gene mutations CAPN3 muscle: a functional map of Screening of calpain-3 autolytic activity in LGMD

See end of article forauthors’ affiliations Correspondence to:Dr M Fanin, VenetianInstitute of MolecularMedicine, via GiuseppeOrus 2, 35129 Padova,Italy; marina.fanin@unipd.itReceived 16 June 2006Revised 22 August 2006Accepted 24 August 2006 J Med Genet 2007;44:38–43. doi: 10.1136/jmg.2006.044859

[1]  T. Maeda,et al.  Suppressed Disassembly of Autolyzing p94/CAPN3 by N2A Connectin/Titin in a Genetic Reporter System* , 2006, Journal of Biological Chemistry.

[2]  L. Santoro,et al.  Early onset calpainopathy with normal non‐functional calpain 3 level , 2006, Developmental medicine and child neurology.

[3]  P. Davies,et al.  Ca2+ dependency of calpain 3 (p94) activation. , 2006, Biochemistry.

[4]  H. Sorimachi,et al.  Possible functions of p94 in connectin-mediated signaling pathways in skeletal muscle cells , 2006, Journal of Muscle Research & Cell Motility.

[5]  I. Richard,et al.  Calpain-3 mutations in Turkey , 2006, European Journal of Pediatrics.

[6]  C. Angelini,et al.  Extensive scanning of the calpain-3 gene broadens the spectrum of LGMD2A phenotypes , 2005, Journal of Medical Genetics.

[7]  J. Emparanza,et al.  LGMD2A: genotype-phenotype correlations based on a large mutational survey on the calpain 3 gene. , 2005, Brain : a journal of neurology.

[8]  C. Angelini,et al.  The frequency of limb girdle muscular dystrophy 2A in northeastern Italy , 2005, Neuromuscular Disorders.

[9]  C. Angelini,et al.  Molecular diagnosis in LGMD2A: Mutation analysis or protein testing? , 2004, Human mutation.

[10]  R. Campbell,et al.  Insertion Sequence 1 of Muscle-specific Calpain, p94, Acts as an Internal Propeptide* , 2004, Journal of Biological Chemistry.

[11]  C. Angelini,et al.  Loss of calpain-3 autocatalytic activity in LGMD2A patients with normal protein expression. , 2003, The American journal of pathology.

[12]  P. Davies,et al.  The protease core of the muscle‐specific calpain, p94, undergoes Ca2+‐dependent intramolecular autolysis , 2002, FEBS letters.

[13]  M. Passos-Bueno,et al.  Clinical variability in calpainopathy: What makes the difference? , 2002, European Journal of Human Genetics.

[14]  J. Beckmann,et al.  Mutations in calpain 3 associated with limb girdle muscular dystrophy: analysis by molecular modeling and by mutation in m-calpain. , 2001, Biophysical journal.

[15]  K. Bushby,et al.  The phenotype of calpainopathy: diagnosis based on a multidisciplinary approach , 2001, Neuromuscular Disorders.

[16]  I. Richard,et al.  Normal calpain expression in genetically confirmed limb–girdle muscular dystrophy type 2A , 2001, Neurology.

[17]  J. Beckmann,et al.  Calpainopathy-a survey of mutations and polymorphisms. , 1999, American journal of human genetics.

[18]  C. Angelini,et al.  Calpain III mutation analysis of a heterogeneous limb–girdle muscular dystrophy population , 1999, Neurology.

[19]  J. Beckmann,et al.  Characterization of monoclonal antibodies to calpain 3 and protein expression in muscle from patients with limb-girdle muscular dystrophy type 2A. , 1998, The American journal of pathology.

[20]  K Suzuki,et al.  Functional Defects of a Muscle-specific Calpain, p94, Caused by Mutations Associated with Limb-Girdle Muscular Dystrophy Type 2A* , 1998, The Journal of Biological Chemistry.

[21]  J. Beckmann,et al.  A biochemical, genetic, and clinical survey of autosomal recessive limb girdle muscular dystrophies in Turkey , 1997, Annals of neurology.

[22]  J. Beckmann,et al.  Multiple independent molecular etiology for limb-girdle muscular dystrophy type 2A patients from various geographical origins. , 1997, American journal of human genetics.

[23]  Isabelle Richard,et al.  Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A , 1995, Cell.

[24]  H. Kawasaki,et al.  Muscle-specific calpain, p94, is degraded by autolysis immediately after translation, resulting in disappearance from muscle. , 1993, The Journal of biological chemistry.