Key result
Mutations in fast skeletal muscle regulatory proteins significantly enhanced ATPase rates and increased Ca2+ sensitivity compared to wild-type proteins.
Population
Actomyosin ATPase assays and troponin-replaced rabbit psoas fibers
Comparison
Mutant proteins vs Wild-type (WT) proteins
Design
Preclinical
Authors
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May inform mechanisms of distal arthrogryposis contractures; leaves open human relevance and therapeutic translation.
Mutations in fast skeletal troponin and beta-tropomyosin associated with distal arthrogryposis increase contractile function, suggesting a mechanism for the development of muscle contractures and limb deformities.
Robinson et al. (2006) studied Distal arthrogryposis. Mutations in fast skeletal muscle regulatory proteins (Arg63His TnT, Arg91Gly beta-TM, Arg174Gln TnI, Arg156ter TnI) vs. Wild-type (WT) proteins was evaluated on Contractile function (actomyosin ATPase rates, Ca2+ sensitivity, maximum force). Mutations in fast skeletal muscle regulatory proteins significantly enhanced ATPase rates and increased Ca2+ sensitivity compared to wild-type proteins.
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