Molecular and cellular basis of calpainopathy (limb girdle muscular dystrophy type 2A)

Biochim Biophys Acta. 2007 Feb;1772(2):128-44. doi: 10.1016/j.bbadis.2006.07.002. Epub 2006 Jul 15.

Abstract

Limb girdle muscular dystrophy type 2A results from mutations in the gene encoding the calpain 3 protease. Mutations in this disease are inherited in an autosomal recessive fashion and result in progressive proximal skeletal muscle wasting but no cardiac abnormalities. Calpain 3 has been shown to proteolytically cleave a wide variety of cytoskeletal and myofibrillar proteins and to act upstream of the ubiquitin-proteasome pathway. In this review, we summarize the known biochemical and physiological features of calpain 3 and hypothesize why mutations result in disease.

Publication types

  • Review

MeSH terms

  • Animals
  • Calpain / chemistry*
  • Calpain / genetics*
  • Calpain / physiology
  • Humans
  • Muscle Proteins / chemistry*
  • Muscle Proteins / genetics*
  • Muscle Proteins / physiology
  • Muscular Dystrophies, Limb-Girdle / classification
  • Muscular Dystrophies, Limb-Girdle / genetics*
  • Muscular Dystrophies, Limb-Girdle / metabolism
  • Muscular Dystrophies, Limb-Girdle / pathology*
  • Mutation, Missense

Substances

  • Muscle Proteins
  • CAPN3 protein, human
  • Calpain