Organization of glycosaminoglycan chains in a chondroitin sulfate - dermatan sulfate proteoglycan from bovine aorta

1986 ◽  
Vol 882 (1) ◽  
pp. 85-96 ◽  
Author(s):  
Bhandaru Radhakrishnamurthy ◽  
Neil Jeansonne ◽  
Gerald S. Berenson
1975 ◽  
Vol 171 (1) ◽  
pp. 361-369 ◽  
Author(s):  
Kenneth C. Ehrlich ◽  
Bhandaru Radhakrishnamurthy ◽  
Gerald S. Berenson

Author(s):  
Yi-Fan Huang ◽  
Shuji Mizumoto ◽  
Morihisa Fujita

Glycosaminoglycans (GAGs) including chondroitin sulfate, dermatan sulfate, heparan sulfate, and keratan sulfate, except for hyaluronan that is a free polysaccharide, are covalently attached to core proteins to form proteoglycans. More than 50 gene products are involved in the biosynthesis of GAGs. We recently developed a comprehensive glycosylation mapping tool, GlycoMaple, for visualization and estimation of glycan structures based on gene expression profiles. Using this tool, the expression levels of GAG biosynthetic genes were analyzed in various human tissues as well as tumor tissues. In brain and pancreatic tumors, the pathways for biosynthesis of chondroitin and dermatan sulfate were predicted to be upregulated. In breast cancerous tissues, the pathways for biosynthesis of chondroitin and dermatan sulfate were predicted to be up- and down-regulated, respectively, which are consistent with biochemical findings published in the literature. In addition, the expression levels of the chondroitin sulfate-proteoglycan versican and the dermatan sulfate-proteoglycan decorin were up- and down-regulated, respectively. These findings may provide new insight into GAG profiles in various human diseases including cancerous tumors as well as neurodegenerative disease using GlycoMaple analysis.


2000 ◽  
Vol 275 (45) ◽  
pp. 35448-35456 ◽  
Author(s):  
Hiroto Kawashima ◽  
Mayumi Hirose ◽  
Jun Hirose ◽  
Daisuke Nagakubo ◽  
Anna H. K. Plaas ◽  
...  

1986 ◽  
Vol 34 (8) ◽  
pp. 1013-1019 ◽  
Author(s):  
B Voss ◽  
J Glössl ◽  
Z Cully ◽  
H Kresse

Polyclonal antibodies against the core protein of the small chondroitin sulfate-dermatan sulfate proteoglycan from human skin fibroblast secretions were used, after affinity-purification, as a probe to study localization of crossreactive material in several human tissues by indirect immunocytochemistry. In contrast to skin, kidney, and the adventitial layer of aorta, positive staining of brain, liver, cartilage, and intimal and medial layers of aorta required pre-treatment of tissue sections with chondroitin ABC lyase. In all tissues investigated, antigenic material was present in the interstitial space. Filamentous structures were perpendicularly oriented towards basement membranes. In liver, specific staining was seen along the sinusoidal walls. Reticular fibers with or without focal condensations were seen in cerebral cortex and cerebellum. The results suggest a role of small chondroitin sulfate-dermatan sulfate proteoglycan in cell-matrix interactions.


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