Use of Endoglycosidase H as a diagnostic tool for MAN1B1-CDG patients

被引：8

作者：

Duvet, Sandrine ^{[1
,2
]}

Mouajjah, Dounia ^{[1
,2
]}

Peanne, Romain ^{[2
,3
]}

Matthijs, Gert ^{[2
,3
]}

Raymond, Kimiyo ^{[4
]}

Jaeken, Jaak ^{[5
]}

Morava, Eva ^{[6
]}

Foulquier, Francois ^{[1
,2
]}

机构：

[1] Univ Lille, CNRS, UMR 8576, UGSF,Unite Glycobiol Struct & Fonct, F-59000 Lille, France

[2] Lab Res Congenital Disorders Glycosylat Cellular, LIA GLYCOLAB4CDG France Belgium Int Assoc Lab, Lille, France

[3] Katholieke Univ Leuven, Ctr Human Genet, Leuven, Belgium

[4] Mayo Clin, Coll Med, Dept Lab Med & Pathol, Biochem Genet Lab, Rochester, MN USA

[5] Univ Hosp Leuven, Dept Pediat, Metab Ctr, Leuven, Belgium

[6] Tulane Univ, Sch Med, Hayward Genet Ctr, New Orleans, LA 70118 USA

来源：

ELECTROPHORESIS | 2018年 / 39卷 / 24期

基金：

欧盟地平线“2020”;

关键词：

CDG; Endo-beta-N-acetylglucosaminidase H; Glycomics; MAN1B1; N-Glycans; CONGENITAL DISORDERS; N-GLYCAN; GLYCOSYLATION; GLYCOPROTEINS; DEFECTS;

D O I：

10.1002/elps.201800020

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Congenital disorders of glycosylation (CDG) are heterogeneous group of genetic protein and lipid glycosylation abnormalities. With some 33 reported patients, MAN1B1-CDG belongs to the more frequent causes of CDG-II. MAN1B1 encodes an alpha 1,2-mannosidase that removes the terminal mannose residue from the middle branch. Several methods have been proposed to characterize the glycosylation changes. In MAN1B1-CDG, the abnormal accumulating N-glycan structures are mostly absent or found in trace amounts in total human serum. To overcome this issue, in this study, we present a straightforward procedure based on the use of Endo-beta-N-acetylglucosaminidase H to easily diagnose MAN1B1-CDG patients and mannosidase defects.

引用

页码：3133 / 3141

页数：9

共 20 条

[1] Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum
Clerc, Simone
Hirsch, Christian
Oggier, Daniela Maria
Deprez, Paola
Jakob, Claude
Sommer, Thomas
Aebi, Markus
[J]. JOURNAL OF CELL BIOLOGY, 2009, 184 (01) : 159 - 172
[2] A rapid mass spectrometric strategy for the characterization of N- and O-glycan chains in the diagnosis of defects in glycan biosynthesis
Faid, Valegh
Chirat, Frederic
Seta, Nathalie
Foulquier, Francois
Morelle, Willy
[J]. PROTEOMICS, 2007, 7 (11) : 1800 - 1813
[3] Understanding Human Glycosylation Disorders: Biochemistry Leads the Charge
Freeze, Hudson H.
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2013, 288 (10) : 6936 - 6945
[4] Stimulation of ERAD of misfolded null Hong Kong α1-antitrypsin by golgi α1,2-mannosidases
Hosokawa, Nobuko
You, Zhipeng
Tremblay, Linda O.
Nagata, Kazuhiro
Herscovics, Annette
[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2007, 362 (03) : 626 - 632
[5] A Golgi-localized Mannosidase ( MAN1B1) Plays a Nonenzymatic Gatekeeper Role in Protein Biosynthetic Quality Control
Iannotti, Michael J.
Figard, Lauren
Sokac, Anna M.
Sifers, Richard N.
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2014, 289 (17) : 11844 - 11858
[6] Molecular and enzymic properties of recombinant 1,2-α-mannosidase from Aspergillus saitoi overexpressed in Aspergillus oryzae cells
Ichishima, E
Taya, N
Ikeguchi, M
Chiba, Y
Nakamura, M
Kawabata, C
Inoue, T
Takahashi, K
Minetoki, T
Ozeki, K
Kumagai, C
Gomi, K
Yoshida, T
Nakajima, T
[J]. BIOCHEMICAL JOURNAL, 1999, 339 : 589 - 597
[7] Jaeken J, 2013, HAND CLINIC, V113, P1737, DOI 10.1016/B978-0-444-59565-2.00044-7
[8] Congenital disorders of glycosylation: A rapidly expanding disease family
Jaeken, Jaak
Matthijs, Gert
[J]. ANNUAL REVIEW OF GENOMICS AND HUMAN GENETICS, 2007, 8 : 261 - 278
[9] Jaeken J, 2017, J INHERIT METAB DIS, V40, P569, DOI 10.1007/s10545-017-0050-6
[10] Substrate specificities of recombinant murine Golgi α1,2-mannosidases IA and IB and comparison with endoplasmic reticulum and Golgi processing α1,2-mannosidases
Lal, A
Pang, P
Kalelkar, S
Romero, PA
Herscovics, A
Moremen, KW
[J]. GLYCOBIOLOGY, 1998, 8 (10) : 981 - 995

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