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Volumn 29, Issue 3, 2006, Pages 655-663

Apoptosis induced by novel aldehyde calpain inhibitors in human tumor cell lines

Author keywords

Apoptosis; Calpain; Cell cycle

Indexed keywords

ALDEHYDE; CALPAIN; CASP3 PROTEIN, HUMAN; CASPASE; CASPASE 3; CYSTEINE PROTEINASE INHIBITOR; PROTEASOME;

EID: 33749363042     PISSN: 10196439     EISSN: 17912423     Source Type: Journal    
DOI: 10.3892/ijo.29.3.655     Document Type: Article
Times cited : (15)

References (36)
  • 1
    • 0033920566 scopus 로고    scopus 로고
    • Protease inhibitor-induced apoptosis: Accumulation of wt p53, p21WAF1/CIP1, and induction of apoptosis are independent markers of proteasome inhibition
    • An WG, Hwang SG, Trepel JB and Blagosklonny MV: Protease inhibitor-induced apoptosis: accumulation of wt p53, p21WAF1/CIP1, and induction of apoptosis are independent markers of proteasome inhibition. Leukemia 14: 1276-1283, 2000.
    • (2000) Leukemia , vol.14 , pp. 1276-1283
    • An, W.G.1    Hwang, S.G.2    Trepel, J.B.3    Blagosklonny, M.V.4
  • 3
    • 4344684216 scopus 로고    scopus 로고
    • The emerging role of bortezomib in the treatment of indolent non-Hodgkin's and mantle cell lymphomas
    • O'Connor OA: The emerging role of bortezomib in the treatment of indolent non-Hodgkin's and mantle cell lymphomas. Curr Treat Options Oncol 5: 269-281, 2004.
    • (2004) Curr Treat Options Oncol , vol.5 , pp. 269-281
    • O'Connor, O.A.1
  • 4
    • 0021111512 scopus 로고
    • Proteolytic activation of calcium-activated, phospholipid-dependent protein kinase by calcium-dependent neutral protease
    • Kishimoto A, Kajikawa N, Shiota M and Nishizuka Y: Proteolytic activation of calcium-activated, phospholipid-dependent protein kinase by calcium-dependent neutral protease. J Biol Chem 258: 1156-1164, 1983.
    • (1983) J Biol Chem , vol.258 , pp. 1156-1164
    • Kishimoto, A.1    Kajikawa, N.2    Shiota, M.3    Nishizuka, Y.4
  • 5
    • 0027494395 scopus 로고
    • Calpain-catalyzed cleavage and subcellular relocation of protein phosphotyrosine phosphatase 1B (PTP-1B) in human platelets
    • Frangioni JV, Oda A, Smith M, Salzman EW and Neel BG: Calpain-catalyzed cleavage and subcellular relocation of protein phosphotyrosine phosphatase 1B (PTP-1B) in human platelets. EMBO J 12: 4843-4856, 1993. (Pubitemid 23330291)
    • (1993) EMBO Journal , vol.12 , Issue.12 , pp. 4843-4856
    • Frangioni, J.V.1    Oda, A.2    Smith, M.3    Salzman, E.W.4    Neel, B.G.5
  • 6
    • 1242316976 scopus 로고    scopus 로고
    • Calpain-1 Regulates Bax and Subsequent Smac-dependent Caspase-3 Activation in Neutrophil Apoptosis
    • DOI 10.1074/jbc.M308576200
    • Altznauer F, Conus S, Cavalli A, Folkers G and Simon HU: Calpain-1 regulates Bax and subsequent Smac-dependent caspase-3 activation in neutrophil apoptosis. J Biol Chem 279: 5947-5957, 2004. (Pubitemid 38220627)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.7 , pp. 5947-5957
    • Altznauer, F.1    Conus, S.2    Cavalli, A.3    Folkers, G.4    Simon, H.-U.5
  • 7
    • 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: Specific proteolysis of the c-mos proto-oncogene product by calpain on fertilization of Xenopus eggs. Nature 342: 505-511, 1989.
    • (1989) Nature , vol.342 , pp. 505-511
    • Watanabe, N.1    Vande Woude, G.F.2    Ikawa, Y.3    Sagata, N.4
  • 8
    • 0022518154 scopus 로고
    • Fodrin degradation by calcium-activated neutral proteinase (CANP) in retinal ganglion cell neurons and optic glia: Preferential localization of CANP activities in neurons
    • Nixon RA: Fodrin degradation by calcium-activated neutral proteinase (CANP) in retinal ganglion cell neurons and optic glia: preferential localization of CANP activities in neurons. J Neurosci 6: 1264-1271, 1986.
    • (1986) J Neurosci , vol.6 , pp. 1264-1271
    • Nixon, R.A.1
  • 9
    • 0028282502 scopus 로고
    • Immunolocalization of calpain I-mediated spectrin degradation to vulnerable neurons in the ischemic gerbil brain
    • Roberts-Lewis JM, Savage MJ, Marcy VR, Pinsker LR and Siman R: Immunolocalization of calpain I-mediated spectrin degradation to vulnerable neurons in the ischemic gerbil brain. J Neurosci 14: 3934-3944, 1994.
    • (1994) J Neurosci , vol.14 , pp. 3934-3944
    • Roberts-Lewis, J.M.1    Savage, M.J.2    Marcy, V.R.3    Pinsker, L.R.4    Siman, R.5
  • 10
    • 0025900722 scopus 로고
    • Degradation of transcription factors, c-Jun and c-Fos, by calpain
    • Hirai S, Kawasaki H, Yaniv M and Suzuki K: Degradation of transcription factors, c-Jun and c-Fos, by calpain. FEBS Lett 287: 57-61, 1991.
    • (1991) FEBS Lett , vol.287 , pp. 57-61
    • Hirai, S.1    Kawasaki, H.2    Yaniv, M.3    Suzuki, K.4
  • 11
    • 0033534475 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha-inducible IkappaBalpha proteolysis mediated by cytosolic m-Calpain: A mechanism parallel to the ubiquitin-proteasome pathway for nuclear factor-kappaB activation
    • Han Y, Weinman S, Boldogh I, Walker RK and Brasier AR: Tumor necrosis factor-alpha-inducible IkappaBalpha proteolysis mediated by cytosolic m-calpain. A mechanism parallel to the ubiquitin-proteasome pathway for nuclear factor-kappab activation. J Biol Chem 274: 787-794, 1999. (Pubitemid 129535237)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.2 , pp. 787-794
    • Han, Y.1    Weinman, S.2    Boldogh, I.3    Walker, R.K.4    Brasier, A.R.5
  • 12
    • 0030270612 scopus 로고    scopus 로고
    • Calpain inhibitors and serine protease inhibitors can produce apoptosis in HL-60 cells
    • DOI 10.1006/abbi.1996.0443
    • Lu Q and Mellgren RL: Calpain inhibitors and serine protease inhibitors can produce apoptosis in HL-60 cells. Arch Biochem Biophys 334: 175-181, 1996. (Pubitemid 26329815)
    • (1996) Archives of Biochemistry and Biophysics , vol.334 , Issue.1 , pp. 175-181
    • Lu, Q.1    Mellgren, R.L.2
  • 13
    • 0034130450 scopus 로고    scopus 로고
    • Calpain inhibitor II induces caspase-dependent apoptosis in human acute lymphoblastic leukemia and non-Hodgkin's lymphoma cells as well as some solid tumor cells
    • Zhu DM and Uckun FM: Calpain inhibitor II induces caspase-dependent apoptosis in human acute lymphoblastic leukemia and non-Hodgkin's lymphoma cells as well as some solid tumor cells. Clin Cancer Res 6: 2456-2463, 2000.
    • (2000) Clin Cancer Res , vol.6 , pp. 2456-2463
    • Zhu, D.M.1    Uckun, F.M.2
  • 14
    • 0028827264 scopus 로고
    • Calpain inhibitor-induced apoptosis in human prostate adenocarcinoma cells
    • Zhu W, Murtha PE and Young CY: Calpain inhibitor-induced apoptosis in human prostate adenocarcinoma cells. Biochem Biophys Res Commun 214: 1130-1137, 1995.
    • (1995) Biochem Biophys Res Commun , vol.214 , pp. 1130-1137
    • Zhu, W.1    Murtha, P.E.2    Young, C.Y.3
  • 16
    • 14044252859 scopus 로고    scopus 로고
    • Interferon-inducible protein 9 (CXCL11)-induced cell motility in keratinocytes requires calcium flux-dependent activation of mu-calpain
    • Satish L, Blair HC, Glading A and Wells A: Interferon-inducible protein 9 (CXCL11)-induced cell motility in keratinocytes requires calcium flux-dependent activation of mu-calpain. Mol Cell Biol 25: 1922-1941, 2005.
    • (2005) Mol Cell Biol , vol.25 , pp. 1922-1941
    • Satish, L.1    Blair, H.C.2    Glading, A.3    Wells, A.4
  • 17
    • 0036887581 scopus 로고    scopus 로고
    • Calpain: A role in cell transformation and migration
    • Carragher NO and Frame MC: Calpain: a role in cell transformation and migration. Int J Biochem Cell Biol 34: 1539-1543, 2002.
    • (2002) Int J Biochem Cell Biol , vol.34 , pp. 1539-1543
    • Carragher, N.O.1    Frame, M.C.2
  • 18
    • 0036791034 scopus 로고    scopus 로고
    • Calpain as an effector of the Gq signaling pathway for inhibition of Wnt/beta-catenin-regulated cell proliferation
    • Li G and Iyengar R: Calpain as an effector of the Gq signaling pathway for inhibition of Wnt/beta-catenin-regulated cell proliferation. Proc Natl Acad Sci USA 99: 13254-13259, 2002.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13254-13259
    • Li, G.1    Iyengar, R.2
  • 19
    • 0037077297 scopus 로고    scopus 로고
    • Calpain inhibition decreases the growth rate of mammalian cell colonies
    • DOI 10.1074/jbc.M111689200
    • Xu Y and Mellgren RL: Calpain inhibition decreases the growth rate of mammalian cell colonies. J Biol Chem 277: 21474-21479, 2002. (Pubitemid 34952290)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.24 , pp. 21474-21479
    • Xu, Y.1    Mellgren, R.L.2
  • 20
    • 5644271513 scopus 로고    scopus 로고
    • Cleavage of beta-catenin by calpain in prostate and mammary tumor cells
    • DOI 10.1158/0008-5472.CAN-04-1048
    • Rios-Doria J, Kuefer R, Ethier SP and Day ML: Cleavage of beta-catenin by calpain in prostate and mammary tumor cells. Cancer Res 64: 7237-7240, 2004. (Pubitemid 39372058)
    • (2004) Cancer Research , vol.64 , Issue.20 , pp. 7237-7240
    • Rios-Doria, J.1    Kuefer, R.2    Ethier, S.P.3    Day, M.L.4
  • 25
    • 0035713687 scopus 로고    scopus 로고
    • Real-time quantitative PCR
    • Schmittgen TD: Real-time quantitative PCR. Methods 25: 383-385, 2001.
    • (2001) Methods , vol.25 , pp. 383-385
    • Schmittgen, T.D.1
  • 27
    • 0029886022 scopus 로고    scopus 로고
    • Kinetic characterization of the chymotryptic activity of the 20S proteasome
    • DOI 10.1021/bi952262x
    • Stein RL, Melandri F and Dick L: Kinetic characterization of the chymotryptic activity of the 20S proteasome. Biochemistry 35: 3899-3908, 1996. (Pubitemid 26113443)
    • (1996) Biochemistry , vol.35 , Issue.13 , pp. 3899-3908
    • Stein, R.L.1    Melandri, F.2    Dick, L.3
  • 28
    • 0026775178 scopus 로고
    • Expression of calpain II gene in human hematopoietic system cells infected with human T-cell leukemia virus type I
    • Adachi Y, Kitahara-Ozawa A, Sugamura K, Lee WJ, Yodoi J, Maki M, Murachi T and Hatanaka M: Expression of calpain II gene in human hematopoietic system cells infected with human T-cell leukemia virus type I. J Biol Chem 267: 19373-19378, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 19373-19378
    • Adachi, Y.1    Kitahara-Ozawa, A.2    Sugamura, K.3    Lee, W.J.4    Yodoi, J.5    Maki, M.6    Murachi, T.7    Hatanaka, M.8
  • 29
    • 0037810356 scopus 로고    scopus 로고
    • Revisiting ubiquity and tissue specificity of human calpains
    • DOI 10.1515/BC.2003.106
    • Farkas A, Tompa P and Friedrich P: Revisiting ubiquity and tissue specificity of human calpains. Biol Chem 384: 945-949, 2003. (Pubitemid 36874509)
    • (2003) Biological Chemistry , vol.384 , Issue.6 , pp. 945-949
    • Farkas, A.1    Tompa, P.2    Friedrich, P.3
  • 31
    • 0031014946 scopus 로고    scopus 로고
    • Proteolytic cleavage of human p53 by calpain: A potential regulator of protein stability
    • Kubbutat MH and Vousden KH: Proteolytic cleavage of human p53 by calpain: a potential regulator of protein stability. Mol Cell Biol 17: 460-468, 1997.
    • (1997) Mol Cell Biol , vol.17 , pp. 460-468
    • Kubbutat, M.H.1    Vousden, K.H.2
  • 33
    • 0024285560 scopus 로고
    • Calpain II involvement in mitosis
    • Schollmeyer JE: Calpain II involvement in mitosis. Science 240: 911-913, 1988.
    • (1988) Science , vol.240 , pp. 911-913
    • Schollmeyer, J.E.1
  • 34
    • 0034625418 scopus 로고    scopus 로고
    • Mitotic clonal expansion during preadipocyte differentiation: Calpain-mediated turnover of p27
    • Patel YM and Lane MD: Mitotic clonal expansion during preadipocyte differentiation: calpain-mediated turnover of p27. J Biol Chem 275: 17653-17660, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 17653-17660
    • Patel, Y.M.1    Lane, M.D.2
  • 36
    • 0035900769 scopus 로고    scopus 로고
    • Involvement of the interaction between p21 and proliferating cell nuclear antigen for the maintenance of G2/M arrest after DNA damage
    • Ando T, Kawabe T, Ohara H, Ducommun B, Itoh M and Okamoto T: Involvement of the interaction between p21 and proliferating cell nuclear antigen for the maintenance of G2/M arrest after DNA damage. J Biol Chem 276: 42971-42977, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 42971-42977
    • Ando, T.1    Kawabe, T.2    Ohara, H.3    Ducommun, B.4    Itoh, M.5    Okamoto, T.6


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