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.
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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)
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Chemical References |
- Chondroitin Sulfate Proteoglycans
- Glycosaminoglycans
- LUM protein, human
- Lumican
- Proteoglycans
- proteodermatan sulfate
- Dermatan Sulfate
- Chondroitin
- Heparitin Sulfate
- Keratan Sulfate
- Chondroitin Lyases
- Leucine
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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)
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