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our results suggest that calcium influx through mechanosensitive TRPC1 channels on filopodia activates calpain to control growth cone turning during development.
Destabilization of PGC1a (zeige PPARGC1A ELISA Kits) is attributable to decreased p38 MAPK (zeige MAPK14 ELISA Kits) activation via diminished CaMKII (zeige CAMK2G ELISA Kits) signaling. Thus, we elucidate a pathway downstream of Ca(2 (zeige CA2 ELISA Kits)+)-mediated CaMKII (zeige CAMK2G ELISA Kits) activation that is dysfunctional in C3KO(Capn3 knock-out mice ) mice, leading to reduced transcription of genes involved in muscle adaptation
CAPN3 deficiency leads to degradation of SERCA (zeige ATP2A3 ELISA Kits) proteins and Ca2 (zeige CA2 ELISA Kits)+ dysregulation in the skeletal muscle.
calpain 3 is necessary for ubiquitination and that it acts upstream of the ubiquitination machinery
Cleavage of C-terminal titin (zeige TTN ELISA Kits) by CAPN3 is associated with limb-girdle muscular dystrophy 2A and tibial muscular dystrophy.
these studies reveal a novel interaction between CAPN3 and CaM and identify CaM as the first positive regulator of CAPN3 activity.
data suggest that skNAC controls myoblast migration and sarcomere architecture in a calpain-dependent manner
our results suggest that a component of FSHD pathogenesis may arise by over-expression of FRG1 (zeige FRG1 ELISA Kits), reducing Rbfox1 (zeige A2BP1 ELISA Kits) levels and leading to aberrant expression of an altered Calpain 3 protein through dysregulated splicing
The Ky gene was downregulated in CAPN3 knockout muscles suggesting that Ky protease may play a complementary role in regulating muscle cytoskeleton homeostasis in response to changes in muscle activity
The decrease in CaMKII (zeige CAMK2G ELISA Kits) signaling in the absence of CAPN3 is associated with a reduction of muscle adaptation response.
stretch-induced dynamic redistribution of p94 is dependent on its protease activity and essential to protect muscle from degeneration
The higher CAPN3 gene expression in less tender muscles confirmed the lack of a direct involvement of calpain 3 in meat tenderization.
This study demonstrates that a cluster of patients with Limb-Girdle Muscular Dystrophy Type 2A in a small Mexican village arises from a novel CAPN3 founder mutation.
Heterozygosity for c.643_663del21 in CAPN3 results in a myopathy resembling the recessive form.
Here, for the first time, we report a new variant in the CAPN3 gene that can be considered as a robust genetics factor causing limb-girdle muscular dystrophy type 2A disease.
Genetic analysis of CAPN3 gene by whole exome sequencing revealed five causative variants which had not been reported in the Iranian population before including a novel 6 bp deletion (c.795_800delCATTGA) and four previously reported mutations (c.1939G > T, c.2243G > A, c.2257delGinsAA, and c.2380 + 2T > G)
The allele frequency of CAPN3 gene mutation in limb-girdle muscular dystrophy patients was different in patients from Latvia and Lithuania.
Studies indicate that gene mutations causing muscle-specific calcium-activated neutral protease 3 protein (CAPN3) defects are responsible for limb-girdle muscular dystrophy type 2A (LGMD2A).
We analyzed 76 families affected with LGMD and identified 62 probands with mutations in the CANP3 gene. C.550delA was the most common mutation identified, being found in 78% of the LGMD2A families
We identified four novel CAPN3 mutations and demonstrated clinical and pathological heterogeneity in Korean patients with calpainopathy.
2 CAPN3 transcripts in the skeletal muscle individuals of local black cattle from Jilin, China, were identified.
Calpain-system gene markers have beneficial effects on eating quality, consistent with previous findings for objective meat quality.
activated Capn3 may be involved in molecular pathways leading to the overexpression of E2F3, which in turn could be responsible for urothelial tumor cell proliferation
A QTL for meat tenderness is located in the Calpain 3 region of bovine chromosome 10.
Calpain, a heterodimer consisting of a large and a small subunit, is a major intracellular protease, although its function has not been well established. This gene encodes a muscle-specific member of the calpain large subunit family that specifically binds to titin. Mutations in this gene are associated with limb-girdle muscular dystrophies type 2A. Alternate promoters and alternative splicing result in multiple transcript variants encoding different isoforms and some variants are ubiquitously expressed.
, calpain 3, (p94)
, lens-specific calpain Lp82
, CANP 3
, calcium-activated neutral proteinase 3
, calpain L3
, calpain p94
, muscle-specific calcium-activated neutral protease 3
, skeletal muscle specific calpain p94
, new calpain 1
, skeletal muscle specific calpain
, calpain p94, large [catalytic] subunit
, calpain, large polypeptide L3
, muscle-specific calcium-activated neutral protease 3 large subunit
, skeletal muscle-specific calpain