reduced with NaBH4. The resulting sulfated disaccharide alditol showed the same retention time in SAX-HPLC as that of [3H]Gal(6SO4) beta 1-4GlcNAc-ol. The sulfated product formed from SLN was also degraded by a reaction sequence of neuraminidase digestion, hydrazinolysis, deamination, and NaBH4 reduction. The final product was coeluted with [3H]Gal(6SO4) beta 1-4anhydromannitol in SAX-HPLC. These observations show that C6ST could transfer sulfate to position 6 of Gal residue of SLN. Incorporation of sulfate into SL2L4 was much higher than the incorporation into SL1L1, suggesting that sulfate moiety attached to adjacent GlcNAc residue may stimulate the transfer of sulfate to Gal residue. The recombinant C6ST also catalyzed sulfation of the sialyl lactosamine oligosaccharides, indicating that a single protein catalyzes sulfation of chondroitin, keratan sulfate, and sialyl lactosamine oligosaccharides. These results raised a possibility that C6ST may be one of the candidates involved in the biosynthesis of sulfated sialyl Lewis x ligand for L-selectin.
40 citations
TL;DR: A comparison was made of the concentration and composition of the acidic glycosaminoglycans in human cornea, sclera and skin during five to nine months fetal development and in the adult.
Abstract: A comparison was made of the concentration and composition of the acidic glycosaminoglycans in human cornea, sclera and skin during five to nine months fetal development and in the adult. In skin, the concentration of the acidic glycosaminoglycans decreases gradually duringfetal development; the adult value is still less than the newborn; hyaluronic acid and dermatan sulfate are always present. In sclera, during the same period of development the concentration of the acidic glycosaminoglycans varied little; dermatan sulfate is the main component in both fetus and adult but the latter also contains some hyaluronic acid and chondroitin 4(6)-sulfate. The concentration of the acidic glycosaminoglycans in cornea increased by 33% at seven months gestation and remained constant; fetal cornea has chondroitin 4(6)-sulfate, chondroitin and a small amount of keratan sulfate (18 to 27% of the acidic glycosaminoglycans); in contrast, the adult cornea is rich in keratan sulfate (64 % of the acidic glycosaminoglycans) a...
40 citations
TL;DR: The results suggested that the synthesis of chondroitin sulfate on proteoglycan only occurs in medial/trans-Golgi cisternae as a late event in proteoglycans biosynthesis, and suggests that glycosaminoglycan synthesis on proteglycans takes place in a compartment in common with events in the biosynthesis of both O-linked and N-linked oligosaccharides on other secretory glycoproteins.
Abstract: The intracellular pathway of cartilage proteoglycan biosynthesis was investigated in isolated chondrocytes using a protein A-gold electron microscopy immunolocalization procedure. Proteoglycans contain a protein core to which chondroitin sulfate and keratan sulfate chains and oligosaccharides are added in posttranslational processing. Specific antibodies have been used in this study to determine separately the distribution of the protein core and chondroitin sulfate components. In normal chondrocytes, proteoglycan protein core was readily localized only in smooth-membraned vesicles which co-labeled with ricin, indicating them to be galactose-rich medial/trans-Golgi cisternae, whereas there was only a low level of labeling in the rough endoplasmic reticulum. Chondroitin sulfate was also localized in medial/trans-Golgi cisternae of control chondrocytes but was not detected in other cellular compartments. In cells treated with monensin (up to 1.0 microM), which strongly inhibits proteoglycan secretion (Burditt, L.J., A. Ratcliffe, P. R. Fryer, and T. Hardingham, 1985, Biochim. Biophys. Acta., 844:247-255), there was greatly increased intracellular localization of proteoglycan protein core in both ricin-positive vesicles, and in ricin-negative vesicles (derived from cis-Golgi stacks) and in the distended rough endoplasmic reticulum. Chondroitin sulfate also increased in abundance after monensin treatment, but continued to be localized only in ricin-positive vesicles. The results suggested that the synthesis of chondroitin sulfate on proteoglycan only occurs in medial/trans-Golgi cisternae as a late event in proteoglycan biosynthesis. This also suggests that glycosaminoglycan synthesis on proteoglycans takes place in a compartment in common with events in the biosynthesis of both O-linked and N-linked oligosaccharides on other secretory glycoproteins.
40 citations
TL;DR: The matrix components of the mandibular condyle seem to be adapted to its special functional needs including parallel articulation and growth, which may be involved in the control of cell proliferation and differentiation.
40 citations