Dyggve-Melchior-Clausen syndrome: normal degradation of proteodermatan sulfate, proteokeratan sulfate and heparan sulfate.

Abstract

It 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. In all these experiments Dyggve-Melchior-Clausen fibroblasts behaved normally.

• Authors: M Beck, R Lücke, H Kresse
• Journal: Clinica chimica acta; international journal of clinical chemistry (Clin Chim Acta) Vol. 141 Issue 1 Pg. 7-15 (Aug 15 1984) ISSN: 0009-8981 [Print] Netherlands
• PMID: 6235983 (Publication Type: Case Reports, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Chondroitin Sulfate Proteoglycans
• Glycosaminoglycans
• LUM protein, human
• Lumican
• Proteoglycans
• proteodermatan sulfate
• Dermatan Sulfate
• Chondroitin
• Heparitin Sulfate
• Keratan Sulfate
• Chondroitin Lyases
• Leucine

Topics

• Carbohydrate Metabolism, Inborn Errors (metabolism)
• Cells, Cultured
• Child
• Chondroitin (analogs & derivatives)
• Chondroitin Lyases (metabolism)
• Chondroitin Sulfate Proteoglycans (metabolism)
• Dermatan Sulfate (analogs & derivatives, metabolism)
• Electrophoresis, Polyacrylamide Gel
• Endocytosis
• Fibroblasts (metabolism)
• Glycosaminoglycans (metabolism)
• Heparitin Sulfate (metabolism)
• Humans
• Keratan Sulfate (metabolism)
• Leucine (metabolism)
• Lumican
• Male
• Molecular Weight
• Proteoglycans (metabolism)
• Skin (metabolism)