Calpain 3 is activated through autolysis within the active site and lyses sarcomeric and sarcolemmal components
about
Calpain 3 is a rapid-action, unidirectional proteolytic switch central to muscle remodelingA new pathway encompassing calpain 3 and its newly identified substrate cardiac ankyrin repeat protein is involved in the regulation of the nuclear factor-κB pathway in skeletal muscleNovel variants of muscle calpain 3 identified in human melanoma cells: cisplatin-induced changes in vitro and differential expression in melanocytic lesionsMultiple molecular interactions implicate the connectin/titin N2A region as a modulating scaffold for p94/calpain 3 activity in skeletal muscleCalpain 3 is a modulator of the dysferlin protein complex in skeletal muscleNovel protein-protein interactions inferred from literature contextFilamin C interacts with the muscular dystrophy KY protein and is abnormally distributed in mouse KY deficient muscle fibresModified Ca(v)1.4 expression in the Cacna1f(nob2) mouse due to alternative splicing of an ETn inserted in exon 2Novel role of calpain-3 in the triad-associated protein complex regulating calcium release in skeletal muscleDown-regulation of MyoD by calpain 3 promotes generation of reserve cells in C2C12 myoblastsTaurine supplementation increases skeletal muscle force production and protects muscle function during and after high-frequency in vitro stimulationEndogenous calpain-3 activation is primarily governed by small increases in resting cytoplasmic [Ca2+] and is not dependent on stretchLoss of FilaminC (FLNc) results in severe defects in myogenesis and myotube structureExpression, crystallization and preliminary crystallographic data analysis of filamin A repeats 14-16.Myogenic stage, sarcomere length, and protease activity modulate localization of muscle-specific calpain.An extension to a statistical approach for family based association studies provides insights into genetic risk factors for multiple sclerosis in the HLA-DRB1 gene.Calcium-dependent plasma membrane repair requires m- or mu-calpain, but not calpain-3, the proteasome, or caspases.Comprehensive survey of p94/calpain 3 substrates by comparative proteomics--possible regulation of protein synthesis by p94.Suppressed disassembly of autolyzing p94/CAPN3 by N2A connectin/titin in a genetic reporter system.The N- and C-terminal autolytic fragments of CAPN3/p94/calpain-3 restore proteolytic activity by intermolecular complementation.Muscle giants: molecular scaffolds in sarcomerogenesis.Mutations in the N-terminal actin-binding domain of filamin C cause a distal myopathyRegulation of the M-cadherin-beta-catenin complex by calpain 3 during terminal stages of myogenic differentiationElectron microscopy and x-ray diffraction evidence for two Z-band structural statesPathogenity of some limb girdle muscular dystrophy mutations can result from reduced anchorage to myofibrils and altered stability of calpain 3.From proteins to genes: immunoanalysis in the diagnosis of muscular dystrophies.The genetic and molecular bases of monogenic disorders affecting proteolytic systems.Calpain-3 impairs cell proliferation and stimulates oxidative stress-mediated cell death in melanoma cells.Membrane Repair: Mechanisms and Pathophysiology.Impaired calcium calmodulin kinase signaling and muscle adaptation response in the absence of calpain 3The role of Ca2+ in muscle cell damage.Calpain involvement in the remodeling of cytoskeletal anchorage complexes.Calpain 3: a key regulator of the sarcomere?Processing and assembly of the dystrophin glycoprotein complex.Calpain 3 deficiency affects SERCA expression and function in the skeletal muscle.Calpain 3, the "gatekeeper" of proper sarcomere assembly, turnover and maintenance.Mitochondrial abnormalities, energy deficit and oxidative stress are features of calpain 3 deficiency in skeletal muscleFast-twitch sarcomeric and glycolytic enzyme protein loss in inclusion body myositis.Myofibrillar Z-discs Are a Protein Phosphorylation Hot Spot with Protein Kinase C (PKCα) Modulating Protein Dynamics.mu-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans.
P2860
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P2860
Calpain 3 is activated through autolysis within the active site and lyses sarcomeric and sarcolemmal components
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
Calpain 3 is activated through ...... ric and sarcolemmal components
@en
type
label
Calpain 3 is activated through ...... ric and sarcolemmal components
@en
prefLabel
Calpain 3 is activated through ...... ric and sarcolemmal components
@en
P2093
P2860
P1476
Calpain 3 is activated through ...... ric and sarcolemmal components
@en
P2093
Carinne Roudaut
Guillaume Sillon
Isabelle Richard
Marc Bartoli
Mathieu Taveau
Nathalie Bourg
P2860
P304
P356
10.1128/MCB.23.24.9127-9135.2003
P407
P577
2003-12-01T00:00:00Z