Christian-scott E. McCartney

Insertion sequence 1 from calpain-3 is functional in calpain-2 as an internal propeptide Christian-Scott E. McCartney, Qilu Ye, Robert L. Campbell and Peter L. Davies1 From the Department of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario K7L 3N6, Canada ↵1 Holder of the Canada Research Chair in Protein Engineering. To whom correspondence should be addressed: Dept. of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario K7L 3N6, Canada.

Calpains are intracellular, calcium-activated cysteine proteases. Calpain-3 is abundant in skeletal muscle, where its mutation-induced loss of function causes limb-girdle muscular dystrophy type 2A. Unlike the small subunit–containing calpains-1 and -2, the calpain-3 isoform homodimerizes through pairing of its C-terminal penta-EF-hand domain.

Insertion sequence 1 from calpain-3 is functional in calpain-2 as an internal propeptide Christian-Scott E. McCartney1, Qilu Ye2, Robert L. Campbell3 and Peter L.