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Volumn 6, Issue 1, 2004, Pages 53-73

Calpain Activity Is Generally Elevated during Transformation but Has Oncogene-Specific Biological Functions

Author keywords

Apoptosis; Calpain; Focal adhesion; Migration; Oncogene

Indexed keywords

ACTIN; CALPAIN; FOCAL ADHESION KINASE; K RAS PROTEIN; MYC PROTEIN; ONCOPROTEIN; PROTEIN V FOS; PROTEIN V JUN; PROTEIN V SRC; SPECTRIN; TALIN; UNCLASSIFIED DRUG; V MYC PROTEIN;

EID: 1642349839     PISSN: 15228002     EISSN: None     Source Type: Journal    
DOI: 10.1016/s1476-5586(04)80053-8     Document Type: Article
Times cited : (63)

References (84)
  • 1
    • 0038057187 scopus 로고
    • Endogenous inhibitor for calcium-dependent cysteine protease contains four internal repeats that could be responsible for its multiple reactive sites
    • Emori Y, Kawasaki H, Imajoh S, Imahori K, and Suzuki K (1987). Endogenous inhibitor for calcium-dependent cysteine protease contains four internal repeats that could be responsible for its multiple reactive sites. Proc Natl Acad Sci USA 84, 3590-3594.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3590-3594
    • Emori, Y.1    Kawasaki, H.2    Imajoh, S.3    Imahori, K.4    Suzuki, K.5
  • 2
    • 0024844775 scopus 로고
    • Inhibition of calpain by a synthetic oligopeptide corresponding to an exon of the human calpastatin gene
    • Maki M, Bagci H, Hamaguchi K, Ueda M, Murachi T, and Hatanaka M (1989). Inhibition of calpain by a synthetic oligopeptide corresponding to an exon of the human calpastatin gene. J Biol Chem 264, 18866-18869.
    • (1989) J Biol Chem , vol.264 , pp. 18866-18869
    • Maki, M.1    Bagci, H.2    Hamaguchi, K.3    Ueda, M.4    Murachi, T.5    Hatanaka, M.6
  • 3
    • 0024346641 scopus 로고
    • Identification and characterization of inhibitory sequences in four repeating domains of the endogenous inhibitor for calcium-dependent protease
    • Kawasaki H, Emori Y, Imajoh-Ohmi S, Minami Y, and Suzuki K (1989). Identification and characterization of inhibitory sequences in four repeating domains of the endogenous inhibitor for calcium-dependent protease. J Biochem (Tokyo) 106, 274-281.
    • (1989) J Biochem (Tokyo) , vol.106 , pp. 274-281
    • Kawasaki, H.1    Emori, Y.2    Imajoh-Ohmi, S.3    Minami, Y.4    Suzuki, K.5
  • 4
    • 0035830903 scopus 로고    scopus 로고
    • Cleavage of focal adhesion kinase by different proteases during SRC-regulated transformation and apoptosis. Distinct roles for calpain and caspases
    • Carragher NO, Fincham VJ, Riley D, and Frame MC (2001). Cleavage of focal adhesion kinase by different proteases during SRC-regulated transformation and apoptosis. Distinct roles for calpain and caspases. J Biol Chem 276, 4270-4275.
    • (2001) J Biol Chem , vol.276 , pp. 4270-4275
    • Carragher, N.O.1    Fincham, V.J.2    Riley, D.3    Frame, M.C.4
  • 6
    • 0031570762 scopus 로고    scopus 로고
    • The calpain-calpastatin system and cellular proliferation and differentiation in rodent osteoblastic cells
    • Murray SS, Grisanti MS, Bentley GV, Kahn AJ, Urist MR, and Murray EJ (1997). The calpain-calpastatin system and cellular proliferation and differentiation in rodent osteoblastic cells. Exp Cell Res 233, 297-309.
    • (1997) Exp Cell Res , vol.233 , pp. 297-309
    • Murray, S.S.1    Grisanti, M.S.2    Bentley, G.V.3    Kahn, A.J.4    Urist, M.R.5    Murray, E.J.6
  • 7
    • 0034698878 scopus 로고    scopus 로고
    • Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis
    • Nakagawa T and Yuan J (2000). Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. J Cell Biol 150, 887-894.
    • (2000) J Cell Biol , vol.150 , pp. 887-894
    • Nakagawa, T.1    Yuan, J.2
  • 8
    • 0034625418 scopus 로고    scopus 로고
    • Mitotic clonal expansion during pre-adipocyte differentiation: Calpain-mediated turnover of p27
    • Patel YM and Lane MD (2000). Mitotic clonal expansion during pre-adipocyte differentiation: calpain-mediated turnover of p27. J Biol Chem 275, 17653-17660.
    • (2000) J Biol Chem , vol.275 , pp. 17653-17660
    • Patel, Y.M.1    Lane, M.D.2
  • 9
    • 0031452173 scopus 로고    scopus 로고
    • Structure and physiological function of calpains
    • Sorimachi H, Ishiura S, and Suzuki K (1997). Structure and physiological function of calpains. Biochem J 328, 721-732.
    • (1997) Biochem J , vol.328 , pp. 721-732
    • Sorimachi, H.1    Ishiura, S.2    Suzuki, K.3
  • 10
    • 0023661249 scopus 로고
    • Colocalization of calcium-dependent protease II and one of its substrates at sites of cell adhesion
    • Beckerle MC, Burridge K, DeMartino GN, and Croall DE (1987). Colocalization of calcium-dependent protease II and one of its substrates at sites of cell adhesion. Cell 51, 569-577.
    • (1987) Cell , vol.51 , pp. 569-577
    • Beckerle, M.C.1    Burridge, K.2    DeMartino, G.N.3    Croall, D.E.4
  • 11
    • 0034734992 scopus 로고    scopus 로고
    • Evidence that beta3 integrin-induced Rac activation involves the calpain-dependent formation of integrin clusters that are distinct from the focal complexes and focal adhesions that form as Rac and RhoA become active
    • Bialkowska K, Kulkarni S, Du X, Goll DE, Saido TC, and Fox JE (2000). Evidence that beta3 integrin-induced Rac activation involves the calpain-dependent formation of integrin clusters that are distinct from the focal complexes and focal adhesions that form as Rac and RhoA become active. J Cell Biol 151, 685-696.
    • (2000) J Cell Biol , vol.151 , pp. 685-696
    • Bialkowska, K.1    Kulkarni, S.2    Du, X.3    Goll, D.E.4    Saido, T.C.5    Fox, J.E.6
  • 12
    • 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, Greer PA, Arthur JS, Elce JS, and Huttenlocher A (2001). Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts. J Biol Chem 276, 48382-48388.
    • (2001) J Biol Chem , vol.276 , pp. 48382-48388
    • Dourdin, N.1    Bhatt, A.K.2    Dutt, P.3    Greer, P.A.4    Arthur, J.S.5    Elce, J.S.6    Huttenlocher, A.7
  • 13
    • 0036711804 scopus 로고    scopus 로고
    • Regulation of focal complex composition and disassembly by the calcium-dependent protease calpain
    • Bhatt A, Kaverina I, Otey C, and Huttenlocher A (2002). Regulation of focal complex composition and disassembly by the calcium-dependent protease calpain. J Cell Sci 115, 3415-3425.
    • (2002) J Cell Sci , vol.115 , pp. 3415-3425
    • Bhatt, A.1    Kaverina, I.2    Otey, C.3    Huttenlocher, A.4
  • 15
    • 0025955448 scopus 로고
    • In vitro proteolysis of brain spectrin by calpain I inhibits association of spectrin with ankyrin-independent membrane binding site(s)
    • Hu RJ and Bennett V (1991). In vitro proteolysis of brain spectrin by calpain I inhibits association of spectrin with ankyrin-independent membrane binding site(s). J Biol Chem 266, 18200-18205.
    • (1991) J Biol Chem , vol.266 , pp. 18200-18205
    • Hu, R.J.1    Bennett, V.2
  • 17
    • 0037025350 scopus 로고    scopus 로고
    • Calpain cleaves RhoA generating a dominant-negative form that inhibits integrin-induced actin filament assembly and cell spreading
    • Kulkarni S, Goll DE, and Fox JE (2002). Calpain cleaves RhoA generating a dominant-negative form that inhibits integrin-induced actin filament assembly and cell spreading. J Biol Chem 277, 24435-24441.
    • (2002) J Biol Chem , vol.277 , pp. 24435-24441
    • Kulkarni, S.1    Goll, D.E.2    Fox, J.E.3
  • 18
  • 19
    • 0025900722 scopus 로고
    • Degradation of transcription factors, c-Jun and c-Fos, by calpain
    • Hirai S, Kawasaki H, Yaniv M, and Suzuki K (1991). Degradation of transcription factors, c-Jun and c-Fos, by calpain. FEBS Lett 287, 57-61.
    • (1991) FEBS Lett , vol.287 , pp. 57-61
    • Hirai, S.1    Kawasaki, H.2    Yaniv, M.3    Suzuki, K.4
  • 21
    • 0027258640 scopus 로고
    • pp60src is an endogenous substrate for calpain in human blood platelets
    • Oda A, Druker BJ, Ariyoshi H, Smith M, and Salzman EW (1993). pp60src is an endogenous substrate for calpain in human blood platelets. J Biol Chem 268, 12603-12608.
    • (1993) J Biol Chem , vol.268 , pp. 12603-12608
    • Oda, A.1    Druker, B.J.2    Ariyoshi, H.3    Smith, M.4    Salzman, E.W.5
  • 22
    • 0024326801 scopus 로고
    • Specific proteolysis of the c-mos proto-oncogene product by calpain on fertilization of Xenopus eggs
    • Watanabe N, Vande Woude GF, Ikawa Y, and Sagata N (1989). Specific proteolysis of the c-mos proto-oncogene product by calpain on fertilization of Xenopus eggs. Nature 342, 505-511.
    • (1989) Nature , vol.342 , pp. 505-511
    • Watanabe, N.1    Vande Woude, G.F.2    Ikawa, Y.3    Sagata, N.4
  • 23
    • 0027990307 scopus 로고
    • The calpain cleavage sites in the epidermal growth factor receptor kinase domain
    • Gregoriou M, Willis AC, Pearson MA, and Crawford C (1994). The calpain cleavage sites in the epidermal growth factor receptor kinase domain. Eur J Biochem 223, 455-464.
    • (1994) Eur J Biochem , vol.223 , pp. 455-464
    • Gregoriou, M.1    Willis, A.C.2    Pearson, M.A.3    Crawford, C.4
  • 24
  • 25
    • 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, and Cohen SN (2000). Antisense RNA-mediated deficiency of the calpain protease, nCL-4, in NIH3T3 cells is associated with neoplastic transformation and tumorigenesis. J Biol Chem 275, 31093-31098.
    • (2000) J Biol Chem , vol.275 , pp. 31093-31098
    • Liu, K.1    Li, L.2    Cohen, S.N.3
  • 26
    • 0031014946 scopus 로고    scopus 로고
    • Proteolytic cleavage of human p53 by calpain: A potential regulator of protein stability
    • Kubbutat MH and Vousden KH (1997). Proteolytic cleavage of human p53 by calpain: a potential regulator of protein stability. Mol Cell Biol 17, 460-468.
    • (1997) Mol Cell Biol , vol.17 , pp. 460-468
    • Kubbutat, M.H.1    Vousden, K.H.2
  • 27
    • 0034426280 scopus 로고    scopus 로고
    • Calpain-dependent proteolysis of NF2 protein: Involvement in schwannomas and meningiomas
    • Kimura Y, Saya H, and Nakao M (2000). Calpain-dependent proteolysis of NF2 protein: involvement in schwannomas and meningiomas. Neuropathology 20, 153-160.
    • (2000) Neuropathology , vol.20 , pp. 153-160
    • Kimura, Y.1    Saya, H.2    Nakao, M.3
  • 28
    • 0031594708 scopus 로고    scopus 로고
    • Novel IkappaB alpha proteolytic pathway in WEHI231 immature B cells
    • Miyamoto S, Seufzer BJ, and Shumway SD (1998). Novel IkappaB alpha proteolytic pathway in WEHI231 immature B cells. Mol Cell Biol 18, 19-29.
    • (1998) Mol Cell Biol , vol.18 , pp. 19-29
    • Miyamoto, S.1    Seufzer, B.J.2    Shumway, S.D.3
  • 31
    • 0036887581 scopus 로고    scopus 로고
    • Calpain: A role in cell transformation and migration
    • Carragher NO and Frame MC (2002). Calpain: a role in cell transformation and migration. Int J Biochem Cell Biol 34, 1539-1543.
    • (2002) Int J Biochem Cell Biol , vol.34 , pp. 1539-1543
    • Carragher, N.O.1    Frame, M.C.2
  • 33
    • 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
    • Glading A, Chang P, Lauffenburger DA, and Wells A (2000). Epidermal growth factor receptor activation of calpain is required for fibroblast motility and occurs via an ERK/MAP kinase signaling pathway. J Biol Chem 275, 2390-2398.
    • (2000) J Biol Chem , vol.275 , pp. 2390-2398
    • Glading, A.1    Chang, P.2    Lauffenburger, D.A.3    Wells, A.4
  • 34
    • 0037112514 scopus 로고    scopus 로고
    • Protein kinase CK2 promotes aberrant activation of nuclear factor-kappaB, transformed phenotype, and survival of breast cancer cells
    • Romieu-Mourez R, Landesman-Bollag E, Seldin DC, and Sonenshein GE (2002). Protein kinase CK2 promotes aberrant activation of nuclear factor-kappaB, transformed phenotype, and survival of breast cancer cells. Cancer Res 62, 6770-6778.
    • (2002) Cancer Res , vol.62 , pp. 6770-6778
    • Romieu-Mourez, R.1    Landesman-Bollag, E.2    Seldin, D.C.3    Sonenshein, G.E.4
  • 35
    • 0041633860 scopus 로고    scopus 로고
    • Calpain-2 as a target for limiting prostate cancer invasion
    • Mamoune A, Luo JH, Lauffenburger DA, and Wells A (2003). Calpain-2 as a target for limiting prostate cancer invasion. Cancer Res 63, 4632-4640.
    • (2003) Cancer Res , vol.63 , pp. 4632-4640
    • Mamoune, A.1    Luo, J.H.2    Lauffenburger, D.A.3    Wells, A.4
  • 36
    • 0032913644 scopus 로고    scopus 로고
    • Expression of calpain I messenger RNA in human renal cell carcinoma: Correlation with lymph node metastasis and histological type
    • Braun C, Engel M, Seifert M, Theisinger B, Seitz G, Zang KD, and Welter C (1999). Expression of calpain I messenger RNA in human renal cell carcinoma: correlation with lymph node metastasis and histological type. Int J Cancer 84, 6-9.
    • (1999) Int J Cancer , vol.84 , 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
  • 38
    • 0037421967 scopus 로고    scopus 로고
    • Cyclin E in breast tumors is cleaved into its low molecular weight forms by calpain
    • Wang XD, Rosales JL, Magliocco A, Gnanakumar R, and Lee KY (2003). Cyclin E in breast tumors is cleaved into its low molecular weight forms by calpain. Oncogene 22, 769-774.
    • (2003) Oncogene , vol.22 , pp. 769-774
    • Wang, X.D.1    Rosales, J.L.2    Magliocco, A.3    Gnanakumar, R.4    Lee, K.Y.5
  • 40
    • 0034079985 scopus 로고    scopus 로고
    • Isolation of two novel genes, down-regulated in gastric cancer
    • Yoshikawa Y, Mukai H, Hino F, Asada K, and Kato I (2000). Isolation of two novel genes, down-regulated in gastric cancer. Jpn J Cancer Res 91, 459-463.
    • (2000) Jpn J Cancer Res , vol.91 , pp. 459-463
    • Yoshikawa, Y.1    Mukai, H.2    Hino, F.3    Asada, K.4    Kato, I.5
  • 41
    • 0028988989 scopus 로고
    • v-Src-induced degradation of focal adhesion kinase during morphological transformation of chicken embryo fibroblasts
    • Fincham VJ, Wyke JA, and Frame MC (1995). v-Src-induced degradation of focal adhesion kinase during morphological transformation of chicken embryo fibroblasts. Oncogene 10, 2247-2252 (published erratum appears in Oncogene 1995; 11(10), 2185).
    • (1995) Oncogene , vol.10 , pp. 2247-2252
    • Fincham, V.J.1    Wyke, J.A.2    Frame, M.C.3
  • 42
    • 0028852114 scopus 로고
    • published erratum
    • Fincham VJ, Wyke JA, and Frame MC (1995). v-Src-induced degradation of focal adhesion kinase during morphological transformation of chicken embryo fibroblasts. Oncogene 10, 2247-2252 (published erratum appears in Oncogene 1995; 11(10), 2185).
    • (1995) Oncogene , vol.11 , Issue.10 , pp. 2185
  • 43
    • 0023889189 scopus 로고
    • A single point mutation has pleiotropic effects on pp60v-src function
    • Welham MJ and Wyke JA (1988). A single point mutation has pleiotropic effects on pp60v-src function. J Virol 62, 1898-1906.
    • (1988) J Virol , vol.62 , pp. 1898-1906
    • Welham, M.J.1    Wyke, J.A.2
  • 44
    • 0027171138 scopus 로고
    • Activation of mitogen-activated protein kinase/extracellular signal-regulated kinase kinase by G protein and tyrosine kinase oncoproteins
    • Gardner AM, Vaillancourt RR, and Johnson GL (1993). Activation of mitogen-activated protein kinase/extracellular signal-regulated kinase kinase by G protein and tyrosine kinase oncoproteins. J Biol Chem 268, 17896-17901.
    • (1993) J Biol Chem , vol.268 , pp. 17896-17901
    • Gardner, A.M.1    Vaillancourt, R.R.2    Johnson, G.L.3
  • 45
    • 0034621967 scopus 로고    scopus 로고
    • Growth factor-dependent activation of the Ras-Raf-MEK-MAPK pathway in the human pancreatic carcinoma cell line PANC-1 carrying activated K-ras: Implications for cell proliferation and cell migration
    • Giehl K, Skripczynski B, Mansard A, Menke A, and Gierschik P (2000). Growth factor-dependent activation of the Ras-Raf-MEK-MAPK pathway in the human pancreatic carcinoma cell line PANC-1 carrying activated K-ras: implications for cell proliferation and cell migration. Oncogene 19, 2930-2942.
    • (2000) Oncogene , vol.19 , pp. 2930-2942
    • Giehl, K.1    Skripczynski, B.2    Mansard, A.3    Menke, A.4    Gierschik, P.5
  • 46
    • 0035968342 scopus 로고    scopus 로고
    • Membrane proximal ERK signaling is required for M-calpain activation downstream of epidermal growth factor receptor signaling
    • Glading A, Uberall F, Keyse SM, Lauffenburger DA, and Wells A (2001). Membrane proximal ERK signaling is required for M-calpain activation downstream of epidermal growth factor receptor signaling. J Biol Chem 276, 23341-23348.
    • (2001) J Biol Chem , vol.276 , pp. 23341-23348
    • Glading, A.1    Uberall, F.2    Keyse, S.M.3    Lauffenburger, D.A.4    Wells, A.5
  • 50
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany G, Standaert RF, Lane WS, Choi S, Corey EJ, and Schreiber SL (1995). Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268, 726-731.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 51
    • 0018763480 scopus 로고
    • Inhibition of the lysosomal pathway of protein degradation in isolated rat hepatocytes by ammonia, methylamine, chloroquine and leupeptin
    • Seglen PO, Grinde B, and Solheim AE (1979). Inhibition of the lysosomal pathway of protein degradation in isolated rat hepatocytes by ammonia, methylamine, chloroquine and leupeptin. Eur J Biochem 95, 215-225.
    • (1979) Eur J Biochem , vol.95 , pp. 215-225
    • Seglen, P.O.1    Grinde, B.2    Solheim, A.E.3
  • 52
    • 0000391671 scopus 로고
    • Decrease in macrophage antigen catabolism caused by ammonia and chloroquine is associated with inhibition of antigen presentation to T cells
    • Ziegler HK and Unanue ER (1982). Decrease in macrophage antigen catabolism caused by ammonia and chloroquine is associated with inhibition of antigen presentation to T cells. Proc Natl Acad Sci USA 79, 175-178.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 175-178
    • Ziegler, H.K.1    Unanue, E.R.2
  • 53
    • 0035985071 scopus 로고    scopus 로고
    • Effect of cysteine proteinase inhibitors on murine B16 melanoma cell invasion in vitro
    • Sever N, Filipic M, Brzin J, and Lah TT (2002). Effect of cysteine proteinase inhibitors on murine B16 melanoma cell invasion in vitro. Biol Chem 383, 839-842.
    • (2002) Biol Chem , vol.383 , pp. 839-842
    • Sever, N.1    Filipic, M.2    Brzin, J.3    Lah, T.T.4
  • 55
    • 0020999298 scopus 로고
    • Talin: A cytoskeletal component concentrated in adhesion plaques and other sites of actin-membrane interaction
    • Burridge K and Connell L (1983). Talin: a cytoskeletal component concentrated in adhesion plaques and other sites of actin-membrane interaction. Cell Motil 3, 405-417.
    • (1983) Cell Motil , vol.3 , pp. 405-417
    • Burridge, K.1    Connell, L.2
  • 56
    • 0037509990 scopus 로고    scopus 로고
    • Focal adhesion kinase: The first ten years
    • Parsons JT (2003). Focal adhesion kinase: the first ten years. J Cell Sci 116, 1409-1416.
    • (2003) J Cell Sci , vol.116 , pp. 1409-1416
    • Parsons, J.T.1
  • 57
    • 0027333413 scopus 로고
    • The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane
    • Bennett V and Gilligan DM (1993). The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane. Annu Rev Cell Biol 9, 27-66.
    • (1993) Annu Rev Cell Biol , vol.9 , pp. 27-66
    • Bennett, V.1    Gilligan, D.M.2
  • 59
    • 0033229742 scopus 로고    scopus 로고
    • Degraded collagen fragments promote rapid disassembly of smooth muscle focal adhesions that correlates with cleavage of pp125(FAK), paxillin, and talin
    • Carragher NO, Levkau B, Ross R, and Raines EW (1999). Degraded collagen fragments promote rapid disassembly of smooth muscle focal adhesions that correlates with cleavage of pp125(FAK), paxillin, and talin. J Cell Biol 147, 619-630.
    • (1999) J Cell Biol , vol.147 , pp. 619-630
    • Carragher, N.O.1    Levkau, B.2    Ross, R.3    Raines, E.W.4
  • 60
    • 0033571776 scopus 로고    scopus 로고
    • The behavior of calpain-generated N- and C-terminal fragments of talin in integrin-mediated signaling pathways
    • Hayashi M, Suzuki H, Kawashima S, Saido TC, and Inomata M (1999). The behavior of calpain-generated N- and C-terminal fragments of talin in integrin-mediated signaling pathways. Arch Biochem Biophys 371, 133-141.
    • (1999) Arch Biochem Biophys , vol.371 , pp. 133-141
    • Hayashi, M.1    Suzuki, H.2    Kawashima, S.3    Saido, T.C.4    Inomata, M.5
  • 61
    • 0029854806 scopus 로고    scopus 로고
    • Non-erythroid alpha-spectrin breakdown by calpain and interleukin 1 beta-converting-enzyme-like protease(s) in apoptotic cells: Contributory roles of both protease families in neuronal apoptosis
    • Nath R, Raser KJ, Stafford D, Hajimohammadreza I, Posner A, Allen H, Talanian RV, Yuen P, Gilbertsen RB, and Wang KK (1996). Non-erythroid alpha-spectrin breakdown by calpain and interleukin 1 beta-converting-enzyme-like protease(s) in apoptotic cells: contributory roles of both protease families in neuronal apoptosis. Biochem J 319, 683-690.
    • (1996) Biochem J , vol.319 , pp. 683-690
    • Nath, R.1    Raser, K.J.2    Stafford, D.3    Hajimohammadreza, I.4    Posner, A.5    Allen, H.6    Talanian, R.V.7    Yuen, P.8    Gilbertsen, R.B.9    Wang, K.K.10
  • 63
    • 0032536543 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of focal adhesion kinase pp125FAK and disassembly of focal adhesions in human endothelial cell apoptosis
    • Levkau B, Herren B, Koyama H, Ross R, and Raines EW (1998). Caspase-mediated cleavage of focal adhesion kinase pp125FAK and disassembly of focal adhesions in human endothelial cell apoptosis. J Exp Med 187, 579-586.
    • (1998) J Exp Med , vol.187 , pp. 579-586
    • Levkau, B.1    Herren, B.2    Koyama, H.3    Ross, R.4    Raines, E.W.5
  • 64
    • 0025021281 scopus 로고
    • Cysteine proteinase inhibitors and ras gene products share the same biological activities including transforming activity toward NIH3T3 mouse fibroblasts and the differentiation-inducing activity toward PC12 rat pheochromocytoma cells
    • Hiwasa T, Sawada T, and Sakiyama S (1990). Cysteine proteinase inhibitors and ras gene products share the same biological activities including transforming activity toward NIH3T3 mouse fibroblasts and the differentiation-inducing activity toward PC12 rat pheochromocytoma cells. Carcinogenesis 11, 75-80.
    • (1990) Carcinogenesis , vol.11 , pp. 75-80
    • Hiwasa, T.1    Sawada, T.2    Sakiyama, S.3
  • 65
    • 0029922539 scopus 로고    scopus 로고
    • Comparative analysis of the structure and function of the chicken c-myc and v-myc genes: v-myc is a more potent inducer of cell proliferation and apoptosis than c-myc
    • Petropoulos CJ, Givol I, and Hughes SH (1996). Comparative analysis of the structure and function of the chicken c-myc and v-myc genes: v-myc is a more potent inducer of cell proliferation and apoptosis than c-myc. Oncogene 12, 2611-2621.
    • (1996) Oncogene , vol.12 , pp. 2611-2621
    • Petropoulos, C.J.1    Givol, I.2    Hughes, S.H.3
  • 66
    • 0036724767 scopus 로고    scopus 로고
    • Calpain activates caspase-3 during UV-induced neuronal death but only calpain is necessary for death
    • McCollum AT, Nasr P, and Estus S (2002). Calpain activates caspase-3 during UV-induced neuronal death but only calpain is necessary for death. J Neurochem 2, 1208-1220.
    • (2002) J Neurochem , vol.2 , pp. 1208-1220
    • McCollum, A.T.1    Nasr, P.2    Estus, S.3
  • 67
    • 0034193138 scopus 로고    scopus 로고
    • Cleavage of Bax enhances its cell death function
    • Wood DE and Newcomb EW (2000). Cleavage of Bax enhances its cell death function. Exp Cell Res 256, 375-382.
    • (2000) Exp Cell Res , vol.256 , pp. 375-382
    • Wood, D.E.1    Newcomb, E.W.2
  • 68
    • 0036236471 scopus 로고    scopus 로고
    • Calpain-mediated Bid cleavage and calpain-independent Bak modulation: Two separate pathways in cisplatin-induced apoptosis
    • Mandic A, Viktorsson K, Strandberg L, Heiden T, Hansson J, Linder S, and Shoshan MC (2002). Calpain-mediated Bid cleavage and calpain-independent Bak modulation: two separate pathways in cisplatin-induced apoptosis. Mol Cell Biol 22, 3003-3013.
    • (2002) Mol Cell Biol , vol.22 , pp. 3003-3013
    • Mandic, A.1    Viktorsson, K.2    Strandberg, L.3    Heiden, T.4    Hansson, J.5    Linder, S.6    Shoshan, M.C.7
  • 69
    • 0034086332 scopus 로고    scopus 로고
    • Calpain inhibitor 1 activates p53-dependent apoptosis in tumor cell lines
    • Atencio IA, Ramachandra M, Shabram P, and Demers GW (2000). Calpain inhibitor 1 activates p53-dependent apoptosis in tumor cell lines. Cell Growth Differ 11, 247-253.
    • (2000) Cell Growth Differ , vol.11 , pp. 247-253
    • Atencio, I.A.1    Ramachandra, M.2    Shabram, P.3    Demers, G.W.4
  • 70
    • 0001110114 scopus 로고    scopus 로고
    • Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases
    • Chua BT, Guo K, and Li P (2000). Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases. J Biol Chem 275, 5131-5135.
    • (2000) J Biol Chem , vol.275 , pp. 5131-5135
    • Chua, B.T.1    Guo, K.2    Li, P.3
  • 71
    • 0041018181 scopus 로고    scopus 로고
    • Cleavage of the calpain inhibitor, calpastatin, during apoptosis
    • Porn-Ares MI, Samali A, and Orrenius S (1998). Cleavage of the calpain inhibitor, calpastatin, during apoptosis. Cell Death Differ 5, 1028-1033.
    • (1998) Cell Death Differ , vol.5 , pp. 1028-1033
    • Porn-Ares, M.I.1    Samali, A.2    Orrenius, S.3
  • 72
    • 0027768659 scopus 로고
    • Evidence for enhanced expression of c-fos, c-jun, and the Ca(2+)-activated neutral protease in rat liver following carbon tetrachloride administration
    • Zawaski K, Gruebele A, Kaplan D, Reddy S, Mortensen A, and Novak RF (1993). Evidence for enhanced expression of c-fos, c-jun, and the Ca(2+)-activated neutral protease in rat liver following carbon tetrachloride administration. Biochem Biophys Res Commun 197, 585-590.
    • (1993) Biochem Biophys Res Commun , vol.197 , pp. 585-590
    • Zawaski, K.1    Gruebele, A.2    Kaplan, D.3    Reddy, S.4    Mortensen, A.5    Novak, R.F.6
  • 74
    • 0029922373 scopus 로고    scopus 로고
    • Investigation of the interaction of m-calpain with phospholipids: Calpain-phospholipid interactions
    • Arthur JS and Crawford C (1996). Investigation of the interaction of m-calpain with phospholipids: calpain-phospholipid interactions. Biochim Biophys Acta 1293, 201-206.
    • (1996) Biochim Biophys Acta , vol.1293 , pp. 201-206
    • Arthur, J.S.1    Crawford, C.2
  • 75
    • 0037092051 scopus 로고    scopus 로고
    • Evidence for involvement of calpain in c-Myc proteolysis in vivo
    • Small GW, Chou TY, Dang CV, and Orlowski RZ (2002). Evidence for involvement of calpain in c-Myc proteolysis in vivo. Arch Biochem Biophys 400, 151-161.
    • (2002) Arch Biochem Biophys , vol.400 , pp. 151-161
    • Small, G.W.1    Chou, T.Y.2    Dang, C.V.3    Orlowski, R.Z.4
  • 77
    • 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
    • Shiraha H, Glading A, Chou J, Jia Z, and Wells A (2002). Activation of m-calpain (calpain II) by epidermal growth factor is limited by protein kinase A phosphorylation of m-calpain, Mol Cell Biol 22, 2716-2727.
    • (2002) Mol Cell Biol , vol.22 , pp. 2716-2727
    • Shiraha, H.1    Glading, A.2    Chou, J.3    Jia, Z.4    Wells, A.5
  • 78
    • 0036168356 scopus 로고    scopus 로고
    • Cutting to the chase: Calpain proteases in cell motility
    • Glading A, Lauffenburger DA, and Wells A (2002). Cutting to the chase: calpain proteases in cell motility. Trends Cell Biol 12, 46-54.
    • (2002) Trends Cell Biol , vol.12 , pp. 46-54
    • Glading, A.1    Lauffenburger, D.A.2    Wells, A.3
  • 80
    • 0035958967 scopus 로고    scopus 로고
    • Calpain cleavage promotes talin binding to the beta 3 integrin cytoplasmic domain
    • Yan B, Calderwood DA, Yaspan B, and Ginsberg MH (2001). Calpain cleavage promotes talin binding to the beta 3 integrin cytoplasmic domain. J Biol Chem 276, 28164-28170.
    • (2001) J Biol Chem , vol.276 , pp. 28164-28170
    • Yan, B.1    Calderwood, D.A.2    Yaspan, B.3    Ginsberg, M.H.4
  • 82
    • 0034714267 scopus 로고    scopus 로고
    • Src-mediated tyrosine phosphorylation of NR2 subunits of N-methyl-D-aspartate receptors protects from calpain-mediated truncation of their C-terminal domains
    • Bi R, Rong Y, Bernard A, Khrestchatisky M, and Baudry M (2000). Src-mediated tyrosine phosphorylation of NR2 subunits of N-methyl-D-aspartate receptors protects from calpain-mediated truncation of their C-terminal domains. J Biol Chem 275, 26477-26483.
    • (2000) J Biol Chem , vol.275 , pp. 26477-26483
    • Bi, R.1    Rong, Y.2    Bernard, A.3    Khrestchatisky, M.4    Baudry, M.5
  • 83
    • 0033551399 scopus 로고    scopus 로고
    • The v-myc oncogene
    • Lee CM and Reddy EP (1999). The v-myc oncogene. Oncogene 18, 2997-3003.
    • (1999) Oncogene , vol.18 , pp. 2997-3003
    • Lee, C.M.1    Reddy, E.P.2
  • 84
    • 0036781812 scopus 로고    scopus 로고
    • c-MYC: More than just a matter of life and death
    • Pelengaris S, Khan M, and Evan G (2002). c-MYC: more than just a matter of life and death. Natl Rev Cancer 2, 764-776.
    • (2002) Natl Rev Cancer , vol.2 , pp. 764-776
    • Pelengaris, S.1    Khan, M.2    Evan, G.3


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