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Lookup NU author(s): Faye Haldane, Dr Steven Laval, Dr Louise VB Anderson, Emerita Professor Katherine Bushby
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Mutations in dysferlin, a member of the fer1-like protein family that plays a role in membrane integrity and repair, can give rise to a spectrum of neuromuscular disorders with phenotypic variability including limbgirdle muscular dystrophy 2B, Myoshi myopathy and distal anterior compartment myopathy. To improve the tools available for understanding the pathogenesis of the dysferlinopathies, we have established a large source of highly specific antibody reagents against dysferlin by selection of heavy-chain antibody fragments originating from a nonimmune llama-derived phage-display library. By utilizing different truncated forms of recombinant dysferlin for selection and diverse selection methodologies, antibody fragments with specificity for two different dysferlin domains could be identified. The selected llama antibody fragments are functional in Western blotting, immunofluorescence microscopy and immunoprecipitation applications. Using these antibody fragments, we found that calpain 3, which shows a secondary reduction in the dysferlinopathies, interacts with dysferlin.
Author(s): Huang Y, Verheesen P, Roussis A, Frankhuizen W, Ginjaar I, Haldane F, Laval S, Anderson LVB, Verrips T, Frants RR, de Haard H, Bushby K, den Dunnen J, van der Maarel SM
Publication type: Article
Publication status: Published
Journal: European Journal of Human Genetics
Year: 2005
Volume: 13
Issue: 6
Pages: 721-730
ISSN (print): 1018-4813
ISSN (electronic): 1476-5438
Publisher: Nature Publishing Group
URL: http://dx.doi.org/10.1038/sj.ejhg.5201414
DOI: 10.1038/sj.ejhg.5201414
PubMed id: 15827562
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