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Purification and characterization of iduronic acid-rich and glucuronic acid-rich proteoglycans implicated in human post-burn keloid scar

โœ Scribed by Hari G. Garg; Eric W. Lippay; D.Andrew R. Burd; Peter J. Neame


Publisher
Elsevier Science
Year
1990
Tongue
English
Weight
741 KB
Volume
207
Category
Article
ISSN
0008-6215

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โœฆ Synopsis


Small proteoglycans (PGs), extracted from human keloid scar tissue with 4M guanidinium chloride and fractionated by DEAE-cellulose chromatography, were separated by ethanol precipitation into one L-iduronic acid-rich and one D-glucuronic acid-rich fraction. The size of the L-iduronic acid-rich PG was 102 kDa with a 27 kDa glycosaminoglycan chain, that of the D-glucuronic acid-rich PG was 90 kDa with a 26 kDa glycosaminoglycan chain, and the protein core of both PGs was 14.5 kDa. The two PGs carried sulfate groups mostly attached at C-4 of the 2-amino-2-deoxy-D-galactose units. The N-terminal amino acid sequence of both was similar to human bone PGII (decorin), normal and hypertrophic scar, and human dermal tissue PG.


๐Ÿ“œ SIMILAR VOLUMES


Iduronic acid-rich proteoglycans (PGIdoA
โœ Hari G. Garg; John W. Siebert; Arvin Garg; Peter J. Neame ๐Ÿ“‚ Article ๐Ÿ“… 1995 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 502 KB

Proteoglycans (PGs) were extracted from human hypertrophic and normal scar tissues from two different stages of maturation after bum injury, under dissociative conditions (4 M guanidinium chloride containing proteinase inhibitors). The extracts were fractionated by ion-exchange chromatography, follo

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Hypertrophic scarring is characterized by disordered collagen fibrils. In order to determine whether this is, in part, a result of changes in the population of proteoglycans that are thought to be involved in regulation of collagen fibril formation, we have compared PGs from post-bum normal and hype