These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Defective glycosaminoglycan substitution of decorin in a patient with progeroid syndrome is a direct consequence of two point mutations in the galactosyltransferase I (beta4GalT-7) gene.
    Author: Götte M, Kresse H.
    Journal: Biochem Genet; 2005 Feb; 43(1-2):65-77. PubMed ID: 15859521.
    Abstract:
    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 beta4 galactosyltransferase I (beta4GalT-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 beta4GalT-7 in galactosyltransferase-deficient CHO618 cells. Decorin was less efficiently substituted with glycosaminoglycan chains upon expression of beta4GalT-7(186D) compared to beta4GalT-7-expressing cells. Decorin from beta4GalT-7-expressing cells displayed increased molecular heterogeneity. Decorin glycosaminoglycan chains were completely susceptible to chondroitinase ABC treatment. Cells expressing beta4GalT-7(206P) did not synthesize the proteoglycanform of decorin. Thus, the beta4GalT-7 mutations directly affect the molecular phenotype of decorin observed in a patient with the progeroid form of Ehlers-Danlos syndrome, which may be a major mechanistic cause for the skin and wound healing defects observed in this patient.
    [Abstract] [Full Text] [Related] [New Search]