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Information on EC 3.4.22.53 - calpain-2 and Organism(s) Homo sapiens and UniProt Accession P07384

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     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.53 calpain-2
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: P07384 not found.
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
broad endopeptidase specificity
Synonyms
3.4.22.17, Cal II, calcium-activated neutral protease II, calpain 2, calpain II, calpain xCL-2 (Xenopus leavis), calpain-2, calpain-2-like, calpain2, CAPN II, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
calcium-activated neutral protease II
-
-
-
-
calpain 2
calpain II
calpain xCL-2 (Xenopus leavis)
-
-
-
-
calpain2
247
-
CAPN2
247
-
CAPN2 g.p. (Homo sapiens)
-
-
-
-
CPN2
247
-
EC 3.4.22.17
247
formerly
human calpain 2
274481
-
m-calpain
milli-calpain
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
702693-80-9
-
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
alpha-2 spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
androgen receptor + H2O
?
show the reaction diagram
-
-
-
-
?
androgen receptor + H2O
low molecular weight androgen receptor + ?
show the reaction diagram
-
-
-
-
?
Bcl-xL + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
filamin A + H2O
?
show the reaction diagram
-
-
-
-
?
myocillin + H2O
?
show the reaction diagram
RRRRRRRR-(EDANS)-GQQEVYGMMPRDG-(DABCYL) + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
talin + H2O
?
show the reaction diagram
-
-
-
-
?
tert-butyloxycarbonyl-L-leucyl-L-methionine-7-amido-4-chloromethylcoumarin + H2O
tert-butyloxycarbonyl-L-leucyl-L-methionine + 7-amino-4-chloromethylcoumarin
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-2 spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
androgen receptor + H2O
?
show the reaction diagram
-
-
-
-
?
filamin A + H2O
?
show the reaction diagram
-
-
-
-
?
myocillin + H2O
?
show the reaction diagram
-
calpain II is responsible for the intracellular processing of myocilin in the lumen of the endoplasmic reticulum. It is proposed that this cleavage might regulate extracellular interactions of myocilin, contributing to the control of intraocular pressure
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-Leu-Leu-Nle-CHO
-
complete inhibition at 0.001 mM
ALLM
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-
ALLN
-
-
benzyloxycarbonyl-L-leucyl-L-leucinal
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-
calpastatin
-
Calpeptin
PD150606
-
-
SNJ-1945
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
upregulation of calpain 2 post eccentric exercise
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
calpain-1 catalytic subunit
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
calpain 2 is important for both the formation of invadopodia and invasive capacity of breast cancer cells
Manually annotated by BRENDA team
-
pulmonary microvascular endothelial cell. Incubation of the cells with vascular endothelial growth factor results in dose- and time-dependent increases in calpain activity and protein content of calpain-2. Vascular endothelial growth factor does not change the protein contents of calpain-1 and the small subunit or of calpastatin. Inhibition of calpain activity by siRNA directed against calpain-2 and by overexpression of calpastatin prevents vascular endothelial growth factor-induced increases in actin stress fibers in endothelial cells and angiogenesis
Manually annotated by BRENDA team
-
calpain 2 localizes to GM-3-rich lipid rafts at the leading edge
Manually annotated by BRENDA team
-
membrane abnormalities and altered signaling pathways observed in Duchenne muscular dystrophy lymphocytes may be due to the increased association of calpain II onto membrane and cytosol
Manually annotated by BRENDA team
-
primary neutrophil
Manually annotated by BRENDA team
-
calpain 2 activity is critical for the life cycle of echovirus 1 and important in the multiplication of the viral RNA genome
Manually annotated by BRENDA team
-
active calpain 2 is concentrated in the trailing edge of the migrating T cell
Manually annotated by BRENDA team
-
physiological shear stress elicits Ca2+ influx-sensitive activation of m-calain in umbilical vein endothelial cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
membrane abnormalities and altered signaling pathways observed in Duchenne muscular dystrophy lymphocytes may be due to the increased association of calpain II onto membrane and cytosol
Manually annotated by BRENDA team
-
membrane abnormalities and altered signaling pathways observed in Duchenne muscular dystrophy lymphocytes may be due to the increased association of calpain II onto membrane and cytosol
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
-
calpain 2 regulates endothelial nitric oxide synthase phosphorylation during cord formation by lymphatic endothelial cells on Matrigel
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
CAN1_HUMAN
714
0
81890
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
-
1 * 80000 + 1 * 32000, only the 80000 Da subunit shows catalytic ativity, SDS-PAGE
80000
-
1 * 80000 + 1 * 32000, only the 80000 Da subunit shows catalytic ativity, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
1 * 80000 + 1 * 32000, only the 80000 Da subunit shows catalytic ativity, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
brain-derived neurotrophic factor stimulates m-calpain serine phosphorylation
side-chain modification
-
calpain-2 is small ubiquitin-like modifier-modified at lysine residue 390, sumoylation is important for calpain-2 activity
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
full-length human m-calpain containing an N-terminal Gly-Arg-Arg-Asp-Arg-Ser L-chain elongation overexpressed in a baculovirus expression system. Crystals grown by vapor diffusion. The 2.3 A crystal structure of full length heterodimeric m-calpain crystallized in the absence of calcium reveals an oval disc-like shape, with the papain-like catalytic domain dII and the two calmodulin, like domains dIV+dVI occupying opposite poles, and the tumor necrosis factor alpha-like beta-sandwich domain dIII and the N-terminal segments dI+dV located between
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C105S
-
mutant enzyme of mutant large subunit m-C105S-80K, coexpressed with 30000 Da subunit in Sf-9 cells does not degrade casein nor the artificial substrate succinyl-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide. The mutant enzyme does not show autolytic activity with Ca2+
K390R
-
overexpression of K390R mutant fails to increase the calpain activity since sumoylation at K390 is important for calpain-2 activity
additional information
used as a model for calpain 3 in combination with calpastatin-inhibited rat calpain 2
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
m-calpain loses 50-55% of its proteolytic activity within 5 min during incubation at pH 7.5 in 300 mM or high salt and at a slower rat in 100 mM salt. This loss of activity is not reversed by dialysis for 18 h against a low-ionic-strength buffer at pH 7.5. Proteolytic activity of the unautolyzed calpains is not affected by incubation for 45 min at ionic strength up to 1000 mM. Ionic strengths of 100 mM or above cause dissociation of the two subunits of autolyzed calpains. The dissociated large subunits aggregate to form dimers and trimers, which are proteolytically inactive
-
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
cloning of the cDNA for the large subunit
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development of an adenoviral vector harboring calpain-2 siRNA expression unit in which sense and anti-sense strands composing the siRNA duplex are connected by a loop and transcribed into a siRNA in porcine pulmonary artery endothelial cells. The adenoviral vector harboring calpain-2 siRNA expression unit is a valuable tool to study the biology of calpains
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functional analysis of the upstream region of the gene for the large subunit by means of transient expression assay on HeLa cells using chloramphenicol transferase constructs identifies four negative regulatory regions tandemly reiterated just upstream of the promoter region, P1 and P2
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m-calpain is produced in a soluble form using a baculovirus expression system
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
0.1 mM indomethacin and 0.1 mM NS-398 decrease expression of calpain 2 in total membrane fractions and in plasma membranes by 70%, while 0.001 mM SC-560 decreases expression of calpain 2 in total membrane fractions and in plasma membranes by 30%
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a 6-day treatment with siRNA results in an about 60% reduction of calpain 2 protein levels in R1 cells
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brain-derived neurotrophic factor and epidermal growth factor activate neuronal m-calpain via mitogen-activated protein kinase-dependent phosphorylation
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incubation of human retinal microvascular endothelial cells with vascular endothelial growth factor results in 1.6fold increased activity of calpain 2 at 24 h
-
inhibition of MEK1/2 using PD98059 reduces the expression of calpain-2
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p38 MAPK and JNK are required to stimulate m-calpain activity when TRPM7 is overexpressed, TRPM7-mediated activation of m-calpain is not dependent on the nature of the divalent conducted by the channel
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
m-calpain is a marker of tumor aggressiveness and is apotential target for limiting development of rhabdomyosarcoma tumor as well as their metastatic behavior
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shastri, R.; Jagadeesh, G.; Anandaraj, M.P.J.S.
Human placental calcium activated neutral proteinase: Separation and functional characterization of subunits
J. Biosci.
15
427-434
1990
Homo sapiens
-
Manually annotated by BRENDA team
Rojas, F.J.; Brush, M.; Moretti-Rojas, I.
Calpain-calpastatin: a novel, complete calcium-dependent protease system in human spermatozoa
Mol. Hum. Reprod.
5
520-526
1999
Homo sapiens
Manually annotated by BRENDA team
Strobl S.; Fernandez-Catalan C.; Braun M.; Huber R.; Masumoto H.; Nakagawa K.; Irie A.; Sorimachi H.; Bourenkow G.; Bartunik H.; Suzuki K.; Bode W.
The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium
Proc. Natl. Acad. Sci. USA
97
588-592
2000
Homo sapiens, Homo sapiens (P17655)
Manually annotated by BRENDA team
Imajoh S.; Aoki K.; Ohno S.; Emori Y.; Kawasaki H.; Sugihara H.; Suzuki K.
Molecular cloning of the cDNA for the large subunit of the high-Ca2+-requiring form of human Ca2+-activated neutral protease
Biochemistry
27
8122-8128
1988
Homo sapiens (P17655)
Manually annotated by BRENDA team
Hata A.; Ohno S.; Akita Y.; Suzuki K.
Tandemly reiterated negative enhancer-like elements regulate transcription of a human gene for the large subunit of calcium-dependent protease
J. Biol. Chem.
264
6404-6411
1989
Homo sapiens (P17655)
Manually annotated by BRENDA team
Ye Z.; Connor J.R.
cDNA cloning by amplification of circularized first strand cDNAs reveals non-IRE-regulated iron-responsive mRNAs
Biochem. Biophys. Res. Commun.
275
223-227
2000
Homo sapiens (P17655)
Manually annotated by BRENDA team
Strausberg R.L.; Feingold E.A.; Grouse L.H.; Derge J.G.; et al.
Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences
Proc. Natl. Acad. Sci. USA
99
16899-16903
2002
Homo sapiens (P17655)
Manually annotated by BRENDA team
Masumoto, H.; Yoshizawa, T.; Sorimachi, H.; Nishino, T.; Ishiura, S.; Suzuki, K.
Overexpression, purification, and characterization of human m-calpain and its active site mutant, m-C105S-calpain, using a baculovirus expression system
J. Biochem.
124
957-961
1998
Homo sapiens
Manually annotated by BRENDA team
Dedieu, S.; Mazeres, G.; Dourdin, N.; Cottin, P.; Brustis, J.J.
Transactivation of capn2 by Myogenic Regulatory Factors During Myogenesis
J. Mol. Biol.
326
453-465
2003
Homo sapiens
Manually annotated by BRENDA team
Veerann, V.; Kaji, T.; Boland, B.; Odrljin, T.; Mohan, P.; Basavarajappa, B.S.; Peterhoff, C.; Cataldo, A.; Rudnicki, A.; Amin, N.; Li, B.S.; Pant, H.C.; Hungund, B.L.; Arancio, O.; Nixon, R.A.
Calpain mediates calcium-induced activation of the Erk1,2 MAPK pathway and cytoskeletal phosphorylation in neurons: Relevance to Alzheimers disease
Am. J. Pathol.
165
795-805
2004
Homo sapiens
Manually annotated by BRENDA team
Li, H.; Thompson, V.F.; Goll, D.E.
Effects of autolysis on properties of mu- and m-calpain
Biochim. Biophys. Acta
1691
91-103
2004
Homo sapiens
Manually annotated by BRENDA team
Carragher, N.O.
Calpain inhibition: a therapeutic strategy targeting multiple disease states
Curr. Pharm. Des.
12
615-638
2006
Homo sapiens, Homo sapiens (P07384)
Manually annotated by BRENDA team
Upla, P.; Marjomaeki, V.; Nissinen, L.; Nylund, C.; Waris, M.; Hyypiae, T.; Heino, J.
Calpain 1 and 2 are required for RNA replication of echovirus 1
J. Virol.
82
1581-1590
2008
Homo sapiens
Manually annotated by BRENDA team
Miyazaki, T.; Honda, K.; Ohata, H.
Requirement of Ca2+ influx- and phosphatidylinositol 3-kinase-mediated m-calpain activity for shear stress-induced endothelial cell polarity
Am. J. Physiol.
293
C1216-C1225
2007
Homo sapiens
Manually annotated by BRENDA team
Shanmuga Sundaram, J.; Mohana Rao, V.; Meena, A.K.; Anandaraj, M.P.
Altered expression, intracellular distribution and activity of lymphocyte calpain II in Duchenne muscular dystrophy
Clin. Chim. Acta
373
82-87
2006
Homo sapiens
Manually annotated by BRENDA team
Su, Y.; Cui, Z.; Li, Z.; Bloc, E.R.
Calpain-2 regulation of VEGF-mediated angiogenesis
FASEB J.
20
1443-1451
2006
Homo sapiens
Manually annotated by BRENDA team
Maehara, H.; Suzuki, K.; Sasaki, T.; Oshita, H.; Wada, E.; Inoue, T.; Shimizu, K.
G1-G2 aggrecan product that can be generated by M-calpain on truncation at Ala709-Ala710 is present abundantly in human articular cartilage
J. Biochem.
141
469-477
2007
Homo sapiens
Manually annotated by BRENDA team
Sanchez-Sanchez, F.; Martinez-Redondo, F.; Aroca-Aguilar, J.D.; Coca-Prados, M.; Escribano, J.
Characterization of the intracellular proteolytic cleavage of myocilin and identification of calpain II as a myocilin-processing protease
J. Biol. Chem.
282
27810-27824
2007
Homo sapiens
Manually annotated by BRENDA team
Cortesio, C.L.; Chan, K.T.; Perrin, B.J.; Burton, N.O.; Zhang, S.; Zhang, Z.Y.; Huttenlocher, A.
Calpain 2 and PTP1B function in a novel pathway with Src to regulate invadopodia dynamics and breast cancer cell invasion
J. Cell Biol.
180
957-971
2008
Homo sapiens
Manually annotated by BRENDA team
Nuzzi, P.A.; Senetar, M.A.; Huttenlocher, A.
Asymmetric localization of calpain 2 during neutrophil chemotaxis
Mol. Biol. Cell
18
795-805
2007
Homo sapiens
Manually annotated by BRENDA team
Qiu, K.; Su, Y.; Block, E.R.
Use of recombinant calpain-2 siRNA adenovirus to assess calpain-2 modulation of lung endothelial cell migration and proliferation
Mol. Cell. Biochem.
292
69-78
2006
Homo sapiens
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Vissing, K.; Overgaard, K.; Nedergaard, A.; Fredsted, A.; Schjerling, P.
Effects of concentric and repeated eccentric exercise on muscle damage and calpain-calpastatin gene expression in human skeletal muscle
Eur. J. Appl. Physiol.
103
323-332
2008
Homo sapiens, Homo sapiens (P17655)
Manually annotated by BRENDA team
Babbin, B.A.; Koch, S.; Bachar, M.; Conti, M.A.; Parkos, C.A.; Adelstein, R.S.; Nusrat, A.; Ivanov, A.I.
Non-muscle myosin IIA differentially regulates intestinal epithelial cell restitution and matrix invasion
Am. J. Pathol.
174
436-448
2009
Homo sapiens
Manually annotated by BRENDA team
Wang, H.C.; Huang, Y.S.; Ho, C.C.; Jeng, J.C.; Shih, H.M.
SUMO modification modulates the activity of calpain-2
Biochem. Biophys. Res. Commun.
384
444-449
2009
Homo sapiens
Manually annotated by BRENDA team
Meng, X.N.; Jin, Y.; Yu, Y.; Bai, J.; Liu, G.Y.; Zhu, J.; Zhao, Y.Z.; Wang, Z.; Chen, F.; Lee, K.Y.; Fu, S.B.
Characterisation of fibronectin-mediated FAK signalling pathways in lung cancer cell migration and invasion
Br. J. Cancer
101
327-334
2009
Homo sapiens
Manually annotated by BRENDA team
Barbero, S.; Mielgo, A.; Torres, V.; Teitz, T.; Shields, D.J.; Mikolon, D.; Bogyo, M.; Barila, D.; Lahti, J.M.; Schlaepfer, D.; Stupack, D.G.
Caspase-8 association with the focal adhesion complex promotes tumor cell migration and metastasis
Cancer Res.
69
3755-3763
2009
Homo sapiens
Manually annotated by BRENDA team
Pilop, C.; Aregger, F.; Gorman, R.C.; Brunisholz, R.; Gerrits, B.; Schaffner, T.; Gorman, J.H.; Matyas, G.; Carrel, T.; Frey, B.M.
Proteomic analysis in aortic media of patients with Marfan syndrome reveals increased activity of calpain 2 in aortic aneurysms
Circulation
120
983-991
2009
Homo sapiens
Manually annotated by BRENDA team
Roumes, H.; Leloup, L.; Dargelos, E.; Brustis, J.J.; Daury, L.; Cottin, P.
Calpains: markers of tumor aggressiveness?
Exp. Cell Res.
316
1587-1599
2010
Homo sapiens
Manually annotated by BRENDA team
Chen, H.; Libertini, S.J.; Wang, Y.; Kung, H.J.; Ghosh, P.; Mudryj, M.
ERK regulates calpain 2-induced androgen receptor proteolysis in CWR22 relapsed prostate tumor cell lines
J. Biol. Chem.
285
2368-2374
2010
Homo sapiens
Manually annotated by BRENDA team
Liu, Z.; Wang, S.; Zhou, H.; Yang, Y.; Zhang, M.
Na+/H+ exchanger mediates TNF-alpha-induced hepatocyte apoptosis via the calpain-dependent degradation of Bcl-xL
J. Gastroenterol. Hepatol.
24
879-885
2009
Homo sapiens
Manually annotated by BRENDA team
Su, L.T.; Chen, H.C.; Gonzalez-Pagan, O.; Overton, J.D.; Xie, J.; Yue, L.; Runnels, L.W.
TRPM7 activates m-calpain by stress-dependent stimulation of p38 MAPK and c-Jun N-terminal kinase
J. Mol. Biol.
396
858-869
2010
Homo sapiens
Manually annotated by BRENDA team
Zadran, S.; Jourdi, H.; Rostamiani, K.; Qin, Q.; Bi, X.; Baudry, M.
Brain-derived neurotrophic factor and epidermal growth factor activate neuronal m-calpain via mitogen-activated protein kinase-dependent phosphorylation
J. Neurosci.
30
1086-1095
2010
Homo sapiens
Manually annotated by BRENDA team
Ma, H.; Tochigi, A.; Shearer, T.R.; Azuma, M.
Calpain inhibitor SNJ-1945 attenuates events prior to angiogenesis in cultured human retinal endothelial cells
J. Ocul. Pharmacol. Ther.
25
409-414
2009
Homo sapiens
Manually annotated by BRENDA team
Jang, H.S.; Lal, S.; Greenwood, J.A.
Calpain 2 is required for glioblastoma cell invasion: regulation of matrix metalloproteinase 2
Neurochem. Res.
35
1796-1804
2010
Homo sapiens
Manually annotated by BRENDA team
Svensson, L.; McDowall, A.; Giles, K.M.; Stanley, P.; Feske, S.; Hogg, N.
Calpain 2 controls turnover of LFA-1 adhesions on migrating T lymphocytes
PLoS ONE
5
e15090
2010
Homo sapiens
Manually annotated by BRENDA team
Prangsaengtong, O.; Senda, K.; Doki, Y.; Park, J.Y.; Jo, M.; Sakurai, H.; Shibahara, N.; Saiki, I.; Koizumi, K.
Calpain 1 and -2 play opposite roles in cord formation of lymphatic endothelial cells via eNOS regulation
Hum. Cell
25
36-44
2012
Homo sapiens
Manually annotated by BRENDA team
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