메뉴 건너뛰기




Volumn 15, Issue 3, 2011, Pages 309-323

Calpains as potential anti-cancer targets

Author keywords

Apoptosis; Calpains; Cancer; Invasion; Migration

Indexed keywords

ACETYLSALICYLIC ACID; BEVACIZUMAB; BORTEZOMIB; CALPAIN; CALPAIN 3; CALPAIN 6; CALPAIN 9; CALPASTATIN; CISPLATIN; CURCUMIN; GENISTEIN; OXALIPLATIN; RANIBIZUMAB; RESVERATROL; TRASTUZUMAB; UNCLASSIFIED DRUG;

EID: 79951600584     PISSN: 14728222     EISSN: None     Source Type: Journal    
DOI: 10.1517/14728222.2011.553611     Document Type: Review
Times cited : (95)

References (101)
  • 3
    • 0037025350 scopus 로고    scopus 로고
    • Calpain cleaves RhoA generating a dominant-negative form that inhibits integrin-induced actin filament assembly and cell spreading
    • DOI 10.1074/jbc.M203457200
    • Kulkarni S, Goll DE, Fox JEB. Calpain cleaves RhoA generating a dominant-negative form that inhibits integrin-induced actin filament assembly and cell spreading. J Biol Chem 2002;277:24435-41 (Pubitemid 34951967)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.27 , pp. 24435-24441
    • Kulkarni, S.1    Goll, D.E.2    Fox, J.E.B.3
  • 4
    • 65449148205 scopus 로고    scopus 로고
    • Talin phosphorylation by Cdk5 regulates Smurf1-mediated talin head ubiquitylation and cell migration
    • Huang C, Rajfur Z, Yousefi N, et al. Talin phosphorylation by Cdk5 regulates Smurf1-mediated talin head ubiquitylation and cell migration. Nat Cell Biol 2009;11:624-30
    • (2009) Nat. Cell Biol. , vol.11 , pp. 624-630
    • Huang, C.1    Rajfur, Z.2    Yousefi, N.3
  • 5
    • 0027990307 scopus 로고
    • The calpain cleavage sites in the epidermal growth factor receptor kinase domain
    • DOI 10.1111/j.1432-1033.1994.tb19013.x
    • Gregoriou M, Willis AC, Pearson MA, et al. The calpain cleavage sites in the epidermal growth factor receptor kinase domain. Eur J Biochem 1994;223:455-64 (Pubitemid 24244192)
    • (1994) European Journal of Biochemistry , vol.223 , Issue.2 , pp. 455-464
    • Gregoriou, M.1    Willis, A.C.2    Pearson, M.A.3    Crawford, C.4
  • 7
    • 0033772073 scopus 로고    scopus 로고
    • Genetic variation in the gene encoding calpain-10 is associated with type 2 diabetes mellitus
    • Horikawa Y, Oda N, Cox NJ, et al. Genetic variation in the gene encoding calpain-10 is associated with type 2 diabetes mellitus. Nat Genet 2000;26:163-75
    • (2000) Nat. Genet. , vol.26 , pp. 163-175
    • Horikawa, Y.1    Oda, N.2    Cox, N.J.3
  • 9
    • 0031591699 scopus 로고    scopus 로고
    • 1 phase
    • DOI 10.1006/bbrc.1997.7003
    • Mellgren RL. Evidence for participation of a calpain-like cysteine protease in cell cycle progression through late G1 phase. Biochem Biophys Res Commun 1997;236:555-8 (Pubitemid 27384663)
    • (1997) Biochemical and Biophysical Research Communications , vol.236 , Issue.3 , pp. 555-558
    • Mellgren, R.L.1
  • 11
    • 33645030937 scopus 로고    scopus 로고
    • Identification of calpain cleavage sites in the G1 cyclin-dependent kinase inhibitor p19INK4d
    • Joy J, Nalabothula N, Ghosh M, et al. Identification of calpain cleavage sites in the G1 cyclin-dependent kinase inhibitor p19(INK4d). Biol Chem 2006;387:329-35
    • (2006) Biol. Chem. , vol.387 , pp. 329-335
    • Joy, J.1    Nalabothula, N.2    Ghosh, M.3
  • 13
    • 0037421967 scopus 로고    scopus 로고
    • Cyclin E in breast tumors is cleaved into its low molecular weight forms by calpain
    • DOI 10.1038/sj.onc.1206166
    • Wang XD, Rosales JL, Magliocco A, et al. Cyclin E in breast tumors is cleaved into its low molecular weight forms by calpain. Oncogene 2003;22:769-74 (Pubitemid 36269291)
    • (2003) Oncogene , vol.22 , Issue.5 , pp. 769-774
    • Wang, X.D.1    Rosales, J.L.2    Magliocco, A.3    Gnanakumar, R.4    Lee, K.-Y.5
  • 14
    • 0034745182 scopus 로고    scopus 로고
    • cip1 in cells productively infected with human cytomegalovirus
    • DOI 10.1128/JVI.75.8.3613-3625.2001
    • Chen Z, Knutson E, Kurosky A, et al. Degradation of p21cip1 in cells productively infected with human cytomegalovirus. J Virol 2001;75:3613-25 (Pubitemid 32246371)
    • (2001) Journal of Virology , vol.75 , Issue.8 , pp. 3613-3625
    • Chen, Z.1    Knutson, E.2    Kurosky, A.3    Albrecht, T.4
  • 18
    • 0001110114 scopus 로고    scopus 로고
    • Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases
    • DOI 10.1074/jbc.275.7.5131
    • Chua BT, Guo K, Li P. Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases. J Biol Chem 2000;275:5131-5 (Pubitemid 30108915)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.7 , pp. 5131-5135
    • Chua, B.T.1    Guo, K.2    Li, P.3
  • 19
    • 0034698878 scopus 로고    scopus 로고
    • Cross-talk between two cysteine protease families: Activation of caspase-12 by calpain in apoptosis
    • DOI 10.1083/jcb.150.4.887
    • Nakagawa T, Yuan J. Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. J Cell Biol 2000;150:887-94 (Pubitemid 30663424)
    • (2000) Journal of Cell Biology , vol.150 , Issue.4 , pp. 887-894
    • Nakagawa, T.1    Yuan, J.2
  • 20
    • 0033956278 scopus 로고    scopus 로고
    • Calpain and caspase: Can you tell the difference?
    • DOI 10.1016/S0166-2236(99)01479-4, PII S0166223699014794
    • Wang KK. Calpain and caspase: can you tell the difference? Trends Neurosci 2000;23:20-6 (Pubitemid 30100309)
    • (2000) Trends in Neurosciences , vol.23 , Issue.1 , pp. 20-26
    • Wang, K.K.W.1
  • 21
    • 0031014946 scopus 로고    scopus 로고
    • Proteolytic cleavage of human p53 by calpain: A potential regulator of protein stability
    • Kubbutat MH, Vousden KH. Proteolytic cleavage of human p53 by calpain: a potential regulator of protein stability. Mol Cell Biol 1997;17:460-8 (Pubitemid 26425636)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.1 , pp. 460-468
    • Kubbutat, M.H.G.1    Vousden, K.H.2
  • 22
    • 0036168356 scopus 로고    scopus 로고
    • Cutting to the chase: Calpain proteases in cell motility
    • DOI 10.1016/S0962-8924(01)02179-1, PII S0962892401021791
    • Glading A, Lauffenburger DA, Wells A. Cutting to the chase: calpain proteases in cell motility. Trends Cell Biol 2002;12:46-54 (Pubitemid 34164156)
    • (2002) Trends in Cell Biology , vol.12 , Issue.1 , pp. 46-54
    • Glading, A.1    Lauffenburger, D.A.2    Wells, A.3
  • 23
    • 0036711804 scopus 로고    scopus 로고
    • Regulation of focal complex composition and disassembly by the calcium-dependent protease calpain
    • Bhatt A, Kaverina I, Otey C, et al. Regulation of focal complex composition and disassembly by the calcium-dependent protease calpain. J Cell Sci 2002;115:3415-25 (Pubitemid 34994031)
    • (2002) Journal of Cell Science , vol.115 , Issue.17 , pp. 3415-3425
    • Bhatt, A.1    Kaverina, I.2    Otey, C.3    Huttenlocher, A.4
  • 25
    • 33745829449 scopus 로고    scopus 로고
    • Spatial localization of m-Calpain to the plasma membrane by phosphoinositide biphosphate binding during epidermal growth factor receptor-mediated activation
    • DOI 10.1128/MCB.02243-05
    • Shao H, Chou J, Baty CJ, et al. Spatial localization of m-calpain to the plasma membrane by phosphoinositide biphosphate binding during epidermal growth factor receptor-mediated activation. Mol Cell Biol 2006;26:5481-96 (Pubitemid 44036214)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.14 , pp. 5481-5496
    • Shao, H.1    Chou, J.2    Baty, C.J.3    Burke, N.A.4    Watkins, S.C.5    Stolz, D.B.6    Wells, A.7
  • 26
    • 77958502543 scopus 로고    scopus 로고
    • M-calpain activation is regulated by its membrane localization and by its binding to phosphatidylinositol 45-bisphosphate
    • Leloup L, Shao H, Bae YH, et al. m-Calpain activation is regulated by its membrane localization and by its binding to phosphatidylinositol 4,5-bisphosphate. J Biol Chem 2010;285:33549-66
    • (2010) J. Biol. Chem. , vol.285 , pp. 33549-33566
    • Leloup, L.1    Shao, H.2    Bae, Y.H.3
  • 27
    • 4043077024 scopus 로고    scopus 로고
    • Isoform specific function of calpain 2 in regulating membrane protrusion
    • DOI 10.1016/j.yexcr.2004.05.021, PII S0014482704003040
    • Franco S, Perrin B, Huttenlocher A. Isoform specific function of calpain 2 in regulating membrane protrusion. Exp Cell Res 2004;299:179-87 (Pubitemid 39078393)
    • (2004) Experimental Cell Research , vol.299 , Issue.1 , pp. 179-187
    • Franco, S.1    Perrin, B.2    Huttenlocher, A.3
  • 28
    • 0041633860 scopus 로고    scopus 로고
    • Calpain-2 as a target for limiting prostate cancer invasion
    • Mamoune A, Luo J, Lauffenburger DA, et al. Calpain-2 as a target for limiting prostate cancer invasion. Cancer Res 2003;63:4632-40 (Pubitemid 36951041)
    • (2003) Cancer Research , vol.63 , Issue.15 , pp. 4632-4640
    • Mamoune, A.1    Luo, J.-H.2    Lauffenburger, D.A.3    Wells, A.4
  • 30
    • 0038824666 scopus 로고    scopus 로고
    • The calpastatin-derived calpain inhibitor CP1B reduces mRNA expression of matrix metalloproteinase-2 and -9 and invasion by leukemic THP-1 cells
    • DOI 10.1515/BC.2003.107
    • Popp O, Heidinger M, Ruiz-Heinrich L, et al. The calpastatin-derived calpain inhibitor CP1B reduces mRNA expression of matrix metalloproteinase-2 and -9 and invasion by leukemic THP-1 cells. Biol Chem 2003;384:951-8 (Pubitemid 36874510)
    • (2003) Biological Chemistry , vol.384 , Issue.6 , pp. 951-958
    • Popp, O.1    Heidinger, M.2    Ruiz-Heinrich, L.3    Ries, C.4    Jochum, M.5    Gil-Parrado, S.6
  • 31
  • 33
    • 1642349839 scopus 로고    scopus 로고
    • Calpain activity is generally elevatedduring transformation but has oncogene-specific biological functions
    • Carragher NO, Fonseca BD, Frame MC. Calpain activity is generally elevatedduring transformation but has oncogene-specific biological functions. Neoplasia 2004;6:53-73 (Pubitemid 38391949)
    • (2004) Neoplasia , vol.6 , Issue.1 , pp. 53-73
    • Carragher, N.O.1    Fonseca, B.D.2    Frame, M.C.3
  • 34
    • 52049113458 scopus 로고    scopus 로고
    • Regulation of calpain activity by c-Myc through calpastatin and promotion of transformation in c-Myc-negative cells by calpastatin suppression
    • Niapour M, Yu Y, Berger SA. Regulation of calpain activity by c-Myc through calpastatin and promotion of transformation in c-Myc-negative cells by calpastatin suppression. J Biol Chem 2008;283:21371-81
    • (2008) J. Biol. Chem. , vol.283 , pp. 21371-21381
    • Niapour, M.1    Yu, Y.2    Berger, S.A.3
  • 35
    • 38349014100 scopus 로고    scopus 로고
    • Delineating v-Src downstream effector pathways in transformed myoblasts
    • Ciuffini L, Castellani L, Salvati E, et al. Delineating v-Src downstream effector pathways in transformed myoblasts. Oncogene 2008;27:528-39
    • (2008) Oncogene , vol.27 , pp. 528-539
    • Ciuffini, L.1    Castellani, L.2    Salvati, E.3
  • 37
    • 3242766866 scopus 로고    scopus 로고
    • 2+-mediated, calpain/caspase-12-dependent apoptosis in breast cancer cells
    • DOI 10.1016/j.bbrc.2004.06.173, PII S0006291X04014056
    • Sergeev IN. Genistein induces Ca2+-mediated, calpain/caspase-12- dependent apoptosis in breast cancer cells. Biochem Biophys Res Commun 2004;321:462-7 (Pubitemid 39055768)
    • (2004) Biochemical and Biophysical Research Communications , vol.321 , Issue.2 , pp. 462-467
    • Sergeev, I.N.1
  • 38
    • 78649960531 scopus 로고    scopus 로고
    • Calpain and caspase processing of caspase-12 contribute to the ER stress-induced cell death pathway in differentiated PC12 cells
    • Martinez JA, Zhang Z, Svetlov SI, et al. Calpain and caspase processing of caspase-12 contribute to the ER stress-induced cell death pathway in differentiated PC12 cells. Apoptosis 2010;15:1480-93
    • (2010) Apoptosis , vol.15 , pp. 1480-1493
    • Martinez, J.A.1    Zhang, Z.2    Svetlov, S.I.3
  • 39
    • 33744918550 scopus 로고    scopus 로고
    • Ubiquitous calpains promote caspase-12 and JNK activation during endoplasmic reticulum stress-induced apoptosis
    • DOI 10.1074/jbc.M601299200
    • Tan Y, Dourdin N, Wu C, et al. Ubiquitous calpains promote caspase-12 and JNK activation during endoplasmic reticulum stress-induced apoptosis. J Biol Chem 2006;281:16016-24 (Pubitemid 43848495)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.23 , pp. 16016-16024
    • Tan, Y.1    Dourdin, N.2    Wu, C.3    De Veyra, T.4    Elce, J.S.5    Greer, P.A.6
  • 40
    • 34548329748 scopus 로고    scopus 로고
    • Genistein-induced apoptosis of human breast cancer MCF-7 cells involves calpain-caspase and apoptosis signaling kinase 1-p38 mitogen-activated protein kinase activation cascades
    • DOI 10.1097/CAD.0b013e3280825573, PII 0000181320070700000004
    • Shim H, Park J, Paik H, et al. Genistein-induced apoptosis of human breast cancer MCF-7 cells involves calpain-caspase and apoptosis signaling kinase 1-p38 mitogen-activated protein kinase activation cascades. Anticancer Drugs 2007;18:649-57 (Pubitemid 47343657)
    • (2007) Anti-Cancer Drugs , vol.18 , Issue.6 , pp. 649-657
    • Shim, H.-Y.1    Park, J.-H.2    Paik, H.-D.3    Nah, S.-Y.4    Kim, D.S.H.L.5    Han, Y.S.6
  • 41
    • 33846879204 scopus 로고    scopus 로고
    • Genistein induces apoptosis in human hepatocellular carcinomas via interaction of endoplasmic reticulum stress and mitochondrial insult
    • DOI 10.1016/j.bcp.2006.11.027, PII S0006295206008021
    • Yeh T, Chiang P, Li T, et al. Genistein induces apoptosis in human hepatocellular carcinomas via interaction of endoplasmic reticulum stress and mitochondrial insult. Biochem Pharmacol 2007;73:782-92 (Pubitemid 46227339)
    • (2007) Biochemical Pharmacology , vol.73 , Issue.6 , pp. 782-792
    • Yeh, T.-C.1    Chiang, P.-C.2    Li, T.-K.3    Hsu, J.-L.4    Lin, C.-J.5    Wang, S.-W.6    Peng, C.-Y.7    Guh, J.-H.8
  • 42
    • 74549127500 scopus 로고    scopus 로고
    • Flavonoids activated caspases for apoptosis in human glioblastoma T98G and U87MG cells but not in human normal astrocytes
    • Das A, Banik NL, Ray SK. Flavonoids activated caspases for apoptosis in human glioblastoma T98G and U87MG cells but not in human normal astrocytes. Cancer 2010;116:164-76
    • (2010) Cancer , vol.116 , pp. 164-176
    • Das, A.1    Banik, N.L.2    Ray, S.K.3
  • 43
    • 36348997653 scopus 로고    scopus 로고
    • Mitochondria, calcium, and calpain are key mediators of resveratrol-induced apoptosis in breast cancer
    • DOI 10.1124/mol.107.039040
    • Sareen D, Darjatmoko SR, Albert DM, et al. Mitochondria, calcium, and calpain are key mediators of resveratrol-induced apoptosis in breast cancer. Mol Pharmacol 2007;72:1466-75 (Pubitemid 350146084)
    • (2007) Molecular Pharmacology , vol.72 , Issue.6 , pp. 1466-1475
    • Sareen, D.1    Darjatmoko, S.R.2    Albert, D.M.3    Polans, A.S.4
  • 44
    • 56049113988 scopus 로고    scopus 로고
    • HL-37 a novel anthracene derivative, induces Ca2+-mediated apoptosis in human breast cancer cells
    • Xie S, Zhang Z, Hu G, et al. HL-37, a novel anthracene derivative, induces Ca2+-mediated apoptosis in human breast cancer cells. Toxicology 2008;254:68-74
    • (2008) Toxicology , vol.254 , pp. 68-74
    • Xie, S.1    Zhang, Z.2    Hu, G.3
  • 45
    • 42149164851 scopus 로고    scopus 로고
    • Calpain-mediated pathway dominates cisplatin-induced apoptosis in human lung adenocarcinoma cells as determined by real-time single cell analysis
    • DOI 10.1002/ijc.23378
    • Liu L, Xing D, Chen WR, et al. Calpain-mediated pathway dominates cisplatin-induced apoptosis in human lung adenocarcinoma cells as determined by real-time single cell analysis. Int J Cancer 2008;122:2210-22 (Pubitemid 351542323)
    • (2008) International Journal of Cancer , vol.122 , Issue.10 , pp. 2210-2222
    • Liu, L.1    Xing, D.2    Chen, W.R.3    Chen, T.4    Pei, Y.5    Gao, X.6
  • 46
    • 72449209888 scopus 로고    scopus 로고
    • Micro-calpain regulates caspase-dependent and apoptosis inducing factor-mediated caspase-independent apoptotic pathways in cisplatin-induced apoptosis
    • Liu L, Xing D, Chen WR. Micro-calpain regulates caspase-dependent and apoptosis inducing factor-mediated caspase-independent apoptotic pathways in cisplatin-induced apoptosis. Int J Cancer 2009;125:2757-66
    • (2009) Int. J. Cancer , vol.125 , pp. 2757-2766
    • Liu, L.1    Xing, D.2    Chen, W.R.3
  • 47
    • 70350459849 scopus 로고    scopus 로고
    • Bid and calpains cooperate to trigger oxaliplatin-induced apoptosis of cervical carcinoma HeLa cells
    • Anguissola S, Kohler B, O'Byrne R, et al. Bid and calpains cooperate to trigger oxaliplatin-induced apoptosis of cervical carcinoma HeLa cells. Mol Pharmacol 2009;76:998-1010
    • (2009) Mol. Pharmacol. , vol.76 , pp. 998-1010
    • Anguissola, S.1    Kohler, B.2    O'Byrne, R.3
  • 48
    • 77954759427 scopus 로고    scopus 로고
    • Knockdown of napa using short-hairpin RNA sensitizes cancer cells to cisplatin: Implications to overcome chemoresistance
    • Wu Z, Chao CC. Knockdown of NAPA using short-hairpin RNA sensitizes cancer cells to cisplatin: implications to overcome chemoresistance. Biochem Pharmacol 2010;80:827-37
    • (2010) Biochem. Pharmacol. , vol.80 , pp. 827-837
    • Wu, Z.1    Chao, C.C.2
  • 49
    • 79951590040 scopus 로고    scopus 로고
    • Aspirin has antitumor effects via expression of calpain gene in cervical cancer cells
    • Lee SK, Park MS, Nam MJ. Aspirin has antitumor effects via expression of calpain gene in cervical cancer cells. J Oncol 2008;2008:285374
    • (2008) J. Oncol. 2008 , pp. 285374
    • Lee, S.K.1    Park, M.S.2    Nam, M.J.3
  • 50
    • 33748433166 scopus 로고    scopus 로고
    • Curcumin activated both receptor-mediated and mitochondria-mediated proteolytic pathways for apoptosis in human glioblastoma T98G cells
    • DOI 10.1016/j.neulet.2006.08.013, PII S0304394006008044
    • Karmakar S, Banik NL, Patel SJ, et al. Curcumin activated both receptor-mediated and mitochondria-mediated proteolytic pathways for apoptosis in human glioblastoma T98G cells. Neurosci Lett 2006;407:53-8 (Pubitemid 44345016)
    • (2006) Neuroscience Letters , vol.407 , Issue.1 , pp. 53-58
    • Karmakar, S.1    Banik, N.L.2    Patel, S.J.3    Ray, S.K.4
  • 51
    • 35848949333 scopus 로고    scopus 로고
    • Curcumin suppressed anti-apoptotic signals and activated cysteine proteases for apoptosis in human malignant glioblastoma U87MG cells
    • DOI 10.1007/s11064-007-9376-z
    • Karmakar S, Banik NL, Ray SK. Curcumin suppressed anti-apoptotic signals and activated cysteine proteases for apoptosis in human malignant glioblastoma U87MG cells. Neurochem Res 2007;32:2103-13 (Pubitemid 350059854)
    • (2007) Neurochemical Research , vol.32 , Issue.12 , pp. 2103-2113
    • Karmakar, S.1    Banik, N.L.2    Ray, S.K.3
  • 52
    • 77949266488 scopus 로고    scopus 로고
    • Calpain regulates sensitivity to trastuzumab and survival in HER2-positive breast cancer
    • Kulkarni S, Reddy KB, Esteva FJ, et al. Calpain regulates sensitivity to trastuzumab and survival in HER2-positive breast cancer. Oncogene 2010;29:1339-50
    • (2010) Oncogene , vol.29 , pp. 1339-1350
    • Kulkarni, S.1    Reddy, K.B.2    Esteva, F.J.3
  • 53
    • 77952340703 scopus 로고    scopus 로고
    • Proteasome inhibitor PS-341 bortezomib induces calpain-dependent ikappabalpha degradation
    • Li C, Chen S, Yue P, et al. Proteasome inhibitor PS-341 (bortezomib) induces calpain-dependent IkappaBalpha degradation. J Biol Chem 2010;285:16096-104
    • (2010) J. Biol. Chem. , vol.285 , pp. 16096-16104
    • Li, C.1    Chen, S.2    Yue, P.3
  • 55
    • 0036229049 scopus 로고    scopus 로고
    • Motility is rate-limiting for invasion of bladder carcinoma cell lines
    • DOI 10.1016/S1357-2725(01)00173-X, PII S135727250100173X
    • Kassis J, Radinsky R, Wells A. Motility is rate-limiting for invasion of bladder carcinoma cell lines. Int J Biochem Cell Biol 2002;34:762-75 (Pubitemid 34304166)
    • (2002) International Journal of Biochemistry and Cell Biology , vol.34 , Issue.7 , pp. 762-775
    • Kassis, J.1    Radinsky, R.2    Wells, A.3
  • 56
    • 0029820264 scopus 로고    scopus 로고
    • Modulation of cell migration by integrin-mediated cytoskeletal linkages and ligand-binding affinity
    • Huttenlocher A, Ginsberg MH, Horwitz AF. Modulation of cell migration by integrin-mediated cytoskeletal linkages and ligand-binding affinity. J Cell Biol 1996;134:1551-62 (Pubitemid 26318026)
    • (1996) Journal of Cell Biology , vol.134 , Issue.6 , pp. 1551-1562
    • Huttenlocher, A.1    Ginsberg, M.H.2    Horwitz, A.F.3
  • 57
    • 0035930548 scopus 로고    scopus 로고
    • Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts
    • Dourdin N, Bhatt AK, Dutt P, et al. Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts. J Biol Chem 2001;276:48382-8
    • (2001) J. Biol. Chem. , vol.276 , pp. 48382-48388
    • Dourdin, N.1    Bhatt, A.K.2    Dutt, P.3
  • 58
    • 33645319035 scopus 로고    scopus 로고
    • IP-10 blocks vascular endothelial growth factor-induced endothelial cell motility and tube formation via inhibition of calpain
    • Bodnar RJ, Yates CC, Wells A. IP-10 blocks vascular endothelial growth factor-induced endothelial cell motility and tube formation via inhibition of calpain. Circ Res 2006;98:617-25
    • (2006) Circ. Res. , vol.98 , pp. 617-625
    • Bodnar, R.J.1    Yates, C.C.2    Wells, A.3
  • 59
    • 33746491305 scopus 로고    scopus 로고
    • Calpain-2 regulation of VEGF-mediated angiogenesis
    • DOI 10.1096/fj.05-5354com
    • Su Y, Cui Z, Li Z, et al. Calpain-2 regulation of VEGF-mediated angiogenesis. FASEB J 2006;20:1443-51 (Pubitemid 44943852)
    • (2006) FASEB Journal , vol.20 , Issue.9 , pp. 1443-1451
    • Su, Y.1    Cui, Z.2    Li, Z.3    Block, E.R.4
  • 60
    • 14044252859 scopus 로고    scopus 로고
    • Interferon-inducible protein 9 (CXCL11)-induced cell motility in keratinocytes requires calcium flux-dependent activation of μ-Calpain
    • DOI 10.1128/MCB.25.5.1922-1941.2005
    • Satish L, Blair HC, Glading A, et al. Interferon-inducible protein 9 (CXCL11)-induced cell motility in keratinocytes requires calcium flux-dependent activation of mu-calpain. Mol Cell Biol 2005;25:1922-41 (Pubitemid 40280155)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.5 , pp. 1922-1941
    • Satish, L.1    Blair, H.C.2    Glading, A.3    Wells, A.4
  • 61
  • 63
    • 0034723310 scopus 로고    scopus 로고
    • Epidermal growth factor receptor activation of calpain is required for fibroblast motility and occurs via an ERK/MAP kinase signaling pathway
    • DOI 10.1074/jbc.275.4.2390
    • Glading A, Chang P, Lauffenburger DA, et al. Epidermal growth factor receptor activation of calpain is required for fibroblast motility and occurs via an ERK/MAP kinase signaling pathway. J Biol Chem 2000;275:2390-8 (Pubitemid 30081997)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.4 , pp. 2390-2398
    • Glading, A.1    Chang, P.2    Lauffenburger, D.A.3    Wells, A.4
  • 65
    • 11144227597 scopus 로고    scopus 로고
    • Tobacco-specific nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1- butanone induces phosphorylation of μ- and m-calpain in association with increased secretion, cell migration, and invasion
    • DOI 10.1074/jbc.M409889200
    • Xu L, Deng X. Tobacco-specific nitrosamine 4-(methylnitrosamino)-1-(3- pyridyl)-1-butanone induces phosphorylation of μ- and m-calpain in association with increased secretion, cell migration, and invasion. J Biol Chem 2004;279:53683-90 (Pubitemid 40051876)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.51 , pp. 53683-53690
    • Xu, L.1    Deng, X.2
  • 66
    • 33644620310 scopus 로고    scopus 로고
    • Protein kinase Cι promotes nicotine-induced migration and invasion of cancer cells via phosphorylation of μ- and m-calpains
    • DOI 10.1074/jbc.M510721200
    • Xu L, Deng X. Protein kinase Ci promotes nicotine-induced migration and invasion of cancer cells via phosphorylation of mu- and m-calpains. J Biol Chem 2006;281:4457-66 (Pubitemid 43847877)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.7 , pp. 4457-4466
    • Xu, L.1    Deng, X.2
  • 67
    • 67650588774 scopus 로고    scopus 로고
    • Characterisation of fibronectin-mediated FAK signalling pathways in lung cancer cell migration and invasion
    • Meng XN, Jin Y, Yu Y, et al. Characterisation of fibronectin-mediated FAK signalling pathways in lung cancer cell migration and invasion. Br J Cancer 2009;101:327-34
    • (2009) Br. J. Cancer , vol.101 , pp. 327-334
    • Meng, X.N.1    Jin, Y.2    Yu, Y.3
  • 68
    • 77952892154 scopus 로고    scopus 로고
    • Calpains: Markers of tumor aggressiveness
    • Roumes H, Leloup L, Dargelos E, et al. Calpains: markers of tumor aggressiveness? Exp Cell Res 2010;316:1587-99
    • (2010) Exp. Cell Res. , Issue.316 , pp. 1587-1599
    • Roumes, H.1    Leloup, L.2    Dargelos, E.3
  • 70
    • 71549169276 scopus 로고    scopus 로고
    • Silencing of calpain expression reduces the metastatic potential of human osteosarcoma cells
    • Fan D, Dai J, Tang J, et al. Silencing of calpain expression reduces the metastatic potential of human osteosarcoma cells. Cell Biol Int 2009;33:1263-7
    • (2009) Cell Biol. Int. , vol.33 , pp. 1263-1267
    • Fan, D.1    Dai, J.2    Tang, J.3
  • 72
    • 33845947971 scopus 로고    scopus 로고
    • Suppression of cancer cell migration and invasion by protein phosphatase 2A through dephosphorylation of μ- and m-calpains
    • DOI 10.1074/jbc.M607702200
    • Xu L, Deng X. Suppression of cancer cell migration and invasion by protein phosphatase 2A through dephosphorylation of mu- and m-calpains. J Biol Chem 2006;281:35567-75 (Pubitemid 46036590)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.46 , pp. 35567-35575
    • Xu, L.1    Deng, X.2
  • 73
    • 33748948921 scopus 로고    scopus 로고
    • Calpain 2 and Src dependence distinguishes mesenchymal and amoeboid modes of tumour cell invasion: A link to integrin function
    • DOI 10.1038/sj.onc.1209582, PII 1209582
    • Carragher NO, Walker SM, Scott Carragher LA, et al. Calpain 2 and Src dependence distinguishes mesenchymal and amoeboid modes of tumour cell invasion: a link to integrin function. Oncogene 2006;25:5726-40 (Pubitemid 44435250)
    • (2006) Oncogene , vol.25 , Issue.42 , pp. 5726-5740
    • Carragher, N.O.1    Walker, S.M.2    Carragher, L.A.S.3    Harris, F.4    Sawyer, T.K.5    Brunton, V.G.6    Ozanne, B.W.7    Frame, M.C.8
  • 74
    • 0028846008 scopus 로고
    • VEGF-mediated tumour angiogenesis: A new target for cancer therapy
    • Martiny-Baron G, Marme D. VEGF-mediated tumour angiogenesis: a new target for cancer therapy. Curr Opin Biotechnol 1995;6:675-80
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 675-680
    • Martiny-Baron, G.1    Marme, D.2
  • 76
    • 79551521053 scopus 로고    scopus 로고
    • Phase III trial assessing bevacizumab in stages II and III carcinoma of the colon: Results of nsabp protocol C-08
    • Allegra CJ, Yothers G, O'Connell MJ, et al. Phase III trial assessing bevacizumab in stages II and III carcinoma of the colon: results of NSABP protocol C-08. J Clin Oncol 2011;29:11-16
    • (2011) J. Clin Oncol. , Issue.29 , pp. 11-16
    • Allegra, C.J.1    Yothers, G.2    O'Connell, M.J.3
  • 77
    • 68949181600 scopus 로고    scopus 로고
    • IP-10 induces dissociation of newly formed blood vessels
    • Bodnar RJ, Yates CC, Rodgers ME, et al. IP-10 induces dissociation of newly formed blood vessels. J Cell Sci 2009;122:2064-77
    • (2009) J. Cell Sci. , vol.122 , pp. 2064-2077
    • Bodnar, R.J.1    Yates, C.C.2    Rodgers, M.E.3
  • 78
    • 0036207773 scopus 로고    scopus 로고
    • Activation of m-calpain (calpain II) by epidermal growth factor is limited by protein kinase A phosphorylation of m-calpain
    • DOI 10.1128/MCB.22.8.2716-2727.2002
    • Shiraha H, Glading A, Chou J, et al. Activation of m-calpain (calpain II) by epidermal growth factor is limited by protein kinase A phosphorylation of m-calpain. Mol Cell Biol 2002;22:2716-27 (Pubitemid 34262992)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.8 , pp. 2716-2727
    • Shiraha, H.1    Glading, A.2    Chou, J.3    Jia, Z.4    Wells, A.5
  • 81
    • 66749173427 scopus 로고    scopus 로고
    • Novel variants of muscle calpain 3 identified in human melanoma cells: Cisplatin-induced changes in vitro and differential expression in melanocytic lesions
    • Moretti D, Del Bello B, Cosci E, et al. Novel variants of muscle calpain 3 identified in human melanoma cells: cisplatin-induced changes in vitro and differential expression in melanocytic lesions. Carcinogenesis 2009;30:960-7
    • (2009) Carcinogenesis , vol.30 , pp. 960-967
    • Moretti, D.1    Del Bello, B.2    Cosci, E.3
  • 82
    • 77956411752 scopus 로고    scopus 로고
    • Calpain3 is expressed in a proteolitically active form in papillomavirus-associated urothelial tumors of the urinary bladder in cattle
    • Roperto S, De Tullio R, Raso C, et al. Calpain3 is expressed in a proteolitically active form in papillomavirus-associated urothelial tumors of the urinary bladder in cattle. PLoS ONE 2010;5:e10299
    • (2010) PLoS One , vol.5
    • Roperto, S.1    De Tullio, R.2    Raso, C.3
  • 83
    • 43849092147 scopus 로고    scopus 로고
    • Increased expression of calpain 6 during the progression of uterine cervical neoplasia: Immunohistochemical analysis
    • Lee S, Kim B, Choi Y, et al. Increased expression of calpain 6 during the progression of uterine cervical neoplasia: immunohistochemical analysis. Oncol Rep 2008;19:859-63 (Pubitemid 351802652)
    • (2008) Oncology Reports , vol.19 , Issue.4 , pp. 859-863
    • Lee, S.-J.1    Kim, B.-G.2    Choi, Y.-L.3    Lee, J.-W.4
  • 84
    • 53449095522 scopus 로고    scopus 로고
    • Calpain 6 supports tumorigenesis by inhibiting apoptosis and facilitating angiogenesis
    • Rho SB, Byun H, Park S, et al. Calpain 6 supports tumorigenesis by inhibiting apoptosis and facilitating angiogenesis. Cancer Lett 2008;271:306-13
    • (2008) Cancer Lett. , vol.271 , pp. 306-313
    • Rho, S.B.1    Byun, H.2    Park, S.3
  • 86
    • 0034613338 scopus 로고    scopus 로고
    • Antisense RNA-mediated deficiency of the calpain protease nCL-4 in NIH3T3 cells is associated with neoplastic transformation and tumorigenesis
    • Liu K, Li L, Cohen SN. Antisense RNA-mediated deficiency of the calpain protease, nCL-4, in NIH3T3 cells is associated with neoplastic transformation and tumorigenesis. J Biol Chem 2000;275:31093-8
    • (2000) J. Biol. Chem. , vol.275 , pp. 31093-31098
    • Liu, K.1    Li, L.2    Cohen, S.N.3
  • 87
    • 0002198460 scopus 로고    scopus 로고
    • Ca2+-dependent neutral protease calpain activity in breast cancer tissue and estrogen receptor status
    • Shiba E, Kambayashi JI, Sakon M, et al. Ca2+-dependent neutral protease (calpain) activity in breast cancer tissue and estrogen receptor status. Breast Cancer 1996;3:13-17
    • (1996) Breast Cancer , vol.3 , pp. 13-17
    • Shiba, E.1    Kambayashi, J.I.2    Sakon, M.3
  • 89
    • 13644254921 scopus 로고    scopus 로고
    • Dexamethasone protected human glioblastoma U87MG cells from temozolomide induced apoptosis by maintaining Bax:Bcl-2 ratio and preventing proteolytic activities
    • Das A, Banik NL, Patel SJ, et al. Dexamethasone protected human glioblastoma U87MG cells from temozolomide induced apoptosis by maintaining Bax:Bcl-2 ratio and preventing proteolytic activities. Mol Cancer 2004;3:36
    • (2004) Mol. Cancer , vol.3 , pp. 36
    • Das, A.1    Banik, N.L.2    Patel, S.J.3
  • 91
    • 0345701372 scopus 로고    scopus 로고
    • Different expression patterns of calpain isozymes 1 and 2 (CAPN1 and 2) in squamous cell carcinomas (SCC) and basal cell carcinomas (BCC) of human skin
    • DOI 10.1002/path.1308
    • Reichrath J, Welter C, Mitschele T, et al. Different expression patterns of calpain isozymes 1 and 2 (CAPN1 and 2) in squamous cell carcinomas (SCC) and basal cell carcinomas (BCC) of human skin. J Pathol 2003;199:509-16 (Pubitemid 36411228)
    • (2003) Journal of Pathology , vol.199 , Issue.4 , pp. 509-516
    • Reichrath, J.1    Welter, C.2    Mitschele, T.3    Classen, U.4    Meineke, V.5    Tilgen, W.6    Seifert, M.7
  • 92
    • 0032913644 scopus 로고    scopus 로고
    • Expression of calpain I messenger RNA in human renal cell carcinoma: Correlation with lymph node metastasis and histological type
    • DOI 10.1002/(SICI)1097-0215(1999 0219)84:1<6::AID-IJC2>3.0.CO;2-T
    • Braun C, Engel M, Seifert M, et al. Expression of calpain I messenger RNA in human renal cell carcinoma: correlation with lymph node metastasis and histological type. Int J Cancer 1999;84:6-9 (Pubitemid 29059100)
    • (1999) International Journal of Cancer , vol.84 , Issue.1 , pp. 6-9
    • Braun, C.1    Engel, M.2    Seifert, M.3    Theisinger, B.4    Seitz, G.5    Zang, K.D.6    Welter, C.7
  • 93
    • 0141941738 scopus 로고    scopus 로고
    • Association of mitochondrial calpain activation with increased expression and autolysis of calpain small subunit in an early stage of apoptosis
    • Daniel KG, Anderson JS, Zhong Q, et al. Association of mitochondrial calpain activation with increased expression and autolysis of calpain small subunit in an early stage of apoptosis. Int J Mol Med 2003;12:247-52
    • (2003) Int. J. Mol. Med. , vol.12 , pp. 247-252
    • Daniel, K.G.1    Anderson, J.S.2    Zhong, Q.3
  • 94
    • 61949430429 scopus 로고    scopus 로고
    • Capn4 overexpression underlies tumor invasion and metastasis after liver transplantation for hepatocellular carcinoma
    • Bai D, Dai Z, Zhou J, et al. Capn4 overexpression underlies tumor invasion and metastasis after liver transplantation for hepatocellular carcinoma. Hepatology 2009;49:460-70
    • (2009) Hepatology , vol.49 , pp. 460-470
    • Bai, D.1    Dai, Z.2    Zhou, J.3
  • 95
    • 0037865469 scopus 로고    scopus 로고
    • Constitutive expression of cytotoxic proteases and down-regulation of protease inhibitors in LGL leukemia
    • Kothapalli R, Bailey RD, Kusmartseva I, et al. Constitutive expression of cytotoxic proteases and down-regulation of protease inhibitors in LGL leukemia. Int J Oncol 2003;22:33-9
    • (2003) Int. J. Oncol. , vol.22 , pp. 33-39
    • Kothapalli, R.1    Bailey, R.D.2    Kusmartseva, I.3
  • 96
    • 77955811866 scopus 로고    scopus 로고
    • Immunhistochemical analysis for expression of calpain 1 calpain 2 and calpastatin in endometrial cancer
    • Salehin D, Fromberg I, Haugk C, et al. Immunhistochemical analysis for expression of calpain 1, calpain 2 and calpastatin in endometrial cancer. Anticancer Res 2010;30:2837-43
    • (2010) Anticancer Res. , vol.30 , pp. 2837-2843
    • Salehin, D.1    Fromberg, I.2    Haugk, C.3
  • 97
    • 37449017847 scopus 로고    scopus 로고
    • CAPN10 alleles modify laryngeal cancer risk in the Spanish population
    • Esteban F, Royo JL, Gonzalez-Moles MA, et al. CAPN10 alleles modify laryngeal cancer risk in the Spanish population. Eur J Surg Oncol 2008;34:94-9
    • (2008) Eur. J. Surg. Oncol. , vol.34 , pp. 94-99
    • Esteban, F.1    Royo, J.L.2    Gonzalez-Moles, M.A.3
  • 98
    • 33750080428 scopus 로고    scopus 로고
    • Calpain activation is required for glutamate-induced p27 down-regulation in cultured cortical neurons
    • DOI 10.1111/j.1471-4159.2006.04100.x
    • Akashiba H, Matsuki N, Nishiyama N. Calpain activation is required for glutamate-induced p27 down-regulation in cultured cortical neurons. J Neurochem 2006;99:733-44 (Pubitemid 44583433)
    • (2006) Journal of Neurochemistry , vol.99 , Issue.3 , pp. 733-744
    • Akashiba, H.1    Matsuki, N.2    Nishiyama, N.3
  • 100
    • 67449132347 scopus 로고    scopus 로고
    • Calpain-mediated activation of NO synthase in human neuroblastoma SK-N-BE cells
    • Averna M, Stifanese R, De Tullio R, et al. Calpain-mediated activation of NO synthase in human neuroblastoma SK-N-BE cells. J Neurochem 2009;110:412-21
    • (2009) J. Neurochem. , vol.110 , pp. 412-421
    • Averna, M.1    Stifanese, R.2    De Tullio, R.3
  • 101
    • 77449111847 scopus 로고    scopus 로고
    • Role of calpain-9 and PKC-delta in the apoptotic mechanism of lumen formation in CEACAM1 transfected breast epithelial cells
    • Chen C, Nguyen T, Shively JE. Role of calpain-9 and PKC-delta in the apoptotic mechanism of lumen formation in CEACAM1 transfected breast epithelial cells. Exp Cell Res 2010;316:638-48
    • (2010) Exp. Cell Res. , vol.316 , pp. 638-648
    • Chen, C.1    Nguyen, T.2    Shively, J.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.