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
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General Information
General Information on EC 3.4.22.52 - calpain-1
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malfunction
metabolism
physiological function
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calpain inhibition does not protect endothelial cells during cold storage
malfunction
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calpain inhibition prevents NMDA-induced AIF truncation and nuclear translocation in neurons
malfunction
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calpain-1 overactivation in mitochondrial-deficient cells promotes caspase-3 activation, calpain inhibition decreases alpha-synuclein oligomerization
malfunction
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immunodepletion or inhibition of calpain-1 in hypotonically lysed and resealed erythrocytes prevents the escape of Plasmodium falciparum parasites. Similarly, efficient egress of Tooplasma gondii from mammalian fibroblasts is blocked by either small interfering RNA-mediated suppression or genetic deletion of calpain activity
malfunction
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in utero knockdown of calpain by shRNA rescues defective cortical layering in heterozygous Lis1+/? mice
malfunction
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inhibition of micro-calpain not only significantly reduces caspase-9/-3 activities but also completely blocks apoptosis-inducing factor redistribution
malfunction
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knocking down mu-calpain by siRNA in FA-A cells restores levels of alphaII-spectrin to normal and reverses a number of the cellular deficiencies in these cells. siRNA knockdown of mu-Calpain in FA-A cells leads to increased cell viability and formation of nuclear foci after damage with a DNA interstrand cross-linking agent
malfunction
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engineered cleavage of Rad21 at the calpain-cleavable site without activation of calpain-1 can lead to a loss of sister chromatid cohesion
malfunction
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expression levels of galectin-3 are unchanged when calpain 1 is silenced
malfunction
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calpain inhibition favors differentiation of neuronal stem cells. Calpain 1 silencing results in increased levels of both neuronal and glial markers, beta-III tubulin and glial fibrillary acidic protein
malfunction
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suppression of calpain 1 significantly reduces cell viability in cell proliferation when compared with control cells. Suppression of calpain 1 results in an increase in the expressions of apoptotic caspases such as caspase-3, caspase-6, caspase-7, caspase-8, and caspase-9, as well as heat-shock protein systems and leads to the upregulation of other apoptosis and DNA damage-regulating genes whilst at the same time downregulating proliferation, migration, and differentiation-regulating genes
malfunction
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the knockdown of calpain 1 increases cell adhesion (by 36% after 30 min), enhances migration (by 46% after 12 h), and stabilizes late-stage cord formation on Matrigel by increasing cord length compared to the control human lymphatic microvascular dermal-derived endothelial cells
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calpain 1 is involved in the degradation of endothelial nitric oxide synthase and heat shock protein 90 and the phosphorylation of endothelial nitric oxide synthase
metabolism
calpain-1 regulates platelet function in a humanized mouse model of sickle cell disease
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activation of micro-calpain plays an essential role in regulating both caspase-dependent and apoptosis-inducing factor-mediated caspase-independent apoptotic pathways in cisplatin-induced apoptosis
physiological function
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calcium-dependent plasma membrane repair requires mu-calpain
physiological function
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calpain 1 activation contributes to HIF-2alpha degradation by IH
physiological function
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calpain activation is required for homocysteine-mediated hepatic degradation of inhibitor Ikappa B alpha
physiological function
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calpain activation precedes caspase-12 activation in the Ca2+-mediated apoptotic cascade and, thus, may be necessary for caspase-12 activation
physiological function
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calpain degrades myofibrillar protein under post-mortem condition and is the primary enzyme in the postmortem tenderization process
physiological function
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calpain I is not required for mitochondrial apoptosis-inducing factor release in poly(ADP-ribose) polymerase-1-dependent cell death
physiological function
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calpain regulates trastuzumab sensitivity and survival, and the deregulation of the activation of calpain promotes trastuzumab resistance, trastuzumab-resistant cells require calpain activity for survival and activation of AKT1
physiological function
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calpain-1 activation induces apoptosis through down-regulation of the Na+/K+ ATPase activity in high glucose-stimulated cardiomyocytes and in vivo hyperglycaemic hearts. High glucose-induced calpain-1 activation is mediated through the NADPH oxidase-dependent pathway and associated with activation of L-type calcium channels and ryanodine receptors
physiological function
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calpain-1 induces apoptosis in pulmonary microvascular endothelial cells under septic conditions
physiological function
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calpain-I activity colocalizes with apoptotic cell death
physiological function
dramatic muscle growth during the neonatal period may be partially controlled by down-regulated calpain-calpastatin system
physiological function
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gp91phox-NADPH oxidase-mediated calpain-1 activation induces caspase-3 activation and tumour necrosis factor-alpha expression in cardiomyocytes during lipopolysaccaride stimulation
physiological function
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micro-calpain is a key signal released from 1-methyl-4-phenylpyridinium-damaged neurons, causing selective dopaminergic neuron death through activation of microglial NADPH oxidase and superoxide production. Extracellular micro-calpain activates microglia
physiological function
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mitochondrial mu-calpain is an initiator of the apoptosis-inducing factor-induced cell death signaling pathway. Mitochondrial calpain plays important roles both in caspase-dependent and -independent pathways in cell death phenomena. Mu-calpain can act as a direct activator of apoptosis-inducing factor release in neuronal cultures challenged with oxygen-glucose deprivation
physiological function
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mu-calpain is responsible for Ca2+-induced disruption of excitation-contraction coupling
physiological function
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mu-calpain is specifically recruited into the NMDA receptor-neuronal nitric oxide synthase-heat shock protein 90 complex following calcium loading
physiological function
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mu-calpain plays a role in membrane repair and a protective role in skeletal muscle
physiological function
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mu-calpain plays a role in membrane repair and a protective role in skeletal muscle
physiological function
mu-calpain plays an important role in the postmortem tenderization process of meat
physiological function
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mu-calpain up-regulates alpha- and beta-actin in alveolar rhabdomyosarcoma cells
physiological function
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calpain-1 inhibits the acrosome reaction and alters the plasma membrane-associated cytoskeleton in spermatozoa
physiological function
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exogenous calcium treatment induces a calpain-dependent decrease of mitochondrial apoptosis inducing factor content in isolated mouse heart mitochondria
physiological function
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mu-calpain proteasome-dependent I-kappaBalpha polymer degradation may contribute to cancer progression through constitutive nulear factor-kappaB activation
physiological function
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Rad21 cleavage by calpain-1 promotes separation of sister chromatid arms
physiological function
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calpain 1 plays a role in repressing differentiation, thus maintaining a proliferative neuronal stem cell pool
physiological function
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calpain is involved in lysosomal membrane permeabilization
physiological function
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calpain is involved in lysosomal membrane permeabilization
physiological function
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calpain-1 induces endoplasmic reticulum stress and c-Jun N-terminal protein kinase1/2 activation, thereby mediating apoptosis in cardiomyocytes following hypoxia/reoxygenation. Up-regulation of calpain-1 induces increases in caspase-3 activation and DNA fragmentation, indicative of apoptosis
physiological function
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calpain-1 induces endoplasmic reticulum stress and c-Jun N-terminal protein kinase1/2 activation, thereby mediating apoptosis in cardiomyocytes following hypoxia/reoxygenation. Up-regulation of calpain-1 induces increases in caspase-3 activation and DNA fragmentation, indicative of apoptosis
physiological function
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mu-calpain is involved in the postmortem proteolysis of gizzard smooth muscle
physiological function
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mu-calpain is involved in the postmortem proteolysis of gizzard smooth muscle
physiological function
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neuronal death has a direct relationship with calpain I activity. Calpain I plays an important role in neuronal damage during status epilepticus
physiological function
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the enzyme plays a role in the early phase and during progression of amyotrophic lateral sclerosis
physiological function
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the enzyme plays key roles in regulation of cell proliferation and survival of of bovine skeletal satellite cells
physiological function
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
physiological function
calpain 1 activity within neutrophils is necessary for them to undergo efficient phagocytosis
physiological function
calpain-1 accumulation in mitochondria disrupts ATP synthase and induces ROS generation, which promotes diabetic cardiomyopathy
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
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
physiological function
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