Impaired degradation of chondroitin sulfate in GM2-gangliosidosis.

Abstract

We have prepared a new radiolabeled substrate, derived from chondroitin 6-sulfate oligosaccharide, for the assaying of chondroitin sulfate degradation by beta-N-acetylgalactosaminidase. Using this substrate, we found a striking deficiency of beta-N-acetylgalactosaminidase activity in the cultured skin fibroblasts of patients with Sandhoff disease and Tay-Sachs disease. DEAE-cellulose chromatography at pH 6.0 revealed that both isoenzymes A and B of beta-N-acetylgalactosaminidases from normal human liver participated in the catabolism of chondroitin 6-sulfate. However, there were major differences in substrate specificity between isoenzyme A and isoenzyme B.

• Authors: T Yutaka, T Kato, S Okada, H Yabuuci
• Journal: Clinical genetics (Clin Genet) Vol. 22 Issue 4 Pg. 165-71 (Oct 1982) ISSN: 0009-9163 [Print] Denmark
• PMID: 6217929 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Chondroitin
• Chondroitin Sulfates
• Hexosaminidases
• beta-N-Acetylhexosaminidases

Topics

• Cells, Cultured
• Chondroitin (analogs & derivatives)
• Chondroitin Sulfates (metabolism)
• Fibroblasts (enzymology)
• Hexosaminidases (isolation & purification, metabolism)
• Humans
• Liver (enzymology)
• Sandhoff Disease (enzymology)
• Skin (enzymology)
• Tay-Sachs Disease (enzymology)
• beta-N-Acetylhexosaminidases