Skeletal muscle-specific calpain, p49: structure and physiological function.

K Kinbara; H Sorimachi; S Ishiura; K Suzuki

doi:10.1016/s0006-2952(98)00095-1

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Skeletal muscle-specific calpain, p49: structure and physiological function.

K Kinbara·H Sorimachi·S Ishiura·K Suzuki

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Abstract

Recent studies indicate that calpain, a cytosolic Ca2+-dependent protease, constitutes a large family comprising ubiquitous, tissue-specific, and atypical calpains. p94 is a homologue of the catalytic large subunit of calpain, expressed predominantly in skeletal muscle. Recently, p94 has been found to interact with connectin/titin, a muscle elastic protein, and its gene has been identified as being responsible for limb-girdle muscular dystrophy type 2A. The loss of function of a calpain species eventually leads to the activation of proteases including other calpain species responsible for muscle degradation. p94 does not form a complex with the small subunit of calpain (30K), but exists as a homodimer. This, together with other results, led us to consider a novel mechanism for the activation of calpain, a Ca2+-induced subunit rearrangement.

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Animals Calcium Calpain Connectin Humans Muscle Proteins Muscle, Skeletal Protein Kinases Journal Article Research Support, Non-U.S. Gov't Review

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K Kinbara, H Sorimachi, S Ishiura, K Suzuki. 1998-08-15. Skeletal muscle-specific calpain, p49: structure and physiological function.. https://doi.org/10.1016/s0006-2952(98)00095-1

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