ArticleBiophysical journal2001
Mutations in calpain 3 associated with limb girdle muscular dystrophy: analysis by molecular modeling and by mutation in m-calpain.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 63 citations in OpenAlex.
- Repercussions of the Calpain Cleavage-Related Missense Mutations in the Cytosolic Domains of Human Integrin-β Subunits on the Calpain-Integrin Signaling Axis.International journal of molecular sciences · 2025Article
- Article
- Membrane-anchored calpains - hidden regulators of growth and development beyond plants?Frontiers in plant science · 2023Article
- CRISPR/Cas9 Genome Editing in LGMD2A/R1 Patient-Derived Induced Pluripotent Stem and Skeletal Muscle Progenitor Cells.Stem cells international · 2023Article
- Identification of Phosphorylated Calpain 3 in Rat Brain Mitochondria under mPTP Opening.International journal of molecular sciences · 2021Article
- CAPN5 genetic inactivation phenotype supports therapeutic inhibition trials.Human mutation · 2019Article
- Insertion sequence 1 from calpain-3 is functional in calpain-2 as an internal propeptide.The Journal of biological chemistry · 2018Article
- Autosomal dominant calpainopathy due to heterozygous CAPN3 C.643_663del21.Muscle & nerve · 2018Article
- Structures of human calpain-3 protease core with and without bound inhibitor reveal mechanisms of calpain activation.The Journal of biological chemistry · 2018Article
- Will you still need me (CaAging cell · 2017Article
- CAPN5 mutation in hereditary uveitis: the R243L mutation increases calpain catalytic activity and triggers intraocular inflammation in a mouse model.Human molecular genetics · 2015Article
- Autolytic activation of calpain 3 proteinase is facilitated by calmodulin protein.The Journal of biological chemistry · 2015Article
- Homology modeling study of bovine μ-calpain inhibitor-binding domains.International journal of molecular sciences · 2014Article
- Calpain 3 is important for muscle regeneration: evidence from patients with limb girdle muscular dystrophies.BMC musculoskeletal disorders · 2012Article
- Pathogenity of some limb girdle muscular dystrophy mutations can result from reduced anchorage to myofibrils and altered stability of calpain 3.Human molecular genetics · 2011Article
- Gene expression profiling of skeletal muscle of nursing piglets.International journal of biological sciences · 2010Article
- Calpain 3, the "gatekeeper" of proper sarcomere assembly, turnover and maintenance.Neuromuscular disorders : NMD · 2008Review
- Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains.Nature · 2008Article
- Novel role of calpain-3 in the triad-associated protein complex regulating calcium release in skeletal muscle.Human molecular genetics · 2008Article
- Screening of calpain-3 autolytic activity in LGMD muscle: a functional map of CAPN3 gene mutations.Journal of medical genetics · 2007Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Limb-girdle muscular dystrophy type 2A (LGMD2A) is an autosomal recessive disorder characterized by selective atrophy of the proximal limb muscles. Its occurrence is correlated, in a large number of patients, with defects in the human CAPN3 gene, a gene that encodes the skeletal muscle-specific member of the calpain family, calpain 3 (or p94). Because calpain 3 is difficult to study due to its rapid autolysis, we have developed a molecular model of calpain 3 based on the recently reported crystal structures of m-calpain and on the high-sequence homology between p94 and m-calpain (47% sequence identity). On the basis of this model, it was possible to explain many LGMD2A point mutations in terms of calpain 3 inactivation, supporting the idea that loss of calpain 3 activity is responsible for the disease. The majority of the LGMD2A mutations appear to affect domain/domain interaction, which may be critical in the assembly and the activation of the multi-domain calpain 3. In particular, we suggest that the flexibility of protease domain I in calpain 3 may play a critical role in the functionality of calpain 3. In support of the model, some clinically observed calpain 3 mutations were generated and analyzed in recombinant m-calpain. Mutations of residues forming intramolecular domain contacts caused the expected loss of activity, but mutations of some surface residues had no effect on activity, implying that these residues in calpain 3 may interact in vivo with other target molecules. These results contribute to an understanding of structure-function relationships and of pathogenesis in calpain 3.
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