کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10833216 | 1065789 | 2013 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Congenital disorder of glycosylation due to DPM1 mutations presenting with dystroglycanopathy-type congenital muscular dystrophy
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کلمات کلیدی
CDGDol-PDol-P-ManDLODystroglycanopathyCGHdpmGPiGlcNAccongenital disorder of glycosylation - اختلال مادرزادی گلیسوزیله شدنElectroencephalogram - الکتروانسفالوگرافیMRI - امآرآی یا تصویرسازی تشدید مغناطیسیcomparative genomic hybridization - ترکیب هیبریداسیون ژنومی مقایسه شدهMagnetic resonance imaging - تصویربرداری رزونانس مغناطیسیGDP-mannose - تولید انبوه انارGDP-Man - تولید ناخالص داخلی مردCongenital muscular dystrophy - دیستروفی عضلانی مادرزادیendoplasmic reticulum - شبکه آندوپلاسمی EEG - نوار مغزیN-acetylglucosamine - نیتستیگلوکوزامینCreatine kinase - کراتین کیناز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Congenital disorder of glycosylation due to DPM1 mutations presenting with dystroglycanopathy-type congenital muscular dystrophy Congenital disorder of glycosylation due to DPM1 mutations presenting with dystroglycanopathy-type congenital muscular dystrophy](/preview/png/10833216.png)
چکیده انگلیسی
Congenital disorders of glycosylation (CDG) are rare genetic defects mainly in the post-translational modification of proteins via attachment of carbohydrate chains. We describe an infant with the phenotype of a congenital muscular dystrophy, with borderline microcephaly, hypotonia, camptodactyly, severe motor delay, and elevated creatine kinase. Muscle biopsy showed muscular dystrophy and reduced α-dystroglycan immunostaining with glycoepitope-specific antibodies in a pattern diagnostic of dystroglycanopathy. Carbohydrate deficient transferrin testing showed a pattern pointing to a CDG type I. Sanger sequencing of DPM1 (dolichol-P-mannose synthase subunit 1) revealed a novel Gly > Val change c.455G > T missense mutation resulting in p.Gly152Val) of unknown pathogenicity and deletion/duplication analysis revealed an intragenic deletion from exons 3 to 7 on the other allele. DPM1 activity in fibroblasts was reduced by 80%, while affinity for the substrate was not depressed, suggesting a decrease in the amount of active enzyme. Transfected cells expressing tagged versions of wild type and the p.Gly152Val mutant displayed reduced binding to DPM3, an essential, non-catalytic subunit of the DPM complex, suggesting a mechanism for pathogenicity. The present case is the first individual described with DPM1-CDG (CDG-Ie) to also have clinical and muscle biopsy findings consistent with dystroglycanopathy.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Molecular Genetics and Metabolism - Volume 110, Issue 3, November 2013, Pages 345-351
Journal: Molecular Genetics and Metabolism - Volume 110, Issue 3, November 2013, Pages 345-351
نویسندگان
Amy C. Yang, Bobby G. Ng, Steven A. Moore, Jeffrey Rush, Charles J. Waechter, Kimiyo M. Raymond, Tobias Willer, Kevin P. Campbell, Hudson H. Freeze, Lakshmi Mehta,