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Information on EC 3.4.22.52 - calpain-1 and Organism(s) Rattus norvegicus and UniProt Accession P97571

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.52 calpain-1
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Select one or more organisms in this record: ?
This record set is specific for:
Rattus norvegicus
UNIPROT: P97571 not found.
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
broad endopeptidase specificity
Synonyms
mu-calpain, calpain-1, calpain i, capn1, calpain 1, capn2, micro-calpain, capns1, calpain1, calpain-i, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
calcium-activated neutral protease I
-
-
-
-
calpain 1
calpain I
calpain-1
-
-
calpain-1 (micro-form)
-
-
CAPN1 g.p. (Homo sapiens)
-
-
-
-
cysteine protease
-
-
micro-calpain
mu-calpain
muCANP
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
689772-75-6
-
78990-62-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
AIF + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-actinin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-II-spectrin + H2O
?
show the reaction diagram
-
-
calpain-specific spectrin cleaved products
-
?
alpha-spectrin
?
show the reaction diagram
-
-
-
-
?
alpha-spectrin + H2O
?
show the reaction diagram
apoptosis-inducing factor + H2O
?
show the reaction diagram
-
calpain-mediated truncation of apoptosis-inducing factor is contingent upon poly(ADP-ribose) polymerase-1 activity
-
-
?
apoptosis-inducing factor + H2O
truncated apoptosis-inducing factor + ?
show the reaction diagram
casein + H2O
?
show the reaction diagram
-
-
-
-
?
collapsin response mediator protein 1 + H2O
?
show the reaction diagram
-
-
-
-
?
collapsin response mediator protein 2 + H2O
?
show the reaction diagram
-
-
-
-
?
collapsin response mediator protein 3 + H2O
?
show the reaction diagram
-
-
-
-
?
collapsin response mediator protein 4 + H2O
?
show the reaction diagram
-
-
-
-
?
cyclin dependent kinase-5 + H2O
p25-CDK5
show the reaction diagram
-
-
-
-
?
desmin + H2O
?
show the reaction diagram
-
-
-
-
?
E-(EDANS)-PLFAERK-(Dabcyl) + H2O
?
show the reaction diagram
-
-
-
-
?
fodrin + H2O
?
show the reaction diagram
-
-
-
-
?
lysosomal associated membrane protein 2 + H2O
?
show the reaction diagram
-
calpain 1 is responsible for lysosomal permeabilization by cleavage of the lysosomal associated membrane protein 2
-
-
?
MAP2 + H2O
?
show the reaction diagram
-
-
-
-
?
mature apoptosis-inducing factor (62 kDa) + H2O
cleaved apoptosis-inducing factor (57 kDa) + ?
show the reaction diagram
-
cleaved by the mitochondrial mu-calpain near its N-terminus
-
-
?
mitochondrial major Ca2+ extruding pathway Na+/Ca2+ exchanger + H2O
?
show the reaction diagram
-
cleaved by the mitochondrial mu-calpain
-
-
?
myelin-associated glycoprotein + H2O
?
show the reaction diagram
N-succinyl-L-leucyl-L-valyl-L-tyrosinyl-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Na+/Ca2+ exchanger isoform 3 + H2O
?
show the reaction diagram
-
-
-
-
?
RecTat101 + H2O
?
show the reaction diagram
-
-
-
-
?
spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
titin + H2O
?
show the reaction diagram
-
-
-
-
?
troponin complex + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-actinin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-spectrin + H2O
?
show the reaction diagram
apoptosis-inducing factor + H2O
truncated apoptosis-inducing factor + ?
show the reaction diagram
desmin + H2O
?
show the reaction diagram
-
-
-
-
?
fodrin + H2O
?
show the reaction diagram
-
-
-
-
?
lysosomal associated membrane protein 2 + H2O
?
show the reaction diagram
-
calpain 1 is responsible for lysosomal permeabilization by cleavage of the lysosomal associated membrane protein 2
-
-
?
MAP2 + H2O
?
show the reaction diagram
-
-
-
-
?
mature apoptosis-inducing factor (62 kDa) + H2O
cleaved apoptosis-inducing factor (57 kDa) + ?
show the reaction diagram
-
cleaved by the mitochondrial mu-calpain near its N-terminus
-
-
?
mitochondrial major Ca2+ extruding pathway Na+/Ca2+ exchanger + H2O
?
show the reaction diagram
-
cleaved by the mitochondrial mu-calpain
-
-
?
myelin-associated glycoprotein + H2O
?
show the reaction diagram
-
calpain overexpression due to *OH stress, IFN-gamma stimulation, or Ca2+ influx is involved in C6 cell death
-
-
?
Na+/Ca2+ exchanger isoform 3 + H2O
?
show the reaction diagram
-
-
-
-
?
spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
titin + H2O
?
show the reaction diagram
-
-
-
-
?
troponin complex + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
activates
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-bis(o-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid tetra(acetoxymethyl) ester
-
-
acetyl-calpastatin peptide
-
50 microM
-
acetyl-Leu-Leu-Met-CHO
-
-
acetyl-Leu-Leu-Nle-CHO
-
-
Al3+
-
inactivates enzyme from smooth muscle at millimolar concentrations of Ca2+, calpain 1 and 2
calpain inhibitor III
-
-
calpain inhibitor VI
-
-
calpain inhibitor-III
calpain VI inhibitor
-
78 nM used in assay conditions
-
calpastatin
-
calpastatin 1
-
calpain 1 is under constant inhibiting effect of active calpastatin 1
-
calpeptin
-
-
E-64
-
0.05 mg/ml, complete inhibition
inhibitor protein Ci1
-
non-specific inhibitor
-
lactacystin
-
1 microM
leupeptin
-
0.05 mg/ml, complete inhibition
MDL-28170
-
Cbz-Val-Phel-alanial
MG115
-
inhibitory effect in micromolar concentrations, 1 mircoM
MG132
-
inhibitory effect in micromolar concentrations, 1 microM
N-acetyl-Leu-Leu-norleucinal
-
2-fold increase in Tat levels after pre-treating with ALLN, 10 microM
ritonavir
-
also inhibits calcium-stimulated calpain activity in PC12 cells in situ. Ritonavir or analogues of the drug should by investigated as cytoprotective agents in conditions where cell death or injury is mediated via calpain activation
Z-Val-Phe-CHO
-
i.e. MDL-28710, 1.0 microM
additional information
-
specific capn1 shRNA reduces expression of the targeted isoform
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
angiotensin II
-
1.2-fold increased activity of calpain-1, influence in expression of calpain-1
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0059
ritonavir
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00019
acetyl-Leu-Leu-Nle-CHO
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000008
calpain inhibitor III
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0000075
calpain inhibitor VI
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000052
calpeptin
Rattus norvegicus
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
from Shumiya cataract animals
Manually annotated by BRENDA team
-
progenitor HCN-A94-2
Manually annotated by BRENDA team
-
originated from kidney
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
calpain inhibition prevents NMDA-induced AIF truncation and nuclear translocation in neurons
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CAN1_RAT
713
0
82119
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
-
gel filtration
25000
-
1 * 80000 + 1 * 25000, SDS-PAGE
28000
-
1 * 80000 + 1 * 28000
30000
-
1 * 80000 + 1 * 30000, SDS-PAGE
75000
-
x * 75000, active fragment, SDS-PAGE
76000
-
x * 76000, SDS-PAGE
80000
88000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
heterodimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
calpains are autolyzed in the early stage of skeletal muscle atrophy. This autolysis is specific to the particulate fraction for calpain 1 and to the soluble fraction for calpain 2, indicating specific microlocalization of calpain autolysis regulation. Calpain 1 autolysis occurs without any modification in the total amount. Calpain autolysis is only seen in the slow soleus muscle, while the fast plantaris muscle is not affected. Calpain autolysis and caspase 3 activation found in the soleus muscle could explain a more atrophied condition of this muscle compared with the plantaris muscle
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
30% inactivation by trypsin after 15 min at 30°C, pH 7.5
-
5% autolysis after 10 min, at 0°C, pH 7.5, 10 mM Ca2+
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
small subunit and large subunit
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
at 24 h after status epilepticus, activity of calpain I increases in the hippocampus
-
calpain 1 protein and mRNA levels are low at early developmental time points and increase dramatically by postnatal day 30. Immunoreactivity of the 80 kDa calpain 1 increases 75% from embryonic day 18 to postnatal day 90, with the increase being most rapid between postnatal day 10 and postnatal day 20 in rat brain
-
calpain activity increases in cells exposed to intermittent hypoxia 60 and 0.01 mM 1,2-bis(o-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid tetra(acetoxymethyl) ester prevents this effect
-
cell infection with Ad-capn1 and significantly elevates the protein level of calpain-1
-
delayed calcium deregulation is not sufficient to activate calpain 1
-
high glucose (33 mM) induces calpain-1 activation in cardiomyocytes. Gp91phox-NADPH oxidase contributes to calpain-1 activation in high glucose-induced cardiomyocytes
-
ionomycin and thapsigragin, which elevate [Ca2+], activate calpains in cells exposed to normoxia
-
MK801 added shortly after glutamate prevents calpain 1 activation
-
mu-calpain activity decreases by about 37% immediately and 2 h after acute-exhaustive exercise
-
mu-calpain is activated in neurons after ischemia
-
mu-calpain is not activated immediately following sprint, endurance or eccentric exercise. mu-Calpain is not activated 24 h after a single bout of eccentric exercise
-
there is no age-dependent change in calpain 1 protein expression in control or caloric-restricted rats. Liver samples taken from control rats at 4, 9, and 24 months and from caloric-restricted rats at 24 months do not exhibit any changes in calpain 1 protein expression
-
treatment with 50 mg/kg 7-nitroindozale shows significant suppression of the activity of mu-calpain in brain cortex (penumbra), however, it has no significant effect on the mu-calpain activity in core (striatum and overlying cortex)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dutt, P.; Springgs, C.N.; Davies, P.L.; Jia, Z.; Elce, J.S.
Origins of the difference in Ca2+ requirement for activation of mu- and m-calpain
Biochem. J.
367
263-269
2002
Rattus norvegicus
Manually annotated by BRENDA team
Sorimachi, H.; Amano, S.; Ishiura, S.; Suzuki, K.
Primary sequences of rat mu-calpain large and small subunits are, respectively, moderately and highly similar to those of human
Biochim. Biophys. Acta
1309
37-41
1996
Rattus norvegicus (P97571)
Manually annotated by BRENDA team
Murachi, T.; Tanaka, K.; Hatanaka, M.; Murakami, T.
Intracellular cellular Ca2+-dependent protease (calpain) and its high-molecular-weight endogenous inhibitor (calpastatin)
Adv. Enzyme Regul.
19
407-424
1981
Rattus norvegicus
Manually annotated by BRENDA team
Kishimoto, A.; Kajikawa, N.; Tabuchi, H.; Shiota, M.; Nishizuka, Y.
Calcium-dependent neutral proteases, widespread occurence of a species of protease active at lower concentrations of calcium
J. Biochem.
90
889-892
1981
Rattus norvegicus
Manually annotated by BRENDA team
Kitahara, A.; Sasaki, T.; Kikuchi, T.; Yumoto, N.; Yoshimura, N.; Hatanaka, M.; Murachi, T.
Large-scale purification of porcine calpain I and calpain II and comparison of proteolytic fragments of their subunits
J. Biochem.
95
1759-1766
1984
Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Murachi, T.
Intracellular regulatory system involving calpain and calpastatin
Biochem. Int.
18
263-294
1989
Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Yoshimura, N.; Kikuchi, T.; Sasaki, T.; Kithara, A.; Hatanaka, M.; Murachi, T.
Two distinct Ca2+ proteases (calpain I and calpain II) purified concurrently by the same method from rat kidney
J. Biol. Chem.
258
8883-8889
1983
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Wang, M.; Sakon, M.; Umeshita, K.; Okuyama, M.; Shiozaki, K.; Nagano, H.; Dohno, K.; Nakamori, S.; Monden, M.
Prednisolone suppresses ischemia-reperfusion injury of the rat liver by reducing cytokine production and calpain m activation
J. Hepatol.
34
278-283
2001
Rattus norvegicus
Manually annotated by BRENDA team
Zhang, J.; Miyamoto, K.I.; Hashioka, S.; Hao, H.P.; Murao, K.; Saido, T.C.; Nakanishi, H.
Activation of m-calpain in developing cortical neurons following methylmercury treatment
Brain Res. Dev. Brain Res.
142
105-110
2003
Rattus norvegicus
Manually annotated by BRENDA team
Zhang, H.; Yamamoto, Y.; Shumiya, S.; Kunimatsu, M.; Nishi, K.; Ohkubo, I.; Kani, K.
Peptidases play an important role in cataractogenesis: an immunohistochemical study on lenses derived from Shumiya cataract rats
Histochem. J.
33
511-521
2002
Rattus norvegicus
Manually annotated by BRENDA team
Ray, S.K.; Wilford, G.G.; Crosby, C.V.; Hogan, E.L.; Banik, N.L.
Diverse stimuli induce calpain overexpression and apoptosis in C6 glioma cells
Brain Res.
829
18-27
1999
Rattus norvegicus
Manually annotated by BRENDA team
Sazontova, T.G.; Matskevich, A.A.; Arkhipenko, Y.V.
Calpains: physiological and pathophysiological significance
Pathophysiology
6
91-102
1999
Rattus norvegicus
-
Manually annotated by BRENDA team
Wan, W.; DePetrillo, P.B.
Ritonavir inhibition of calcium-activated neutral proteases
Biochem. Pharmacol.
63
1481-1484
2002
Rattus norvegicus
Manually annotated by BRENDA team
Murphy, R.M.; Verburg, E.; Lamb, G.D.
Ca2+-activation of diffusible and bound pools of micro-calpain in rat skeletal muscle
J. Physiol.
576
595-612
2006
Rattus norvegicus
Manually annotated by BRENDA team
Vermaelen, M.; Sirvent, P.; Raynaud, F.; Astier, C.; Mercier, J.; Lacampagne, A.; Cazorla, O.
Differential localization of autolyzed calpains 1 and 2 in slow and fast skeletal muscles in the early phase of atrophy
Am. J. Physiol.
292
C1723-C1731
2007
Rattus norvegicus
Manually annotated by BRENDA team
Scalia, R.; Gong, Y.; Berzins, B.; Zhao, L.J.; Sharma, K.
Hyperglycemia is a major determinant of albumin permeability in diabetic microcirculation: the role of mu-calpain
Diabetes
56
1842-1849
2007
Rattus norvegicus
Manually annotated by BRENDA team
Badugu, R.; Garcia, M.; Bondada, V.; Joshi, A.; Geddes, J.W.
N terminus of calpain 1 is a mitochondrial targeting sequence
J. Biol. Chem.
283
3409-3417
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Covington, M.D.; Arrington, D.D.; Schnellmann, R.G.
Calpain 10 is required for cell viability and is decreased in the aging kidney
Am. J. Physiol. Renal Physiol.
296
F478-F486
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Passiatore, G.; Rom, S.; Eletto, D.; Peruzzi, F.
HIV-1 Tat C-terminus is cleaved by calpain 1: implication for Tat-mediated neurotoxicity
Biochim. Biophys. Acta
1793
378-387
2009
Rattus norvegicus
Manually annotated by BRENDA team
Bevers, M.B.; Lawrence, E.; Maronski, M.; Starr, N.; Amesquita, M.; Neumar, R.W.
Knockdown of m-calpain increases survival of primary hippocampal neurons following NMDA excitotoxicity
J. Neurochem.
108
1237-1250
2009
Rattus norvegicus
Manually annotated by BRENDA team
Sun, M.; Zhao, Y.; Gu, Y.; Xu, C.
Inhibition of nNOS reduces ischemic cell death through down-regulating calpain and caspase-3 after experimental stroke
Neurochem. Int.
54
339-346
2009
Rattus norvegicus
Manually annotated by BRENDA team
Jiang, L.; Wang, M.; Zhang, J.; Monticone, R.E.; Telljohann, R.; Spinetti, G.; Pintus, G.; Lakatta, E.G.
Increased aortic calpain-1 activity mediates age-associated angiotensin II signaling of vascular smooth muscle cells
PLoS ONE
3
e2231
2008
Rattus norvegicus
Manually annotated by BRENDA team
Kar, P.; Samanta, K.; Shaikh, S.; Chowdhury, A.; Chakraborti, T.; Chakraborti, S.
Mitochondrial calpain system: an overview
Arch. Biochem. Biophys.
495
1-7
2010
Rattus norvegicus
Manually annotated by BRENDA team
Ozaki, T.; Yamashita, T.; Ishiguro, S.
Mitochondrial m-calpain plays a role in the release of truncated apoptosis-inducing factor from the mitochondria
Biochim. Biophys. Acta
1793
1848-1859
2009
Rattus norvegicus
Manually annotated by BRENDA team
Levesque, S.; Wilson, B.; Gregoria, V.; Thorpe, L.B.; Dallas, S.; Polikov, V.S.; Hong, J.S.; Block, M.L.
Reactive microgliosis: extracellular micro-calpain and microglia-mediated dopaminergic neurotoxicity
Brain
133
808-821
2010
Rattus norvegicus
Manually annotated by BRENDA team
Li, X.; Li, Y.; Shan, L.; Shen, E.; Chen, R.; Peng, T.
Over-expression of calpastatin inhibits calpain activation and attenuates myocardial dysfunction during endotoxaemia
Cardiovasc. Res.
83
72-79
2009
Rattus norvegicus
Manually annotated by BRENDA team
Li, Y.; Li, Y.; Feng, Q.; Arnold, M.; Peng, T.
Calpain activation contributes to hyperglycaemia-induced apoptosis in cardiomyocytes
Cardiovasc. Res.
84
100-110
2009
Rattus norvegicus
Manually annotated by BRENDA team
Murphy, R.M.
Calpains, skeletal muscle function and exercise
Clin. Exp. Pharmacol. Physiol.
37
385-391
2010
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Vosler, P.S.; Sun, D.; Wang, S.; Gao, Y.; Kintner, D.B.; Signore, A.P.; Cao, G.; Chen, J.
Calcium dysregulation induces apoptosis-inducing factor release: cross-talk between PARP-1- and calpain-signaling pathways
Exp. Neurol.
218
213-220
2009
Rattus norvegicus
Manually annotated by BRENDA team
Joshi, A.; Bondada, V.; Geddes, J.W.
Mitochondrial micro-calpain is not involved in the processing of apoptosis-inducing factor
Exp. Neurol.
218
221-227
2009
Rattus norvegicus
Manually annotated by BRENDA team
Li, Y.; Bondada, V.; Joshi, A.; Geddes, J.W.
Calpain 1 and Calpastatin expression is developmentally regulated in rat brain
Exp. Neurol.
220
316-319
2009
Rattus norvegicus
Manually annotated by BRENDA team
Bevers, M.B.; Ingleton, L.P.; Che, D.; Cole, J.T.; Li, L.; Da, T.; Kopil, C.M.; Cohen, A.S.; Neumar, R.W.
RNAi targeting micro-calpain increases neuron survival and preserves hippocampal function after global brain ischemia
Exp. Neurol.
224
170-177
2010
Rattus norvegicus
Manually annotated by BRENDA team
Weber, H.; Huehns, S.; Luethen, F.; Jonas, L.
Calpain-mediated breakdown of cytoskeletal proteins contributes to cholecystokinin-induced damage of rat pancreatic acini
Int. J. Exp. Pathol.
90
387-399
2009
Rattus norvegicus
Manually annotated by BRENDA team
Brustovetsky, T.; Bolshakov, A.; Brustovetsky, N.
Calpain activation and Na+/Ca2+ exchanger degradation occur downstream of calcium deregulation in hippocampal neurons exposed to excitotoxic glutamate
J. Neurosci. Res.
88
1317-1328
2010
Rattus norvegicus
Manually annotated by BRENDA team
Wang, L.; Duan, L.; Li, X.; Li, G.
Acute-exercise-induced alterations in calpain and calpastatin expression in rat muscle
J. Sport Rehabil.
18
213-228
2009
Rattus norvegicus
Manually annotated by BRENDA team
Colak, A.; Kaya, M.; Karaoglan, A.; Sagmanligil, A.; Akdemir, O.; Sahan, E.; Celik, O.
Calpain inhibitor AK 295 inhibits calpain-induced apoptosis and improves neurologic function after traumatic spinal cord injury in rats
Neurocirugia (Astur)
20
245-254
2009
Rattus norvegicus
Manually annotated by BRENDA team
Nanduri, J.; Wang, N.; Yuan, G.; Khan, S.A.; Souvannakitti, D.; Peng, Y.J.; Kumar, G.K.; Garcia, J.A.; Prabhakar, N.R.
Intermittent hypoxia degrades HIF-2alpha via calpains resulting in oxidative stress: implications for recurrent apnea-induced morbidities
Proc. Natl. Acad. Sci. USA
106
1199-1204
2009
Rattus norvegicus
Manually annotated by BRENDA team
Villalpando Rodriguez, G.E.; Torriglia, A.
Calpain 1 induce lysosomal permeabilization by cleavage of lysosomal associated membrane protein 2
Biochim. Biophys. Acta
1833
2244-2253
2013
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Zheng, D.; Wang, G.; Li, S.; Fan, G.C.; Peng, T.
Calpain-1 induces endoplasmic reticulum stress in promoting cardiomyocyte apoptosis following hypoxia/reoxygenation
Biochim. Biophys. Acta
1852
882-892
2015
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Gao, H.; Geng, Z.
Calpain I activity and its relationship with hippocampal neuronal death in pilocarpine-induced status epilepticus rat model
Cell Biochem. Biophys.
66
371-377
2013
Rattus norvegicus
Manually annotated by BRENDA team