کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
6041471 | 1189297 | 2015 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A new monoclonal antibody DAG-6F4 against human alpha-dystroglycan reveals reduced core protein in some, but not all, dystroglycanopathy patients
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کلمات کلیدی
LGMD2Ialpha dystroglycanDystroglycanopathyFKRPWGADGCPAGEADGHRPalpha-dystroglycan - آلفا دیستروگلیکانMonoclonal antibody - آنتی بادی مونوکلونالpolyacrylamide gel electrophoresis - الکتروفورز ژل پلی آکریل آمیدCongenital muscular dystrophy - دیستروفی عضلانی مادرزادیLimb-girdle muscular dystrophy - دیستروفی عضلانی کمربند کمربندDystrophin - دیستروفینDystroglycan - دیستروگلیکانDAG - روزDystrophin-glycoprotein complex - مجتمع دیستروفین گلیکوپروتئینEpitope mapping - نقشه برداری اپیتوپHorseradish peroxidase - پراکسیداز هوررادیشFukutin-related protein - پروتئین مرتبط با فوکوتینGlycosylation - گلیکوزیله شدنWheat germ agglutinin - گیاه گندم آگلوتیینین
موضوعات مرتبط
علوم زیستی و بیوفناوری
علم عصب شناسی
علوم اعصاب تکاملی
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چکیده انگلیسی
We generated a novel monoclonal antibody, DAG-6F4, against alpha-dystroglycan which immunolabels the sarcolemma in human muscle biopsies. Its seven amino-acid epitope, PNQRPEL, was identified using phage-displayed peptides and is located immediately after the highly-glycosylated mucin domain of alpha-dystroglycan. On Western blots of recombinant alpha-dystroglycan, epitope accessibility was reduced, but not entirely prevented, by glycosylation. DAG-6F4 immunolabelling was markedly reduced in muscle biopsies from Duchenne muscular dystrophy patients consistent with disruption of the dystroglycan complex. In a range of dystroglycanopathy patients with reduced/altered glycosylation, staining by DAG-6F4 was often less reduced than staining by IIH6 (antibody against the glycan epitope added by LARGE and commonly used to identify glycosylated alpha-dystroglycan). Whereas IIH6 was reduced in all patients, DAG-6F4 was hardly changed in a LARGE patient, less reduced than IIH6 in limb-girdle muscular dystrophy type 2I, but as reduced as IIH6 in some congenital muscular dystrophy patients. Although absence of the LARGE-dependent laminin-binding site appears not to affect alpha-dystroglycan stability at the sarcolemma, the results suggest that further reduction in aDG glycosylation may reduce its stability. These studies suggest that DAG-6F4 may be a useful addition to the antibody repertoire for evaluating the dystroglycan complex in neuromuscular disorders.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Neuromuscular Disorders - Volume 25, Issue 1, January 2015, Pages 32-42
Journal: Neuromuscular Disorders - Volume 25, Issue 1, January 2015, Pages 32-42
نویسندگان
Emma L. Humphrey, Erica Lacey, Lam T. Le, Lucy Feng, Francesca Sciandra, Charlotte R. Morris, Jane E. Hewitt, Ian Holt, Andrea Brancaccio, Rita Barresi, Caroline A. Sewry, Susan C. Brown, Glenn E. Morris,