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
-
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
- 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
results (
results (Substrates Products
Substrates Products on EC 3.4.22.52 - calpain-1
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SUBSTRATE 
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
(4-(4-dimethylaminophenylazo)benzoyl)-TPLKSPPPSPR-(5[(2-aminoethyl)amino]naphthalene-1-sulfonic acid) + H2O
(4-(4-dimethylaminophenylazo)benzoyl)-TPLK + SPPPSPR-(5[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)
-
-
-
-
?
(5(6)-carboxyfluorescin)-GGGQLYGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-RRK-(5- and 6-carboxytetramethylrhodamine)-OH + H2O
(5(6)-carboxyfluorescin)-GGGQLY + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-RRK-(5- and 6-carboxytetramethylrhodamine)-OH
-
-
-
-
?
(EDANS)-EALFAERK-(DABCYL) + H2O
(EDANS)-EA + LFAERK-(DABCYL)
-
about 30% cleavage preference
-
-
?
(EDANS)-EPLFAARK-(DABCYL) + H2O
(EDANS)-EPLFA + ARK-(DABCYL)
-
the sequence PLFAAR is an even better substrate for the calpain 1 protease core than PLFAER, 100% cleavage preference
-
-
?
(EDANS)-EPLFAERK-(DABCYL) + H2O
(EDANS)-EPLFA + ERK-(DABCYL)
-
about 40% cleavage preference
-
-
?
(EDANS)-EPLFGERK-(DABCYL) + H2O
(EDANS)-EPLF + GERK-(DABCYL)
-
less than 20% cleavage preference
-
-
?
(EDANS)-EPLFMERK-(DABCYL) + H2O
(EDANS)-EPLF + MERK-(DABCYL)
-
the peptide sequence PLFMER is rapidly cleaved by the calpain 1 core at the F-M bond with about 45% cleavage preference
-
-
?
2-aminobenzoyl-EVYGMMY(3-NO2)-OH + H2O
2-aminobenzoyl-EVY + GMMY(3-NO2)-OH
-
-
-
-
?
4,4-difluoro-5,7-dimethyl-4-bora-31,4a-diaza-s-indacene-3-propioyl-labeled casein + H2O
?
-
-
-
-
?
5-([4,6-dichlorotriazin-2-yl]amino)fluorescin-labeled microtubule-associated protein 2 + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGNIFGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGNIF + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGNIYGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGNIY + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGNLFGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGNLF + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGNLYGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGNLY + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGQIFGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGQIF + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGQLFGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGQLF + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGQLYGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGQLY + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
-
-
-
-
?
acetyl-LLY-7-amido-4-fluoromethylcoumarin + H2O
acetyl-LLY + 7-amino-4-fluoromethylcoumarin
-
-
-
-
?
alphaII-spectrin + H2O
?
-
Fanconi anemia proteins play an important role in maintaining the stability of alphaII-spectrin in the cell by regulating its cleavage by mu-calpain
-
-
?
apoptosis inducing factor + H2O
truncated apoptosis inducing factor + ?
-
-
-
-
?
Bfl-1 protein + H2O
?
-
mu-calpain cleaves Bfl-1 at two major sites in its N-terminus releasing three fragments of 28000 Da, 12000 Da and 17500 Da
-
-
?
BH3-only Bcl2 interacting domain + H2O
?
-
BH3-only Bcl2 interacting domain is a direct target of a soluble active calpain 1 present in cells expressing hepatitis C virus proteins
-
-
?
Boc-Leu-Met-7-amido-4-chloromethylcoumarin + H2O
Boc-Leu-Met + 7-amino-4-chloromethylcoumarin
-
10 microM, 20 min, 37 °C, with or without magnetic bead stimulation
-
-
?
caspase-7 + H2O
?
-
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
-
-
?
dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala + H2O
dye-Gln-Gln-Gln-Glu-Val-Tyr + Gly-Met-Met-Pro-Arg-Asp-pSer-Ala
-
-
-
-
?
full-length glutamic acid decraboxylase67 + H2O
truncated glutamic acid decarboxylase67 + ?
Hsp70.1 + H2O
?
-
Hsp70.1 in the CA-1 tissue is an in-vivo substrate of activated mu-calpain, carbonylated Hsp70.1 in the CA-1 tissue by artificial oxidative stressors such as hydroxynonenal or hydrogen peroxide is much more vulnerable to the calpain cleavage
-
-
?
human epithelial growth factor receptor 2 + H2O
75000 Da fragment + 42000 Da fragment
-
overexpression of calpain1 or activation of endogenous calpain during adhesion or trastuzumab treatment of trastuzumab-sensitive cells induces cleavage of cytoplasmic domains of human epithelial growth factor receptor 2/phospho-human epithelial growth factor receptor 2 protein
-
-
?
insulin-like growth factor binding protein-2 + H2O
?
-
the primary cleavage site in insulin-like growth factor binding protein-2 is localized to the non-conserved central linker regions
-
-
?
insulin-like growth factor binding protein-3 + H2O
?
-
the primary cleavage site in insulin-like growth factor binding protein-3 is localized to the non-conserved central linker regions. In vitro binding of mu-calpain to insulin-like growth factor binding protein-3 is a Ca2+-dependent reaction with a rapid on/off rate
-
-
?
K-(5(6)-carboxyfluorescein)-EVYGMMK(4-(4-dimethylaminophenylazo)benzoyl)-OH + H2O
K-(5(6)-carboxyfluorescein)-EVY + GMMK(4-(4-dimethylaminophenylazo)benzoyl)-OH
-
-
-
-
?
L-plastin + H2O
?
-
L-plastin interaction with integrin is regulated through cleavage of beta-integrin by micro-calpain
-
-
?
mature apoptosis-inducing factor (62 kDa) + H2O
cleaved apoptosis-inducing factor (57 kDa) + ?
-
cleaved by the mitochondrial mu-calpain near its N-terminus
-
-
?
microtubule-associated protein 2 + H2O
?
-
calpain translates high-frequency Ca2+ transients into decomposition of its sensitive substrate microtubule-associated protein 2
-
-
?
mitochondrial major Ca2+ extruding pathway Na+/Ca2+ exchanger + H2O
?
-
cleaved by the mitochondrial mu-calpain
-
-
?
N-acetyl-LLY-7-amido-4-fluoromethylcoumarin + H2O
N-acetyl-LLY + 7-amino-4-fluoromethylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg-4-methoxy-2-naphthylamide + H2O
N-benzyloxycarbonyl-L-Leu-L-Arg + 4-methoxy-2-naphthylamine
-
-
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-trifluoromethylcoumarin + H2O
N-benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
N-succinyl-L-leucyl-L-valyl-L-tyrosinyl-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
neuronal calcium sensor-1 + H2O
?
-
mu-calpain cleavage of neuronal calcium sensor-1 occurs within an N-terminal pseudoEF-hand domain (at Lys36), which is unable to bind Ca2+
-
-
?
NR2 subunit of NMDA subtype of glutamate receptor + H2O
?
-
all three subtypes of NR2 subunits can be proteolyzed, cleavage of NR2A, NR2B and NR2C subunits is limited to their C-terminal region. Two cleavage sites at amino acids 1279 and 1330. Cleavage of NR2A-containing receptors does not alter basic NMDA receptor properties including calcium uptake, MK801 binding or electrophysiological measurement
-
-
?
p12 subunit of human DNA polymerase delta + H2O
?
-
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
-
-
?
plasma membrane Ca2+-ATPase isoform 1 + H2O
?
-
readily and completely degraded by m-calpain
-
-
?
plasma membrane Ca2+-ATPase isoform 2 + H2O
?
-
slow hydrolysis only to large fragments
-
-
?
plasma membrane Ca2+-ATPase isoform 4 + H2O
?
-
slow hydrolysis only to large fragments
-
-
?
podoplanin + H2O
?
-
podoplanin stability is post-translationally regulated by calpain-1
-
-
?
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
-
-
?
striatal-enriched protein tyrosine phosphatase + H2O
?
-
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
-
-
?
succinyl-L-Leu-L-Leu-L-Val-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Leu-L-Val + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-L-Leu-L-Leu-L-Val-L-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Leu-L-Val-L-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-L-Leu-L-Met-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Met + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-L-Leu-L-Tyr-4-methoxy-2-naphthylamide + H2O
succinyl-L-Leu-L-Tyr + 4-methoxy-2-naphthylamine
-
-
-
-
?
succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Tyr + 7-amino-4-methylcoumarin
succinyl-LLVY-7-amido-4-methylcoumarin + H2O
succinyl-LLVY + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Leu-L-Met-7-amido-4-chloromethylcoumarin + H2O
tert-butyloxycarbonyl-L-Leu-L-Met + 7-amino-4-chloromethylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Leu-L-Met-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Leu-L-Met + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-leucyl-L-methionine-7-amido-4-chloromethylcoumarin + H2O
tert-butyloxycarbonyl-L-leucyl-L-methionine + 7-amino-4-chloromethylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-Leu-Met-7-amido-4-chloromethylcoumarin + H2O
tert-butyloxycarbonyl-Leu-Met + 7-amino-4-chloromethylcoumarin
-
-
-
-
?
[2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 + H2O
[2-Abz]-Ser-Thr-Phe + Ala-Gln-Pro-[3-nitrotyrosine]-NH2
-
-
-
-
?
[4-((4-(dimethylamino)phenyl)azo)benzoic acid, succinimidyl ester]-Thr-Pro-Leu-Lys-Ser-Pro-Pro-Pro-Ser-Pro-Arg-[5-((2-aminoethyl)amino)naphthalene-1-sulfonic acid] + H2O
?
-
-
-
-
?
alpha-II-spectrin + H2O
?
-
-
calpain-specific spectrin cleaved products
-
?
alpha-spectrin + H2O
?
-
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
-
-
?
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
-
-
?
apoptosis-inducing factor + H2O
?
-
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
-
-
?
apoptosis-inducing factor + H2O
?
-
micro-calpain mediates the truncation and release of apoptosis-inducing factor from mitochondria following cisplatin treatment
-
-
?
apoptosis-inducing factor + H2O
?
-
calpain-mediated truncation of apoptosis-inducing factor is contingent upon poly(ADP-ribose) polymerase-1 activity
-
-
?
apoptosis-inducing factor + H2O
truncated apoptosis-inducing factor + ?
-
-
-
-
?
apoptosis-inducing factor + H2O
truncated apoptosis-inducing factor + ?
-
mitochondrial micro-calpain is the protease responsible for processing apoptosis-inducing factor prior to its release
-
-
?
ATP synthase-alpha (ATP5A1) + H2O
?
calpain-1 accumulation in mitochondria disrupts ATP synthase and induces ROS generation, which promotes diabetic cardiomyopathy
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
Frizzled-7 + H2O
?
-
calpain-1 is a regulator of Frizzled-7 turnover at the plasma membrane
-
-
?
full-length glutamic acid decraboxylase67 + H2O
truncated glutamic acid decarboxylase67 + ?
-
-
-
-
?
full-length glutamic acid decraboxylase67 + H2O
truncated glutamic acid decarboxylase67 + ?
-
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
-
-
?
gamma-filamin + H2O
?
-
phosphorylation of the filamin C-terminus domain by PKCalpha protects gamma-filamin against proteolysis by calpain 1 in COS cells
-
-
?
lysosomal associated membrane protein 2 + H2O
?
-
calpain 1 is responsible for lysosomal permeabilization by cleavage of the lysosomal associated membrane protein 2
-
-
?
lysosomal associated membrane protein 2 + H2O
?
-
calpain 1 is responsible for lysosomal permeabilization by cleavage of the lysosomal associated membrane protein 2
-
-
?
myelin-associated glycoprotein + H2O
?
-
calpain overexpression due to *OH stress, IFN-gamma stimulation, or Ca2+ influx is involved in C6 cell death
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
-
-
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
-
-
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
-
-
-
-
?
neuronal nitric oxide synthase + H2O
?
-
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
-
-
?
recombinant procaspase-3 + H2O
?
-
calpain is a potential regulator of caspases and calpain promotes apoptosis-like events during platelet activation
-
-
?
recombinant procaspase-9 + H2O
?
-
calpain is a potential regulator of caspases and calpain promotes apoptosis-like events during platelet activation
-
-
?
RhoA + H2O
?
-
calpain cleaves RhoA and generates a form that inhibits integrin-induced stress fiber assembly and cell spreading
-
-
?
succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
additional information
?
-
-
primary role of calpain 1 and calpain 3 in meat tenderization
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
calpastatin could play an important role in preventing uncontrolled activity of l-calpain which otherwise may facilitate pulmonary hypertension, smooth muscle proliferation and apoptosis
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
calpain mediates calcium-induced activation of the Erk1,2 MAPK pathway and cytoskeletal phosphorylation in neurons
-
-
?
additional information
?
-
-
calpain-1 regulates Bax and subsequent Smac-dependent caspase-3 activation in neutrophil apoptosis
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
calpain 1 and 2 are required for RNA replication of echovirus 1
-
-
?
additional information
?
-
-
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
-
-
?
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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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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(EDANS)-EPAFAERK-(DABCYL), (EDANS)-EPLAAERK-(DABCYL), and (EDANS)-EPLFAEAK-(DABCYL) are very weak substrates for calpain 1 core
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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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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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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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the enzyme mediates tissue injury following post-ischemic and post-traumatic stress
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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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role for mu-calpain isoform in the hypermeability of the diabetic endothelium
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mitochondrial mu-calpain associates with ERp57, whereas, cytosolic mu-calpain does not associate with ERp57
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enzyme is involved in myofibrillar protein degradation
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enzyme is involved in myofibrillar protein degradation
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