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Molecular characterization of beta 1,4-galactosyltransferase 7 genetic mutations linked to the progeroid form of Ehlers-Danlos syndrome (EDS)

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Molecular characterization of beta 1,4-galactosyltransferase 7 genetic mutations linked to the progeroid form of Ehlers-Danlos syndrome (EDS). / Bui, Catherine; Talhaoui, Ibtissam; Chabel, Matthieu; Mulliert, Guillermo; Coughtrie, Michael W. H.; Ouzzine, Mohamed; Fournel-Gigleux, Sylvie.

In: FEBS Letters, Vol. 584, No. 18, 24.09.2010, p. 3962-3968.

Research output: Contribution to journalArticle

Harvard

Bui, C, Talhaoui, I, Chabel, M, Mulliert, G, Coughtrie, MWH, Ouzzine, M & Fournel-Gigleux, S 2010, 'Molecular characterization of beta 1,4-galactosyltransferase 7 genetic mutations linked to the progeroid form of Ehlers-Danlos syndrome (EDS)' FEBS Letters, vol 584, no. 18, pp. 3962-3968., 10.1016/j.febslet.2010.08.001

APA

Bui, C., Talhaoui, I., Chabel, M., Mulliert, G., Coughtrie, M. W. H., Ouzzine, M., & Fournel-Gigleux, S. (2010). Molecular characterization of beta 1,4-galactosyltransferase 7 genetic mutations linked to the progeroid form of Ehlers-Danlos syndrome (EDS). FEBS Letters, 584(18), 3962-3968. 10.1016/j.febslet.2010.08.001

Vancouver

Bui C, Talhaoui I, Chabel M, Mulliert G, Coughtrie MWH, Ouzzine M et al. Molecular characterization of beta 1,4-galactosyltransferase 7 genetic mutations linked to the progeroid form of Ehlers-Danlos syndrome (EDS). FEBS Letters. 2010 Sep 24;584(18):3962-3968. Available from: 10.1016/j.febslet.2010.08.001

Author

Bui, Catherine; Talhaoui, Ibtissam; Chabel, Matthieu; Mulliert, Guillermo; Coughtrie, Michael W. H.; Ouzzine, Mohamed; Fournel-Gigleux, Sylvie / Molecular characterization of beta 1,4-galactosyltransferase 7 genetic mutations linked to the progeroid form of Ehlers-Danlos syndrome (EDS).

In: FEBS Letters, Vol. 584, No. 18, 24.09.2010, p. 3962-3968.

Research output: Contribution to journalArticle

Bibtex - Download

@article{ee58420722084d78bd0e0e0f58f1e1f0,
title = "Molecular characterization of beta 1,4-galactosyltransferase 7 genetic mutations linked to the progeroid form of Ehlers-Danlos syndrome (EDS)",
keywords = "Ehlers-Danlos syndrome, Point mutation, Galactosyltransferase defect, Glycosaminoglycan synthesis, Congenital glycosyltransferase disorder, Galactosyltransferase-I beta4GalT-7, Heparan sulfate, Protein, Biosynthesis, Proteoglycan, Fibroblasts, Expression, Patient, Binding, Identification",
author = "Catherine Bui and Ibtissam Talhaoui and Matthieu Chabel and Guillermo Mulliert and Coughtrie, {Michael W. H.} and Mohamed Ouzzine and Sylvie Fournel-Gigleux",
year = "2010",
doi = "10.1016/j.febslet.2010.08.001",
volume = "584",
number = "18",
pages = "3962--3968",
journal = "FEBS Letters",
issn = "0014-5793",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Molecular characterization of beta 1,4-galactosyltransferase 7 genetic mutations linked to the progeroid form of Ehlers-Danlos syndrome (EDS)

A1 - Bui,Catherine

A1 - Talhaoui,Ibtissam

A1 - Chabel,Matthieu

A1 - Mulliert,Guillermo

A1 - Coughtrie,Michael W. H.

A1 - Ouzzine,Mohamed

A1 - Fournel-Gigleux,Sylvie

AU - Bui,Catherine

AU - Talhaoui,Ibtissam

AU - Chabel,Matthieu

AU - Mulliert,Guillermo

AU - Coughtrie,Michael W. H.

AU - Ouzzine,Mohamed

AU - Fournel-Gigleux,Sylvie

PY - 2010/9/24

Y1 - 2010/9/24

N2 - <p>beta 1,4-Galactosyltransferase 7 (beta 4GalT7) is a key enzyme initiating glycosaminoglycan (GAG) synthesis. Based on in vitro and ex vivo kinetics studies and structure-based modelling, we molecularly characterized beta 4GalT7 mutants linked to the progeroid form of Ehlers-Danlos syndrome (EDS), a severe connective tissue disorder. Our results revealed that loss of activity upon L206P substitution due to altered protein folding is the primary cause for the GAG synthesis defect in patients carrying the compound A186D and L206P mutations. We showed that R270C substitution strongly reduced beta 4GalT7 affinity towards xyloside acceptor, thus affecting GAG chains formation. This study establishes the molecular basis for beta 4GalT7 defects associated with altered GAG synthesis in EDS. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</p>

AB - <p>beta 1,4-Galactosyltransferase 7 (beta 4GalT7) is a key enzyme initiating glycosaminoglycan (GAG) synthesis. Based on in vitro and ex vivo kinetics studies and structure-based modelling, we molecularly characterized beta 4GalT7 mutants linked to the progeroid form of Ehlers-Danlos syndrome (EDS), a severe connective tissue disorder. Our results revealed that loss of activity upon L206P substitution due to altered protein folding is the primary cause for the GAG synthesis defect in patients carrying the compound A186D and L206P mutations. We showed that R270C substitution strongly reduced beta 4GalT7 affinity towards xyloside acceptor, thus affecting GAG chains formation. This study establishes the molecular basis for beta 4GalT7 defects associated with altered GAG synthesis in EDS. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</p>

KW - Ehlers-Danlos syndrome

KW - Point mutation

KW - Galactosyltransferase defect

KW - Glycosaminoglycan synthesis

KW - Congenital glycosyltransferase disorder

KW - Galactosyltransferase-I beta4GalT-7

KW - Heparan sulfate

KW - Protein

KW - Biosynthesis

KW - Proteoglycan

KW - Fibroblasts

KW - Expression

KW - Patient

KW - Binding

KW - Identification

U2 - 10.1016/j.febslet.2010.08.001

DO - 10.1016/j.febslet.2010.08.001

M1 - Article

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 18

VL - 584

SP - 3962

EP - 3968

ER -

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