3.4.22.53: calpain-2
This is an abbreviated version!
For detailed information about calpain-2, go to the full flat file.
Word Map on EC 3.4.22.53
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3.4.22.53
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calpains
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calpastatin
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mu-calpain
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calcium-dependent
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ca2+-dependent
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proteinase
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myofibrillar
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cytoskeletal
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cataract
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zymography
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longissimus
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meat
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autolysis
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calpeptin
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tender
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casein
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cathepsins
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3.4.22.17
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postmortem
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calpain-mediated
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caspase-12
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lumborum
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autolyzed
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lens-specific
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talin
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alpha-spectrin
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canps
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cataractogenesis
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warner-bratzler
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spectrin
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slaughter
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semimembranosus
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calpain-specific
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desmin
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calpain-calpastatin
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lenses
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calpain-dependent
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atrogin-1
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medicine
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calpain-induced
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fodrin
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myofibril
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ca2+-activated
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calmodulin-like
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caseinolytic
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thoracis
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ca2+-requiring
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troponin-t
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micro-calpain
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calpain-like
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proteolyzed
- 3.4.22.53
- calpains
- calpastatin
- mu-calpain
-
calcium-dependent
-
ca2+-dependent
- proteinase
- myofibrillar
- cytoskeletal
- cataract
-
zymography
- longissimus
-
meat
-
autolysis
- calpeptin
-
tender
- casein
- cathepsins
-
3.4.22.17
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postmortem
-
calpain-mediated
- caspase-12
- lumborum
-
autolyzed
-
lens-specific
- talin
- alpha-spectrin
-
canps
-
cataractogenesis
-
warner-bratzler
- spectrin
-
slaughter
- semimembranosus
-
calpain-specific
- desmin
-
calpain-calpastatin
- lenses
-
calpain-dependent
-
atrogin-1
- medicine
-
calpain-induced
- fodrin
- myofibril
-
ca2+-activated
-
calmodulin-like
-
caseinolytic
- thoracis
-
ca2+-requiring
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troponin-t
- micro-calpain
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calpain-like
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proteolyzed
Reaction
broad endopeptidase specificity =
Synonyms
Cal II, calcium-activated neutral protease II, calpain 2, calpain II, calpain xCL-2 (Xenopus leavis), calpain-2, calpain-2-like, calpain2, CAPN II, CAPN2, CAPN2 g.p. (Homo sapiens), CPN2, cysteine protease, EC 3.4.22.17, EC 3.4.24.5, human calpain 2, m-calpain, milli-calpain, mitochondrial m-calpain, nCL-2, rat calpain 2
ECTree
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General Information
General Information on EC 3.4.22.53 - calpain-2
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malfunction
metabolism
physiological function
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calpain 2 depletion impairs mitosis and induces apoptosis, low Capn2 levels induce chromosome alignment defects, the loss of histone H3 threonine 3 phosphorylation at centromeres, and premature sister chromatid separation
malfunction
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calpain inhibition blocks the increased colonic epithelial cell invasion caused by NM IIA knockdown
malfunction
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in vivo knockdown of calpain2 disrupts metastasis among apoptosis-resistant tumors
malfunction
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inhibition of m-calpain induces expression of the adult alpha- and beta-globin genes
malfunction
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short interfering RNA-induced silencing of m-calpain results in increased RhoA activity and hyperpermeability in the aortic arch, which is accompanied by ROCK inhibitor-sensitive phosphorylation of downstream effecter LIM kinase 2, stress fibre accumulation in endothelium and enhanced interendothelial gaps
malfunction
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the blockage of calpain 2 suppresses p38 MAPK phosphorylation
malfunction
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inhibition of calpain activity limits cell migration and in vitro wound healing of IEC-6 cells
malfunction
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knockdown of calpain 2 expression or chemical inhibition of calpain activity reduces glioblastoma cell invasion by 90%. Decreased expression of calpain 2 does not influence morphology or migration
malfunction
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knockdown of calpain 2 inhibits T cell migration at both the level of single cell tracking and general cell speed
malfunction
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calpain 2 knockdown in breast cancer cells correlates with reduced in vitro proliferation, migration, and in vivo tumorigenicity as well as reduced Akt activation, increased nuclear FoxO localization, and increased p27Kip1 expression
malfunction
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calpain inhibition favors differentiation of neuronal stem cells. Calpain 2 silencing elicits decreased levels of glial fibrillary acidic protein
malfunction
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knockdown of calpain 2 results in a 2.9fold decrease in the invasion of human glioblastoma cells in zebrafish brain. Calpain 2 knockdown cells demonstrate a 2.3fold lower area of dispersal compared with control cells
malfunction
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the knockdown of calpain 2 significantly reduces cord formation, adhesion, and migration of human lymphatic microvascular dermal-derived endothelial cells on Matrigel compared to the control
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calpain 2 regulates endothelial nitric oxide synthase phosphorylation during cord formation by lymphatic endothelial cells on Matrigel
metabolism
isoform-specific hyperactivation of calpain-2, but not calpain-1 occurs at the synapse early in the pathogenesis of Alzheimer's disease potentially contributing to the deregulation of synaptic signaling in Alzheimer's disease
metabolism
MARCKS protein i.e. myristoylated alanine-rich C kinase substrate is a substrate of calpain-2 in the presence of Ca2+. Calpain-2 proteolysis of MARCKS promotes its interaction with lipids and ENaC at the plasma membrane to allow for the phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent regulation of epithelial sodium channel (ENaC) activity in the kidney
metabolism
nuclear translocation of calpain-2 mediates apoptosis of hypertrophied cardiomyocytes in transverse aortic constriction rat. Angiotensin II enhances the interaction between activated calpain-2 and Ca2+/calmodulin-dependent protein kinase II deltaB (CaMKIIdB), and promotes the degradation of CaMKIIdB by calpain-2 in the nuclei of hypertrophied cardiomyocytes. The depressed CaMKIIdeltaB downregulates the expression of antiapoptotic Bcl-2 leading to mitochondrial depolarization and release of cytochrome c which leads to apoptosis of hypertrophied cardiomyocytes
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an endoplasmic reticulum stress-related calpain-down-regulated PPAR-gamma/HO-1 pathway is involved in the interleukin-13-enhanced activated death of microglia
physiological function
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Ca2+ overload induces apoptosis, which was correlated with calpain-2 activation
physiological function
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calpain 2 activation is an early event in heat stress-induced male germ cell apoptosis
physiological function
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calpain 2 plays a role in the generation of the low molecular weight-androgen receptor in CWR22-R1 cells
physiological function
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calpain 2 proteolysis of mAbp1 negatively regulates dorsal ruffle formation
physiological function
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calpain 2-mediated proteolysis of focal adhesion kinase regulates adhesion dynamics in motile cells
physiological function
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calpain-2 is crucial for promotion of migration and metastasis by caspase-8
physiological function
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m-calpain antagonizes RhoA overactivation and endothelial barrier dysfunction under disturbed shear conditions
physiological function
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m-calpain translocates during ischemia and activates at reperfusion in isolated rat hearts
physiological function
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m-calpain up-regulates alpha- and beta-actin in alveolar rhabdomyosarcoma cells
physiological function
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mitochondrial m-calpain is associated with ERp75 and plays an important role in releasing of truncated apoptosis-inducing factor from mitochondria
physiological function
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mitochondrial m-calpain plays a role in the release of truncated apoptosis-inducing factor from the mitochondria by cleaving voltage-dependent anion channel
physiological function
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calpain 2 controls turnover of lymphocyte function-associated antigen-1 adhesions on migrating T lymphocytes
physiological function
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calpain 2 is required for matrix metalloproteinase-2 activity in glioblastoma cells. Calpain 2 is required for glioblastoma cell invasion, but not migration
physiological function
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calpain-2 is a mediator of beta cell dysfunction and apoptosis in type 2 diabetes
physiological function
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the Ca2+-dependent release of m-calpain from the mitochondrial outer membrane has important implications in facilitating apoptotic cell death
physiological function
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calpain 2 is required for the invasion of glioblastoma cells in the living zebrafish brain microenvironment
physiological function
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calpain 2 promotes proliferation of cancer cells through Akt-FoxO-p27Kip1 signaling
physiological function
calpain-1 and calpain-2 play opposite functions in both synaptic plasticity/learning and memory and neuroprotection/neurodegeneration. Calpain-1 activation is necessary for certain forms of synaptic plasticity and learning and memory, while calpain-2 activation during a brief consolidation period limits the extent of plasticity/learning. Calpain-1 is neuroprotective, while calpain-2 is neurodegenerative. Calpain-2 activation, through the selective degradation of phosphatase PTEN, is linked to the regulation of mTOR-mediated local protein synthesis
physiological function
calpain-1 and calpain-2 play opposite roles in retinal ganglion cell death induced by acute intraocular pressure elevation. Calpain-1 activity supports survival of retinal ganglion cell after intraocular pressure elevation. Calpain-2 activity promotes cell death of retinal ganglion cells after intraocular pressure elevation. Calpain-2 activation cleaves striatal-enriched protein tyrosine phosphatase and activates STEP-mediated pro-death pathway in retinal ganglion cells after intraocular pressure elevation