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Proteodermatan and proteokeratan sulfate (decorin, lumican/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagen.
Biochemistry
July 1996
Department of Chemical Morphology, School of Biological Sciences, Manchester University, U.K.
The small proteoglycans proteodermatan and proteokeratan sulfates organize collagen fibrils in extracellular matrix [Scott, J. E. (1992) FASEB J.
View Article and Find Full Text PDFDevelopmental changes in proteoglycans of rabbit corneal stroma.
Invest Ophthalmol Vis Sci
September 1988
Rockefeller University, New York, NY 10021.
Proteoglycans have been extracted from rabbit corneal stromas at developmental stages from fetal to adult. Ion exchange fractionation and gel chromatography show that proteodermatan sulfates decrease in sulfation and relative amount and proteokeratan sulfates increase in sulfation and relative amount during development. There are small increases in size of all of the proteoglycans up to 2 weeks after birth, and the final adult composition is achieved by 8 weeks.
View Article and Find Full Text PDFIntralysosomal formation and metabolic fate of N-acetylglucosamine 6-sulfate from keratan sulfate.
Eur J Biochem
September 1985
The physiological relevance of the ability of beta-N-acetylhexosaminidase A to liberate N-acetylglucosamine 6-sulfate from polymeric keratan sulfate was investigated. Upon intravenous injection into rats of [35S]sulfate-labeled proteokeratan sulfate up to 25% of the radioactivity excreted with the urine were identified as N-acetyl-glucosamine 6-sulfate. Within 24 h, however, excretion of inorganic sulfate rose at the expense of the sulfated monosaccharide.
View Article and Find Full Text PDFHybridomas were developed that secreted monoclonal antibodies against two proteokeratan sulfates (PKS) from rabbit corneal stroma. A total of 28 antibodies were isolated, all of the IgG type with kappa light chains. All were found to react with both PKSs.
View Article and Find Full Text PDFIt had been suggested that Dyggve-Melchior-Clausen syndrome may be due to the deficiency of a specific sulfatase and/or a protease involved in proteoglycan degradation. The ability of Dyggve-Melchior-Clausen fibroblasts to endocytose and degrade 3H-leucine- and 35S-sulfate-labelled proteodermatan sulfate and 35S-sulfate-labelled proteokeratan sulfate, respectively, was therefore investigated. The turnover of cell-associated 35S-sulfate-labelled heparan sulfate was also followed.
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