3.4.22.52: calpain-1
This is an abbreviated version!
For detailed information about calpain-1, go to the full flat file.
Word Map on EC 3.4.22.52
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3.4.22.52
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calpains
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calpastatin
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ca2+-dependent
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tender
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calcium-dependent
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meat
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cytoskeletal
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beef
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ischemia
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myofibrillar
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hippocampal
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calpeptin
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autolysis
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caspase
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proteinase
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spectrin
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longissimus
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calpain-mediated
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postmortem
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cathepsins
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calpain-specific
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leupeptin
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lumborum
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medicine
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sarcomere
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non-lysosomal
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nebulin
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calpain-dependent
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slaughter
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calpain-like
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semimembranosus
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fodrin
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food industry
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carcass
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angus
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autoproteolysis
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warner-bratzler
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autolyzed
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ca2+-activated
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steak
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caspase-12
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myofibril
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talin
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troponin-t
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brahman
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calmodulin-like
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thoracis
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proteolyzed
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aif
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canps
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alpha-spectrin
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desmin
- 3.4.22.52
- calpains
- calpastatin
-
ca2+-dependent
-
tender
-
calcium-dependent
-
meat
- cytoskeletal
- beef
- ischemia
- myofibrillar
- hippocampal
- calpeptin
-
autolysis
-
caspase
- proteinase
- spectrin
- longissimus
-
calpain-mediated
-
postmortem
- cathepsins
-
calpain-specific
- leupeptin
- lumborum
- medicine
-
sarcomere
-
non-lysosomal
-
nebulin
-
calpain-dependent
-
slaughter
-
calpain-like
- semimembranosus
- fodrin
- food industry
-
carcass
-
angus
-
autoproteolysis
-
warner-bratzler
-
autolyzed
-
ca2+-activated
-
steak
- caspase-12
- myofibril
- talin
-
troponin-t
-
brahman
-
calmodulin-like
- thoracis
-
proteolyzed
- aif
-
canps
- alpha-spectrin
- desmin
Reaction
broad endopeptidase specificity =
Synonyms
Cal 1, calcium-activated neutral protease I, calpain 1, calpain 1-gamma, calpain 1A, calpain I, calpain small subunit, calpain-1, calpain-1 (micro-form), calpain-I, calpain1, CANP1, CAPN1, CAPN1 g.p. (Homo sapiens), CAPN2, CAPNS1, cysteine protease, EC 3.4.22.17, EC 3.4.24.5, m-CANP, micro-calpain, mit-CPN1, mito-mu-calpain, mu-calpain, muCANP, muI-II
ECTree
3.4.22.52 calpain-1Advanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.4.22.52 - calpain-1
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alphaII-spectrin + H2O
?
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Fanconi anemia proteins play an important role in maintaining the stability of alphaII-spectrin in the cell by regulating its cleavage by mu-calpain
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-
?
apoptosis inducing factor + H2O
?
activated mitochondrial calpain 1 within intermembrane space cleaves apoptosis inducing factor (AIF), whereas the activated mitochondrial calpain 1 within the matrix cleaves complex I subunits and metabolic enzymes
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-
?
apoptosis inducing factor + H2O
truncated apoptosis inducing factor + ?
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-
?
apoptosis-inducing factor + H2O
?
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although calpain I cleaves recombinant apoptosis-inducing factor in a cell free system, in intact cells under conditions where endogenous calpain is activated by either N-methyl-D-aspartate or N-methyl-N'-nitro-N-nitrosoguanidine administration, apoptosis-inducing factor is not cleaved
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-
?
ATP synthase-alpha (ATP5A1) + H2O
?
calpain-1 accumulation in mitochondria disrupts ATP synthase and induces ROS generation, which promotes diabetic cardiomyopathy
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-
?
caspase-7 + H2O
?
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recombinant caspase-7 is directly cleaved and activated by calpain-1 within the large subunit of caspase-7 to produce the large subunit p18 and p17
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-
?
complex I subunits + H2O
?
activated mitochondrial calpain 1 within intermembrane space cleaves apoptosis inducing factor (AIF), whereas the activated mitochondrial calpain 1 within the matrix cleaves complex I subunits and metabolic enzymes
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-
?
dynamin-like protein 1 + H2O
?
dynamin-like protein 1 (DLP1) is the key mitochondrial fission GTPase. It is a substrate of calpain which produced specific N-terminal DLP1 cleavage fragments. DLP1 is a physiological and Alzheimer's disease-relevant pathophysiological substrate of calpain in cells and in the brain. Calpain activation could contribute to reduced DLP1 levels and mitochondrial dynamics abnormalities and mitochondrial dysfunction in Alzheimer's disease
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-
?
Frizzled-7 + H2O
?
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calpain-1 is a regulator of Frizzled-7 turnover at the plasma membrane
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-
?
full-length glutamic acid decraboxylase67 + H2O
truncated glutamic acid decarboxylase67 + ?
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in mu-calpain knockout mice, the level of truncated glutamic acid decarboxylase67 in the brain is greatly reduced compared with the wild-type. mu-Calpain is activated by neuronal stimulation and Ca2+-influx
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-
?
mature apoptosis-inducing factor (62 kDa) + H2O
cleaved apoptosis-inducing factor (57 kDa) + ?
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cleaved by the mitochondrial mu-calpain near its N-terminus
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-
?
microtubule-associated protein 2 + H2O
?
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calpain translates high-frequency Ca2+ transients into decomposition of its sensitive substrate microtubule-associated protein 2
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-
?
mitochondrial major Ca2+ extruding pathway Na+/Ca2+ exchanger + H2O
?
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cleaved by the mitochondrial mu-calpain
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-
?
myelin-associated glycoprotein + H2O
?
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calpain overexpression due to *OH stress, IFN-gamma stimulation, or Ca2+ influx is involved in C6 cell death
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-
?
p12 subunit of human DNA polymerase delta + H2O
?
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the proteolysis of p12 by mu-calpain may be through a DNA polymerase delta4/PCNA complex. The p12/DNA polymerase delta is a target as a nuclear substrate of mu-calpain in calcium-triggered apoptosis
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?
prostacyclin synthase + H2O
?
calpain 1 cleaves and inactivates prostacyclin synthase in mesenteric arteries from diabetic mice. It cleaves the C-terminal domain of PGI2 synthase close to the catalytic site of the enzyme
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-
?
RhoA + H2O
?
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calpain cleaves RhoA and generates a form that inhibits integrin-induced stress fiber assembly and cell spreading
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-
?
striatal-enriched protein tyrosine phosphatase + H2O
?
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calpain-cleavage of striatal-enriched protein tyrosine phosphatase 61 is NMDAR-dependent, Cdk5 enhances calpain-mediated cleavage of striatal-enriched protein tyrosine phosphatase 61, calpain cleaves recombinant striatal-enriched protein tyrosine phosphatase 46 in a dose-dependent manner
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?
alpha-spectrin + H2O
?
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mu-calpain is neuroprotective in the early stage of excitotoxic injury. Activation and proteolysis of alpha-spectrin by mu-calpain preceds neuronal damage in the developing cerebral cortex induced by chronic treatament of methylmercury
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?
apoptosis-inducing factor + H2O
truncated apoptosis-inducing factor + ?
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-
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?
apoptosis-inducing factor + H2O
truncated apoptosis-inducing factor + ?
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mitochondrial micro-calpain is the protease responsible for processing apoptosis-inducing factor prior to its release
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?
lysosomal associated membrane protein 2 + H2O
?
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calpain 1 is responsible for lysosomal permeabilization by cleavage of the lysosomal associated membrane protein 2
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?
lysosomal associated membrane protein 2 + H2O
?
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calpain 1 is responsible for lysosomal permeabilization by cleavage of the lysosomal associated membrane protein 2
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?
neuronal nitric oxide synthase + H2O
?
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the mechanism of neuronal nitric oxide synthase activation is promoted by a calpain-mediated limited proteolysis through conversion of native 160 kDa nNOS into a fully active 130 kDa
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?
recombinant procaspase-3 + H2O
?
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calpain is a potential regulator of caspases and calpain promotes apoptosis-like events during platelet activation
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?
recombinant procaspase-9 + H2O
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calpain is a potential regulator of caspases and calpain promotes apoptosis-like events during platelet activation
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?
additional information
?
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primary role of calpain 1 and calpain 3 in meat tenderization
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?
additional information
?
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because the calcium concentration in postmortem muscle is high enough to activate mu-calpain, but not m-calpain, it seems reasonable to conclude that mu-calpain is responsible for postmortem degradation of calpastatin. Degradation of calpastatin by mu-calpain reduces calpain-inhibitory activity and is probably an important event in regulation of postmortem proteolysis, and, thus, meat tenderness
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?
additional information
?
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calpastatin could play an important role in preventing uncontrolled activity of l-calpain which otherwise may facilitate pulmonary hypertension, smooth muscle proliferation and apoptosis
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?
additional information
?
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translational expression of mu-calpain is up-regulated by 462.5% in MW white matter compared with controls. mu-Calpain activity and translational expression are not increased significantly in white matter from patients with Parkinsons or Alzheimer diseases compared with that of normal controls. Because calpain degrades all major myelin proteins, the increased activity and expression of this proteinase may play a critical role in myelinolysis in MS
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?
additional information
?
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calpain mediates calcium-induced activation of the Erk1,2 MAPK pathway and cytoskeletal phosphorylation in neurons
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?
additional information
?
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calpain-1 regulates Bax and subsequent Smac-dependent caspase-3 activation in neutrophil apoptosis
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?
additional information
?
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pathological conditions associated with the gene of calpain 1: muscular dystrophy, stroke, traumatic brain injury, spinal cord injury, Alzheimer's diseases, neurodegenerative disorders, cataracts, cancer
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?
additional information
?
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calpain 1 and 2 are required for RNA replication of echovirus 1
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?
additional information
?
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in the ischemic condition such as endometriosis, myoma of uterus and microscopic thrombosis, increasing of intracellular calcium ion concentration leads to the activation of l-calpain. Cleavage of integrin beta3 by over activated l-calpain may lead to an adverse effect on early pregnancy and to causing recurrent miscarriage
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?
additional information
?
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mu-calpain but not m-calpain can restore the cell migration rate. Knockdown of mu-calpain alters cell morphology with increased filopodial projections and a highly elongated tail that seems to prevent cell spreading and migration with reduced rear detachment ability. Knockdown of mu-calpain decreases the proteolytic products of filamin and talin, which are specifically rescued by overexpression of mucalpain but not m-calpain, suggesting that their proteolysis could be one of the key mechanisms by which mu-calpain regulates cell migration
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?
additional information
?
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mu-calpain prefers Leu, Val or Ile at the P2 position and Lys, Tyr, Arg, or Met at the P1 position
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?
additional information
?
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age-dependent myelin degeneration and proteolysis of oligodendrocyte proteins is associated with the activation of calpain-1
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?
additional information
?
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mu-Calpain regulates receptor activator of NF-kappaB ligand (RANKL)-supported osteoclastogenesis via NF-kappaB activation in RAW 264.7 cells
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?
additional information
?
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prednisolone suppresses ischemia-reperfusion injury of the rat liver. Its cytoprotective effect is partial, but is closely associated with inhibition of activation of mu-calpain and suppression of IL-beta and TNF-alpha transcription as well as with improved survival rate
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?
additional information
?
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the enzyme mediates tissue injury following post-ischemic and post-traumatic stress
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?
additional information
?
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mu-calpain, m-calpain, 20S proteasome, dipeptidyl peptidase II and III and soluble alanyl aminopeptidase are thought to induce lens opacification kinetically during cataract formation in Shumiya cataract rats through the intracellular turnover of lens proteins
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?
additional information
?
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role for mu-calpain isoform in the hypermeability of the diabetic endothelium
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?
additional information
?
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enzyme is involved in myofibrillar protein degradation
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?
additional information
?
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enzyme is involved in myofibrillar protein degradation
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?
