3.4.22.54: calpain-3
This is an abbreviated version!
For detailed information about calpain-3, go to the full flat file.
Word Map on EC 3.4.22.54
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3.4.22.54
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calpains
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dystrophy
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muscular
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limb-girdle
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girdle
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lgmd2a
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limb
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calpainopathy
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titin
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calpastatin
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myopathy
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dysferlin
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tender
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autolytic
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sarcomere
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mu-calpains
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sarcoglycans
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myofibrillar
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telethonin
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scapular
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alpha-sarcoglycan
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merosin
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autolyzed
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caveolin-3
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nebulin
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lumborum
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m-lines
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dysferlinopathy
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sarcoglycanopathy
- 3.4.22.54
- calpains
- dystrophy
- muscular
-
limb-girdle
-
girdle
-
lgmd2a
- limb
-
calpainopathy
- titin
- calpastatin
- myopathy
-
dysferlin
-
tender
-
autolytic
- sarcomere
- mu-calpains
-
sarcoglycans
- myofibrillar
-
telethonin
-
scapular
-
alpha-sarcoglycan
-
merosin
-
autolyzed
-
caveolin-3
-
nebulin
- lumborum
-
m-lines
-
dysferlinopathy
- sarcoglycanopathy
Reaction
broad endopeptidase activity =
Synonyms
C3DIV, calcium-activated neutral proteinase 3, Calp3, calpain 3, calpain 3 (p94), calpain 3 domain IV, calpain 3/p94, calpain L3, calpain M, calpain p94, calpain-3, calpain3, CANP 3, CAPN3, Cn94, MP78, Mp84, muscle calpain, muscle-specific calcium-activated neutral protease 3, muscle-specific calpain, nCL-1, p94, p94-calpain, p94/calpain 3, skeletal muscle-specific calpain
ECTree
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General Information
General Information on EC 3.4.22.54 - calpain-3
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malfunction
metabolism
calpain 3 has a central role in the regulation of the important cell fate-governing nuclear factor-kappaB pathway. Calpain 3-mediated cardiac ankyrin repeat protein cleavage strengthens its interaction with titin N2A
physiological function
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deficiency in calpain 3 is associated with apoptosis as indicated by increases of caspase 3 activity, the absence of calpain 3 modifies the sarcoplasmic reticulum Ca2+ release, by a decrease of the sarcoplasmic reticulum content, an impairment of ryanodine receptor signalling, and an increase of L-type Ca2+ channel activity
malfunction
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inactivating mutations of the CAPN3 gene, encoding the muscle-specific calpain-3, result in the limb-girdle muscular dystrophy-2A
malfunction
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loss of CAPN3 is 100% specific for limb-girdle muscular dystrophy 2A
malfunction
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mitochondrial abnormalities, energy deficit and oxidative stress are features of calpain 3 deficiency in skeletal muscle
malfunction
mutations in calpain 3 underlie limb-girdle muscular dystrophy 2A
malfunction
mutations in calpain 3 underlie limb-girdle muscular dystrophy 2A
malfunction
gene mutations causing CAPN3 defects are responsible for limb-girdle muscular dystrophy type 2A (LGMD2A)
malfunction
limb-girdle muscular dystrophy type 2a arises from mutations in the Ca+-activated intracellular cysteine protease calpain-3
malfunction
loss of calpain-3 (CAPN3) activity leads to limb-girdle muscular dystrophy 2A. Calpain-3 mediates regulation of the Na+-Ca2+ exchanger isoform 3. The loss of regulation of Na+-Ca2+ exchanger isoform 3 (NCX3) by calpain-3 can be implicated in diverse muscular pathologies such as the limb-girdle muscular dystrophy 2A
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calcium-dependent plasma membrane repair does not require calpain-3
physiological function
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calpain 3 is involved in the myogenic differentiation process, calpain 3 participates in the establishment of the pool of reserve cells by decreasing the transcriptional activity of the key myogenic regulator MyoD via proteolysis independently of the ubiquitin-proteasome degradation pathway
physiological function
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calpain 3 variants can play a proapoptotic role in melanoma cells and its downregulation, as observed in highly aggressive lesions, can contribute to melanoma progression
physiological function
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calpain 3-dependent proteolysis plays a role in activating support proteins of intracellular Ca2+ signalling at a stage of cellular differentiation which is crucial for skeletal muscle regeneration
physiological function
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the enzyme plays a role in tenderizing connective tissue networks during growth and moulting
physiological function
aberrant calpain 3 splicing contributes to the muscle differentiation defects of facioscapulohumeral muscular dystrophy patients
physiological function
proteolytic processing of C-terminal titin by calpain 3 has an important role in normal muscle
physiological function
proteolytic processing of C-terminal titin by calpain 3 has an important role in normal muscle
physiological function
calpain-3 down-regulation can be regarded as a mechanism contributing to melanoma progression. Overexpression of the calpain-3 splicing variant hMp84 in A375 cells or HT-144 cells causes inhibition of cell proliferation, cell death, and increase of both ROS levels and F2-isoprostanes