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Neuromuscul Disord. 2007 Feb;17(2):148-56. Epub 2007 Jan 22.

A third of LGMD2A biopsies have normal calpain 3 proteolytic activity as determined by an in vitro assay.

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1
Laboratory of Clinical Neurogenetics and Muscular Disorders, Zagreb University School of Medicine, Croatian Institute for Brain Research, Salata 12, 10000 Zagreb, Croatia.

Abstract

Limb-girdle muscular dystrophy type 2A (LGMD2A) is an autosomal recessive muscular disorder caused by mutations in the gene coding for calpain 3, a calcium-dependent protease. We developed an in vitro assay that can detect the proteolytic activity of calpain 3 in a muscle sample. This assay is based on the use of an inactive calpain 3 as a substrate for active calpain 3 molecules. A total of 79 human biopsies have been analysed using an unbiased single blind method. Results were confronted with the molecular diagnosis for confirmation. Proteolytic activity was either reduced or absent in 68% of LGMD2A biopsies. In the remaining 32%, normal proteolytic activity was found despite the presence of calpain 3 mutation(s), suggesting that other calpain 3 properties might be impaired to give rise to the LGMD2A phenotype. Our assay is easily adaptable to routine and appears to be more sensitive than common analysis by immunodetection.

PMID:
17236769
DOI:
10.1016/j.nmd.2006.11.001
[Indexed for MEDLINE]
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