Defective Glycosaminoglycan Substitution of Decorin in a Patient With Progeroid Syndrome Is a Direct Consequence of Two Point Mutations in the Galactosyltransferase I (ß4galT-7) Gene

@article{Gtte2005DefectiveGS,
  title={Defective Glycosaminoglycan Substitution of Decorin in a Patient With Progeroid Syndrome Is a Direct Consequence of Two Point Mutations in the Galactosyltransferase I (\ss4galT-7) Gene},
  author={Martin G{\"o}tte and Hans Kresse},
  journal={Biochemical Genetics},
  year={2005},
  volume={43},
  pages={65-77}
}
The small dermatan sulfate proteoglycan decorin is involved in the regulation of collagen fibrillogenesis, cell adhesion and migration, and growth factor signaling. In a progeroid patient carrying two point mutations in ß4galactosyltransferase I (ß4galT-7) only 50% of the decorin core protein molecules are substituted with glycosaminoglycan chains. We expressed decorin, as well as wild-type and mutant alleles of ß4galT-7 in galactosyltransferase-deficient CHO618 cells. Decorin was less… CONTINUE READING

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Tenascin–X deficiency is associated with Ehlers–Danlos syndrome

Nature Genetics • 1997
View 4 Excerpts
Highly Influenced

Decorin is required to maintain commited skeletal muscle cell population grouped allowing normal differentiation in vivo

H. Olguin, E. Brandan
Mol. Biol. Cell 13S:1918. • 2002
View 4 Excerpts
Highly Influenced

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