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Information on EC 3.4.22.53 - calpain-2 and Organism(s) Rattus norvegicus and UniProt Accession Q07009
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3.4.22.53 calpain-2Specify your search results
Word Map
- 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
-
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
-
troponin-t
- micro-calpain
-
calpain-like
-
proteolyzed
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
m-calpain, calpain ii, calpain-2, calpain 2, calpain2, ncl-2, milli-calpain, mitochondrial m-calpain, rat calpain 2, calcium-activated neutral protease ii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
calcium-activated neutral protease II
-
-
-
-
calpain 2
calpain II
calpain xCL-2 (Xenopus leavis)
-
-
-
-
CAPN2 g.p. (Homo sapiens)
-
-
-
-
m-calpain
milli-calpain
-
-
-
-
calpain 2
-
-
-
-
calpain 2
-
-
calpain II
-
-
-
-
m-calpain
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
702693-80-9
-
78990-62-2
-
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
FRET-based substrate PLFAER + H2O
?
10 microM, pH 7.4, 1 mM of CaCl2 added to initiate the reaction
-
-
?
collapsin response mediator protein-1 + H2O
?
-
collapsin response mediator protein-1 is cleaved by calpain-2 at the C-terminus
-
-
?
collapsin response mediator protein-2 + H2O
?
-
collapsin response mediator protein-2 is cleaved by calpain-2 at the C-terminus
-
-
?
collapsin response mediator protein-4 + H2O
?
-
collapsin response mediator protein-4 is cleaved by calpain-2 at the C-terminus
-
-
?
focal adhesion kinase + H2O
?
-
the preferred calpain cleavage site is between the two C-terminal proline-rich regions after Ser-745
-
-
?
mammalian actin-binding protein-1 + H2O
?
-
the preferred cleavage site occurs between the actin-binding domain and the proline-rich region, generating a C-terminal mAbp1 fragment
-
-
?
N-acetyl-LLY-7-amido-4-trifluoromethylcoumarin + H2O
N-acetyl-LLY + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
proteolysis-resistant fragment 130 + H2O
proteolysis-resistant fragment 45 + ?
-
-
-
-
?
proteolysis-resistant fragment 72 + H2O
proteolysis-resistant fragment 45 + ?
-
-
-
-
?
voltage-dependent anion channel + H2O
?
-
mitochondrial m-calpain truncates voltage-dependent anion channel in Ca2+-dependent manner
-
-
?
calmodulin-dependent protein kinase II deltaB + H2O
?
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
-
-
?
GAP-43 + H2O
GAP-43-3 + ?
-
GAP-43 cleavage at Ser41 residue in synaptosomes is mediated by m-calpain
-
-
?
GAP-43 + H2O
GAP-43-3 + ?
-
a GAP-43 fragment, lacking about 40 N-terminal residues (named GAP-43-3), is produced by m-calpain. The fragment prevents complete cleavage of intact GAP-43 by m-calpain as a negative feedback
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
calpain-mediated impairment of Na+/K+-ATPase activity during early reperfusion contributes to cell death after myocardial ischemia
-
-
?
additional information
?
-
-
ERp75 plays important role in the refolding of mitochondrial m-calpain large subunit, cytosolic m-calpain does not associate with ERp57
-
-
?
additional information
?
-
-
representatives of the protein phosphatase 2A subunit classes C, PR65/A, PR55/B and PR61/B' are resistant to m-calpain-mediated degradation
-
-
?
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
calmodulin-dependent protein kinase II deltaB + H2O
?
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
-
-
?
collapsin response mediator protein-1 + H2O
?
-
collapsin response mediator protein-1 is cleaved by calpain-2 at the C-terminus
-
-
?
collapsin response mediator protein-2 + H2O
?
-
collapsin response mediator protein-2 is cleaved by calpain-2 at the C-terminus
-
-
?
collapsin response mediator protein-4 + H2O
?
-
collapsin response mediator protein-4 is cleaved by calpain-2 at the C-terminus
-
-
?
GAP-43 + H2O
GAP-43-3 + ?
-
GAP-43 cleavage at Ser41 residue in synaptosomes is mediated by m-calpain
-
-
?
mammalian actin-binding protein-1 + H2O
?
-
the preferred cleavage site occurs between the actin-binding domain and the proline-rich region, generating a C-terminal mAbp1 fragment
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
calpain-mediated impairment of Na+/K+-ATPase activity during early reperfusion contributes to cell death after myocardial ischemia
-
-
?
additional information
?
-
-
ERp75 plays important role in the refolding of mitochondrial m-calpain large subunit, cytosolic m-calpain does not associate with ERp57
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Al3+
-
millimolar concentrations of Al3+ activate at at submillimolar concentrations of Ca2+
Ca2+
Ca2+
Ca2+-binding must induce conformational changes that reorient the protease domains to form a functional active site
Ca2+
activates. The results support the hypothesis that Ca2+ induces movement of domains I and II closer together to form the functional active site of calpain
Ca2+
half-maximal activity is 0.242 mM for wilde-type enzyme, 0.129 mM for the E504S mutant, 0.226 mM for the K226S mutant, 0.261 mM for the K230S mutant, 0.183 mM for the K234 mutant, 0.256 mM for the K230E mutant and 0.159 mM for the K234E mutant
Ca2+
-
Kd-value: 0.325 mM. 25% of the difference in Kd values between mu-calpain and m-calpain can be ascribed to the N-terminal peptide of the large subunit, whereas the C-terminal EF-hand-containing domain IV accounts for 65% of the difference
Ca2+
-
Ca2+-induced calpain translocation to the membrane during ischemia is independent of its activation
Ca2+
-
the Ca2+ dependency of mitochondrial m-calpain is similar to that of cytosolic m-calpain, 1 mM Ca2+ activates.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S)-3-phenyl-2-([[(2S)-1-(phenylsulfonyl)pyrrolidin-2-yl]carbonyl]amino)propanoic acid
-
-
GAP-43-3
-
a GAP-43 fragment, lacking about 40 N-terminal residues (named GAP-43-3), is produced by m-calpain-mediated cleavage of GAP-43. The fragment prevents complete cleavage of intact GAP-43 by m-calpain as a negative feedback. GAP-43-3 also blocks m-calpain activity against casein
-
additional information
-
specific capn2 shRNA reduces expression of the targeted isoform
-
additional information
-
not inhibited by benzyloxycarbonyl-VAD-fluoromethylketone
-
additional information
-
not inhibited by Ac-Thr-Pro-Leu-alpha-azaglycine-Ser-Pro-NH2, Ac-Pro-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2, Ac-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2, Ac-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2, Ac-Thr-Pro-Thr-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2, Ac-Thr-Pro-Leu-alpha-azaglycine-Ser-Ser-Pro-Pro-Ser-NH2, Ac-Thr-Pro-Leu-alpha-azaglycine-Ser-Gln-Pro-Pro-Ser-NH2, Ac-Thr-Pro-Val-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2, Ac-Thr-Pro-Leu-alpha-azaglycine-Thr-Pro-Pro-Pro-Ser-NH2, and Ac-Thr-Pro-Leu-alpha-azaglycine-Arg-Pro-Pro-Pro-Ser-NH2
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0898
Ac-Thr-Pro-Leu-alpha-azaglycine-Ser-Pro-Pro-NH2
-
in 10 mM HEPES, 150 mM NaCl, 1 mM EDTA, pH 7.5, at 22°C
0.0087
Ac-Thr-Pro-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2
-
in 10 mM HEPES, 150 mM NaCl, 1 mM EDTA, pH 7.5, at 22°C
0.0072
Ac-Thr-Pro-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-Pro-Arg-NH2
-
in 10 mM HEPES, 150 mM NaCl, 1 mM EDTA, pH 7.5, at 22°C
0.0035
Ac-Thr-Ser-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2
-
in 10 mM HEPES, 150 mM NaCl, 1 mM EDTA, pH 7.5, at 22°C
0.0058
Ac-Thr-Trp-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2
-
in 10 mM HEPES, 150 mM NaCl, 1 mM EDTA, pH 7.5, at 22°C
0.0203
Thr-Pro-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-Pro-Arg-NH2
-
in 10 mM HEPES, 150 mM NaCl, 1 mM EDTA, pH 7.5, at 22°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00014
(2S)-3-phenyl-2-([[(2S)-1-(phenylsulfonyl)pyrrolidin-2-yl]carbonyl]amino)propanoic acid
Rattus norvegicus
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.00041
(2S)-4-methyl-2-[(phenylsulfonyl)amino]pentanoic acid
Rattus norvegicus
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.00024
ethyl N-(phenylsulfonyl)-L-leucyl-L-phenylalaninate
Rattus norvegicus
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.00015
MDL28170
Rattus norvegicus
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
initial activity as relative fluorescence units per s: 1.3 for wild type calpain 2, 0.84 for mutant G423R, 0.19 for mutant R628Q, 0.36 for mutant T344M, 0.7 for mutant D346E, 1.0 for mutant D362K
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
calpains 2 is involved in atrophy development in slow type muscle. Calpains 2 is autolyzed in the early stage of skeletal muscle atrophy. This autolysis is specific to the soluble fraction for calpain 2. Calpain 2 autolysis is associated with an increased amount of calpain 2 content. Calpain autolysis is only seen in the slow soleus muscle, while the fast plantaris muscle is not affected
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
angiotensin II increases nuclear translocation of intracellular Ca2þ activated calpain-2 in hypertrophied cardiomyocytes
-
in isolated rat hearts, ischemia induces a time-dependent translocation of m-calpain to the membrane that is not associated with calpain activation
-
m-calpain is present in the intermembrane space of the mitochondria
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
malfunction
-
the blockage of calpain 2 suppresses p38 MAPK phosphorylation
physiological function
physiological function
-
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
-
calpain 2 activation is an early event in heat stress-induced male germ cell apoptosis
physiological function
-
calpain 2 proteolysis of mAbp1 negatively regulates dorsal ruffle formation
physiological function
-
calpain 2-mediated proteolysis of focal adhesion kinase regulates adhesion dynamics in motile cells
physiological function
-
m-calpain translocates during ischemia and activates at reperfusion in isolated rat hearts
physiological function
-
mitochondrial m-calpain is associated with ERp75 and plays an important role in releasing of truncated apoptosis-inducing factor from mitochondria
physiological function
-
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
-
calpain-2 is a mediator of beta cell dysfunction and apoptosis in type 2 diabetes
physiological function
-
the Ca2+-dependent release of m-calpain from the mitochondrial outer membrane has important implications in facilitating apoptotic cell death
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CAN2_RAT
700
0
79919
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2.6 A crystal structure of m-calpain that has a C-terminal histidine-tag and a mutation of the active site C105S in the large subunit in the Ca2+-free form
the refined crystal structure of the mutant enzymes K226S, K230E, K234S and E504S in absence of Ca2+ are indistinguishable from wilde-type calpain
calpastatin inhibitory domain 1 crystallized with calpain 2, calpastatin inhibitory domain 4 crystallized with calpain 2
-
crystallization of recombinant C105S mutant enzyme by hanging drop method
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D346E
mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation
D362K
mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation
E504S
Ca2+ concentration required for half-maximal activity is 0.129 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme
G423R
mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation
K226S
Ca2+ concentration required for half-maximal activity is 0.226 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme
K230E
Ca2+ concentration required for half-maximal activity is 0.256 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme
K230S
Ca2+ concentration required for half-maximal activity is 0.261 mM compared to 0.242 mM for the wild-type enzyme
K234S
Ca2+ concentration required for half-maximal activity is 0.183 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme
K234W
Ca2+ concentration required for half-maximal activity is 0.159 mM compared to 0.242 mM for the wild-type enzyme
R417W
mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation
T344M
mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation
C105S
-
inactive mutant enzyme. The mutant enzyme provides a purified calpain, that is stable to autolysis and oxidation, which is likely to facilitate crystallization in both the presence and absence of calcium
E504S
mutation decreases specific activity to 90% compared to wild-type enzyme
K225S
mutation decreases specific activity to 88% compared to wild-type enzyme
K230E
mutation decreases the specific activity of the enzyme to 16% compared with the wild-type enzyme
K234E
mutation decreases the specific activity of the enzyme to 16% compared with the wild-type enzyme
K234S
mutation decreases specific activity to 81% compared to wild-type enzyme
S50D
-
mutant enzyme has the same specific activity and Ca2+ requirement as the wild-type enzyme
S50E
-
mutant enzyme has the same specific activity and Ca2+ requirement as the wild-type enzyme
S67E
-
mutant enzyme has the same specific activity and Ca2+ requirement as the wild-type enzyme
T70E
-
mutant enzyme has the same specific activity and Ca2+ requirement as the wild-type enzyme
additional information
additional information
used as a model for calpain 3 in combination with calpastatin-inhibited rat calpain 2
additional information
-
replacement of the five m-calpain residues 517-521, Glu-Ala-Asn-Ile-Glu by the corresponding six mu-calpain residues 528-533, Gln-Ala-Asn-Leu-Pro-Asp, replacement of three m-calpain residues 639-641, Pro-Cys-Gln, by the corresponding three mu-calpain residues 651-653, Asn-Lys-Lys, or replacement of two m-calpain residues 578-579, Lys-Ile by the corresponding mu-calpain residues 590-591, Arg-Ser. Mutations do not affect the expression and Kd values of the resultant calpains. In a series of hybrid mu/m large-subunit calpains, the Kd values decrease progressively towards that of mu-calpain as the portion of mu-type sequence increases from 0 to 90%
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular cloning of the cDNA for the 80000 Da subunit and expression in Escherichia coli
coexpression from large-subunit and small-subunit plasmids in Escherichia coli strain BL21(DE3)
-
the bacterial production of recombinant rat calpain II is improved greatly by the use of two compatible plasmids for the two subunits. The calpain small subunit C-terminal fragment is expressed from a new A15-based vector created by cloning T7 contol elements into pACYC177. This vector is compatible with the ColE1-based pET-24d(+) vector containing the calpain large subunit and the yield of calpain activity is increased at least 16fold by coexpression from theses two vectors. A high level of activity is also obtained from a bicistronic construct containing the subunit cDNAs under the control of one T7 promoter
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a heat stress stimulus induces massive germ cells apoptosis, which is associated with an increase in the levels of mRNA encoding calpain 2
-
calpain activation occurs during reperfusion, but only after intracellular pH normalization, and is not prevented by inhibiting its translocation during ischemia with methyl-beta-cyclodextrin
-
endoplasmic reticulum stress stimulates calpain II activation, interleukin-13 enhances endoplasmic reticulum stress-regulated calpain activation and calpain-II expression in lipopolysaccaride-activated microglia
-
m-calpain activation occurs during reperfusion, but only after intracellular pH normalization, and is not prevented by inhibiting its translocation during ischemia with methyl-beta-cyclodextrin
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
m-calpain inhibition at the time of reperfusion is a potentially useful strategy to limit infarct size
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
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
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
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
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
Rattus norvegicus
Molinari, M.; maki, M.; Carafoli, E.
Purification of mu-calpain by a novel affinity chromatography approach. New insight into the mechanism of the interaction of the protease with targets
J. Biol. Chem.
270
14576-14581
1995
Rattus norvegicus
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
Sazontova, T.G.; Matskevich, A.A.; Arkhipenko, Y.V.
Calpains: physiological and pathophysiological significance
Pathophysiology
6
91-102
1999
Rattus norvegicus
-
Deluca C.I.; Davies P.L.; Samis J.A.; Elce J.S.
Molecular cloning and bacterial expression of cDNA for rat calpain II 80 kDa subunit
Biochim. Biophys. Acta
1216
81-93
1993
Rattus norvegicus (Q07009)
Moldoveanu T.; Hosfield C.M.; Jia Z.; Elce J.S.; Davies P.L.
Ca2+-induced structural changes in rat m-calpain revealed by partial proteolysis
Biochim. Biophys. Acta
1545
245-254
2001
Rattus norvegicus (Q07009)
Arthur J.S.; Gauthier S.; Elce J.S.
Active site residues in m-calpain: identification by site-directed mutagenesis
FEBS Lett.
368
397-400
1995
Rattus norvegicus (Q07009)
Hosfield C.M.; Moldoveanu T.; Davies P.L.; Elce J.S.; Jia Z.
Calpain mutants with increased Ca2+ sensitivity and implications for the role of the C2-like domain
J. Biol. Chem.
276
7404-7407
2001
Rattus norvegicus, Rattus norvegicus (Q07009)
Hosfield C.M.; Elce J.S.; Davies P.L.; Jia Z.
Crystal structure of calpain reveals the structural basis for Ca2+-dependent protease activity and a novel mode of enzyme activation
EMBO J.
18
6880-6889
1999
Rattus norvegicus (Q07009)
Hosfield, C.M.; Ye, Q.; Arthur, J.S.C.; Hegadorn, C.; Croall, D.E.; Elce, J.S.; Jia, Z.
Crystallization and X-ray crystallographic analysis of m-calpain, a Ca2+-dependent protease
Acta Crystallogr. Sect. D
55
1484-1486
1999
Rattus norvegicus
-
Elce, J.S.; Hegadorn, C.; Gauthier, S.; Vince, J.W.; Davies, P.L.
Recombinant calpain II: improved expression systems and production of a C105A active-site mutant for crystallography
Protein Eng.
8
843-848
1995
Rattus norvegicus
Smith, S.D.; Jia, Z.; Huynh, K.K.; Wells, A.; Elce, J.S.
Glutamate substitutions at a PKA consensus site are consistent with inactivation of calpain by phosphorylation
FEBS Lett.
542
115-118
2003
Rattus norvegicus
Inserte, J.; Garcia-Dorado, D.; Hernando, V.; Soler-Soler, J.
Calpain-mediated impairment of Na+/K+-ATPase activity during early reperfusion contributes to cell death after myocardial ischemia
Circ. Res.
97
465-473
2005
Rattus norvegicus
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
Zakharov, V.V.; Mosevitsky, M.I.
M-calpain-mediated cleavage of GAP-43 near Ser41 is negatively regulated by protein kinase C, calmodulin and calpain-inhibiting fragment GAP-43-3
J. Neurochem.
101
1539-1551
2007
Rattus norvegicus, Sus scrofa
Garnham, C.; Hanna, R.; Chou, J.; Low, K.; Gourlay, K.; Campbell, R.; Beckmann, J.; Davies, P.
Limb-girdle muscular dystrophy type 2A can result from accelerated autoproteolytic inactivation of calpain 3
Biochemistry
48
3457-3467
2009
Homo sapiens (P04632), Rattus norvegicus (Q07009)
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
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
Janssens, V.; Derua, R.; Zwaenepoel, K.; Waelkens, E.; Goris, J.
Specific regulation of protein phosphatase 2A PR72/B'' subunits by calpain
Biochem. Biophys. Res. Commun.
386
676-681
2009
Rattus norvegicus
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
Liu, S.H.; Yang, C.N.; Pan, H.C.; Sung, Y.J.; Liao, K.K.; Chen, W.B.; Lin, W.Z.; Sheu, M.L.
IL-13 downregulates PPAR-gamma/heme oxygenase-1 via ER stress-stimulated calpain activation: aggravation of activated microglia death
Cell. Mol. Life Sci.
67
1465-1476
2010
Rattus norvegicus
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
Rudinskiy, N.; Grishchuk, Y.; Vaslin, A.; Puyal, J.; Delacourte, A.; Hirling, H.; Clarke, P.G.; Luthi-Carter, R.
Calpain hydrolysis of alpha- and beta2-adaptins decreases clathrin-dependent endocytosis and may promote neurodegeneration
J. Biol. Chem.
284
12447-12458
2009
Rattus norvegicus
Chan, K.T.; Bennin, D.A.; Huttenlocher, A.
Regulation of adhesion dynamics by calpain-mediated proteolysis of focal adhesion kinase (FAK)
J. Biol. Chem.
285
11418-11426
2010
Rattus norvegicus
Lizama, C.; Lagos, C.F.; Lagos-Cabre, R.; Cantuarias, L.; Rivera, F.; Huenchunir, P.; Perez-Acle, T.; Carrion, F.; Moreno, R.D.
Calpain inhibitors prevent p38 MAPK activation and germ cell apoptosis after heat stress in pubertal rat testes
J. Cell. Physiol.
221
296-305
2009
Rattus norvegicus
Hernando, V.; Inserte, J.; Sartorio, C.L.; Parra, V.M.; Poncelas-Nozal, M.; Garcia-Dorado, D.
Calpain translocation and activation as pharmacological targets during myocardial ischemia/reperfusion
J. Mol. Cell. Cardiol.
49
271-279
2010
Rattus norvegicus
Toke, O.; Banoczi, Z.; Tarkanyi, G.; Friedrich, P.; Hudecz, F.
Folding transitions in calpain activator peptides studied by solution NMR spectroscopy
J. Pept. Sci.
15
404-410
2009
Rattus norvegicus
Cortesio, C.L.; Perrin, B.J.; Bennin, D.A.; Huttenlocher, A.
Actin-binding protein-1 interacts with WASp-interacting protein to regulate growth factor-induced dorsal ruffle formation
Mol. Biol. Cell
21
186-197
2010
Rattus norvegicus
Liu, W.; Zhou, X.W.; Liu, S.; Hu, K.; Wang, C.; He, Q.; Li, M.
Calpain-truncated CRMP-3 and -4 contribute to potassium deprivation-induced apoptosis of cerebellar granule neurons
Proteomics
9
3712-3728
2009
Rattus norvegicus
Ozaki, T.; Yamashita, T.; Ishiguro, S.
Ca2+-induced release of mitochondrial m-calpain from outer membrane with binding of calpain small subunit and Grp75
Arch. Biochem. Biophys.
507
254-261
2011
Rattus norvegicus
Huang, C.; Gurlo, T.; Haataja, L.; Costes, S.; Daval, M.; Ryazantsev, S.; Wu, X.; Butler, A.; Butler, P.
Calcium-activated calpain-2 is a mediator of beta cell dysfunction and apoptosis in type 2 diabetes
J. Biol. Chem.
285
339-348
2010
Rattus norvegicus
Banoczi, Z.; Tantos, A.; Farkas, A.; Majer, Z.; Dokus, L.E.; Tompa, P.; Hudecz, F.
New m-calpain substrate-based azapeptide inhibitors
J. Pept. Sci.
19
370-376
2013
Rattus norvegicus
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