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Synonyms
m-calpain, calpain ii, calpain-2, calpain 2, calpain2, ncl-2, milli-calpain, mitochondrial m-calpain, calpain-2-like, rat calpain 2,
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GAP-43 + H2O
GAP-43-3 + ?
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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
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?
microtubule-associated protein 1
?
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?
microtubule-associated protein 2
?
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-
?
selenoprotein K + H2O
?
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cleavage occurs only in unactivated macrophages, m-calpain cleavage at Arg81-Gly82 generates the two selenoprotein K isoforms
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-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
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-
?
succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
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-
-
-
?
additional information
?
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MARCKS protein + H2O
?
MARCKS protein i.e. myristoylated alanine-rich C kinase substrate is a substrate of calpain-2 in the presence of Ca2+. Calpain-2 proteolysis of MARCKS promotes its interaction with lipids and ENaC at the plasma membrane to allow for the phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent regulation of epithelial sodium channel (ENaC) activity in the kidney
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-
?
MARCKS protein + H2O
?
MARCKS protein i.e. myristoylated alanine-rich C kinase substrate is a substrate of calpain-2 in the presence of Ca2+
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?
additional information
?
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enzyme is involved in myofibrillar protein degradation
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?
additional information
?
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enzyme is involved in myofibrillar protein degradation
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?
additional information
?
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hypoxia upregulates calpain activity and mRNA expression in pulmonary artery endothelial cells
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?
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Cbz-Leu-DL-Abu-CONH-(CH2)3-(4-methylpiperazin-1-yl)
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Cbz-Leu-DL-Abu-CONH-(CH2)3-2-methoxyadenin-9-yl
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Cbz-Leu-DL-Abu-CONH-(CH2)3-adenin-9-yl
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Cbz-Leu-DL-Abu-CONH-(CH2)3-cytosin-3-yl
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Cbz-Leu-DL-Abu-CONH-(CH2)3-morpholine
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CBZ-Leu-DL-Phe-CONH-(CH2)2-N-(CH3)2
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CBZ-Leu-DL-Phe-CONH-(CH2)3-(4-methylpiperazin-1-yl)
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CBZ-Leu-DL-Phe-CONH-(CH2)3-2-methoxyadenin-9-yl
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CBZ-Leu-DL-Phe-CONH-(CH2)3-adenin-9-yl
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best inhibitor
CBZ-Leu-DL-Phe-CONH-(CH2)3-cytosin-3-yl
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CBZ-Leu-DL-Phe-CONH-(CH2)3-N-(CH3)2
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GAP-43-3
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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
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NaCl
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m-calpain is more active at 165 mM NaCl than at 295 mM NaCl
calpastatin
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calpastatin
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inhibition of m-calpain is greater at pH 7.5 than at pH 6.5 at both 165 mM and 295 mM NaCl. Percentage inhibition is greater at 295 mM than at 165 mM NaCl
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calpastatin
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oxidation lowers calpastatin inhibition of m-calpain at al pH and ionic strength combinations
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0.000286
Cbz-Leu-DL-Abu-CONH-(CH2)3-(4-methylpiperazin-1-yl)
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in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.000077
Cbz-Leu-DL-Abu-CONH-(CH2)3-2-methoxyadenin-9-yl
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in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.00007
Cbz-Leu-DL-Abu-CONH-(CH2)3-adenin-9-yl
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in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.00114
Cbz-Leu-DL-Abu-CONH-(CH2)3-cytosin-3-yl
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in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.000041
Cbz-Leu-DL-Abu-CONH-(CH2)3-morpholine
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in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.00352
CBZ-Leu-DL-Phe-CONH-(CH2)2-N-(CH3)2
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in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.00636
CBZ-Leu-DL-Phe-CONH-(CH2)3-(4-methylpiperazin-1-yl)
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in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.000209
CBZ-Leu-DL-Phe-CONH-(CH2)3-2-methoxyadenin-9-yl
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in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.000068
CBZ-Leu-DL-Phe-CONH-(CH2)3-adenin-9-yl
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in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.000438
CBZ-Leu-DL-Phe-CONH-(CH2)3-cytosin-3-yl
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in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.000844
CBZ-Leu-DL-Phe-CONH-(CH2)3-N-(CH3)2
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in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
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Sun, W.; Ji, S.Q.; Ebert, P.J.; Bidwell, C.A.; Hancock, D.L.
Cloning the partial cDNAs of mu-calpain and m-calpain from porcine skeletal muscle
Biochimie
75
931-936
1993
Sus scrofa (P43367), Sus scrofa
brenda
Fukui, I.; Toyohara, H.; Ito, K.; Hamakubo, T.; Murachi, T.
Molecular and catalytic characterization of intact heterodimeric and derived monomeric calpains isolated under different conditions from pig polymorphonuclear leukocytes
Biochemistry
27
3260-3267
1988
Sus scrofa
brenda
Yoshimura, N.; Tsukahara, I.; Murachi, T.
Calpain and calpastatin in porcine retina
Biochem. J.
223
47-51
1984
Sus scrofa
brenda
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
brenda
Zhang J.L.; Patel J.M.; Block E.R.
Hypoxia-specific upregulation of calpain activity and gene expression in pulmonary artery endothelial cells
Am. J. Physiol.
275
L461-L468
1998
Sus scrofa (P43367)
brenda
Maddock, K.R.; Huff-Lonergan, E.; Rowe, L.J.; Lonergan, S.M.
Effect of pH and ionic strength on mu- and m-calpain inhibition by calpastatin
J. Anim. Sci.
83
1370-1376
2005
Sus scrofa
brenda
Carlin, K.R.; Huff-Lonergan, E.; Rowe, L.J.; Lonergan, S.M.
Effect of oxidation, pH, and ionic strength on calpastatin inhibition of mu- and m-calpain
J. Anim. Sci.
84
925-937
2006
Sus scrofa
brenda
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
brenda
Kim, Y.; Huff-Lonergan, E.; Lonergan, S.
Effect of calcium lactate on m-calpain activity and protein degradation under oxidising conditions
Food Chem.
131
73-78
2012
Sus scrofa
-
brenda
Huang, Z.; Hoffmann, F.W.; Norton, R.L.; Hashimoto, A.C.; Hoffmann, P.R.
Selenoprotein K is a novel target of m-calpain, and cleavage is regulated by Toll-like receptor-induced calpastatin in macrophages
J. Biol. Chem.
286
34830-34838
2011
Sus scrofa
brenda
Ovat, A.; Li, Z.; Hampton, C.; Asress, S.; Fernandez, F.; Glass, J.; Powers, J.
Peptidyl alpha-ketoamides with nucleobases, methylpiperazine, and dimethylaminoalkyl substituents as calpain inhibitors
J. Med. Chem.
53
6326-6336
2010
Sus scrofa
brenda
Montgomery, D.S.; Yu, L.; Ghazi, Z.M.; Thai, T.L.; Al-Khalili, O.; Ma, H.P.; Eaton, D.C.; Alli, A.A.
ENaC activity is regulated by calpain-2 proteolysis of MARCKS proteins
Am. J. Physiol. Cell Physiol.
313
C42-C53
2017
Sus scrofa (P43367)
brenda