PMID: 2123140Jan 1, 1990Paper

Heterogeneity in glycosylation of dermatan sulfate proteoglycan core proteins isolated from human aorta

Connective Tissue Research
T C Register, W D Wagner

Abstract

Small proteoglycans were dissociatively extracted from normal human thoracic aorta with 4 M guanidine hydrochloride containing protease inhibitors, and purified by Sepharose CL-4B chromatography, dissociative cesium chloride density gradient centrifugation, and diethylaminoethyl cellulose chromatography. The intact proteoglycans migrated in the 270,000-340,000 range on 4-20% sodium dodecyl sulfate polyacrylamide gradient gels. Core proteins prepared following digestion of the intact proteoglycan monomer with chondroitinase ABC consisted of a major Coomassie blue-staining protein band of 50,000 along with a minor band of 44,000. Subsequent studies using endoglycosidases H, F, and N-glycanase demonstrated that mainly complex type N-linked glycans were present on the 50,000 cores while the 44,000 cores appeared to be devoid of N-linked glycans. Western blotting demonstrated that both of these cores were recognized by the monoclonal antibody 2-B-6, indicating the presence of the terminal 4-sulfated unsaturated disaccharide (delta Di-4S) remaining on the linkage region following chondroitinase ABC digestion. In contrast, a diffuse pattern of delta Di-4S epitopes ranging from 50,000 to approximately 60,000 was observed following chon...Continue Reading

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Citations

May 15, 1993·Experientia·H KresseE Schönherr
Feb 17, 1998·Journal of Microencapsulation·T ModenaA Gazzaniga
Jan 1, 1992·Arteriosclerosis and Thrombosis : a Journal of Vascular Biology·R A RobbinsB Caterson
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Sep 1, 1996·Arteriosclerosis, Thrombosis, and Vascular Biology·R A ShirkW D Wagner

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