메뉴 건너뛰기




Volumn 21, Issue 1, 2007, Pages 9-15

Cleavage of tensin during cytoskeleton disruption in YTX-induced apoptosis

Author keywords

Apoptosis; F actin cytoskeleton; Fibrillar adhesions; Focal adhesion complexes; Tensin; Yessotoxin

Indexed keywords

F ACTIN; PROTEIN; TENSIN; YESSOTOXIN;

EID: 33845196954     PISSN: 08872333     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tiv.2006.07.012     Document Type: Article
Times cited : (32)

References (59)
  • 1
    • 0029833286 scopus 로고    scopus 로고
    • Platelet-derived growth factor-induced formation of tensin and phophoinositide 3-kinase complexes
    • Auger K.R., Songyang Z., Lo S.H., Roberts T.M., and Chen L.B. Platelet-derived growth factor-induced formation of tensin and phophoinositide 3-kinase complexes. J. Biol. Chem. 271 (1996) 23452-23457
    • (1996) J. Biol. Chem. , vol.271 , pp. 23452-23457
    • Auger, K.R.1    Songyang, Z.2    Lo, S.H.3    Roberts, T.M.4    Chen, L.B.5
  • 2
    • 0036028014 scopus 로고    scopus 로고
    • Comparison of oral and intraperitoneal toxicity of yessotoxin towards mice
    • Aune T., Sørby R., Yasumoto T., Ramstad H., and Landsverk T. Comparison of oral and intraperitoneal toxicity of yessotoxin towards mice. Toxicon 40 (2002) 77-82
    • (2002) Toxicon , vol.40 , pp. 77-82
    • Aune, T.1    Sørby, R.2    Yasumoto, T.3    Ramstad, H.4    Landsverk, T.5
  • 3
    • 0033853424 scopus 로고    scopus 로고
    • The E-cadherin-catenin complex in tumor metastasis: Structure, function and regulation
    • Beavon I.R.G. The E-cadherin-catenin complex in tumor metastasis: Structure, function and regulation. Eur. J. Cancer 36 (2000) 1607-1620
    • (2000) Eur. J. Cancer , vol.36 , pp. 1607-1620
    • Beavon, I.R.G.1
  • 4
    • 0002424141 scopus 로고    scopus 로고
    • Cytoskeleton-associated anchor and signal transduction proteins. Introduction
    • Kreis T., and Vale R. (Eds), Oxford University Press, New York
    • Bershadsky A., and Geiger B. Cytoskeleton-associated anchor and signal transduction proteins. Introduction. In: Kreis T., and Vale R. (Eds). Guidebook to the Extracellular Matrix Anchor and Adhesion Proteins (1999), Oxford University Press, New York 3-11
    • (1999) Guidebook to the Extracellular Matrix Anchor and Adhesion Proteins , pp. 3-11
    • Bershadsky, A.1    Geiger, B.2
  • 5
    • 0028245813 scopus 로고
    • Cadherin expression in carcinomas: Role in the formation of cell junctions and the prevention of invasiveness
    • Birchmeier W., and Behrens J. Cadherin expression in carcinomas: Role in the formation of cell junctions and the prevention of invasiveness. Biochim. Biophys. Acta 1198 (1994) 11-26
    • (1994) Biochim. Biophys. Acta , vol.1198 , pp. 11-26
    • Birchmeier, W.1    Behrens, J.2
  • 6
    • 0026488698 scopus 로고
    • Localization of a 215 kDa tyrosine-phosphorylated protein that cross-reacts with tensin antibodies
    • Bockholt S.M., Otey C.A., Glenney J.R., and Burridge K. Localization of a 215 kDa tyrosine-phosphorylated protein that cross-reacts with tensin antibodies. Exp. Cell Res. 203 (1992)
    • (1992) Exp. Cell Res. , vol.203
    • Bockholt, S.M.1    Otey, C.A.2    Glenney, J.R.3    Burridge, K.4
  • 7
    • 0033137070 scopus 로고    scopus 로고
    • Extracellular matrix and integrin signalling: The shape of things to come
    • Boudreau N.J., and Jones P.L. Extracellular matrix and integrin signalling: The shape of things to come. Biochem. J. 339 (1999) 481-488
    • (1999) Biochem. J. , vol.339 , pp. 481-488
    • Boudreau, N.J.1    Jones, P.L.2
  • 8
    • 0032487438 scopus 로고    scopus 로고
    • Fibronectin matrix regulates activation of Rho and Cdc42 GTPases and cell cycle progression
    • Bourdoulous S., Orend D., MacKenna D.A., Pasqualini R., and Ruoslahti E. Fibronectin matrix regulates activation of Rho and Cdc42 GTPases and cell cycle progression. J. Cell Biol. 143 1 (1998) 267-276
    • (1998) J. Cell Biol. , vol.143 , Issue.1 , pp. 267-276
    • Bourdoulous, S.1    Orend, D.2    MacKenna, D.A.3    Pasqualini, R.4    Ruoslahti, E.5
  • 10
    • 0037204948 scopus 로고    scopus 로고
    • TNF-R1 signalling: A beautiful pathway
    • Chen G., and Goeddel D.V. TNF-R1 signalling: A beautiful pathway. Science 296 (2002) 1634-1635
    • (2002) Science , vol.296 , pp. 1634-1635
    • Chen, G.1    Goeddel, D.V.2
  • 11
    • 0037444799 scopus 로고    scopus 로고
    • Regulation of tensin-promoted cell cell migration by its focal ahesion localization and the SH2 domain
    • Chen H., and Lo S.H. Regulation of tensin-promoted cell cell migration by its focal ahesion localization and the SH2 domain. Biochem. J. 370 (2003) 1039-1045
    • (2003) Biochem. J. , vol.370 , pp. 1039-1045
    • Chen, H.1    Lo, S.H.2
  • 13
    • 0033079605 scopus 로고    scopus 로고
    • The role of the cell-adhesion molecule E-cadherin as a tumour suppressor gene
    • Christofori G., and Semb H. The role of the cell-adhesion molecule E-cadherin as a tumour suppressor gene. TIBS 24 (1999) 73-76
    • (1999) TIBS , vol.24 , pp. 73-76
    • Christofori, G.1    Semb, H.2
  • 14
    • 0028956756 scopus 로고
    • Molecular cloning, expression, and mapping of the high affinity acting-capping domain of chicken cardiac tensin
    • Chuang J.Z., Lin D., and Kin S. Molecular cloning, expression, and mapping of the high affinity acting-capping domain of chicken cardiac tensin. J. Cell Biol. 128 (1995) 1095-1109
    • (1995) J. Cell Biol. , vol.128 , pp. 1095-1109
    • Chuang, J.Z.1    Lin, D.2    Kin, S.3
  • 15
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark E.A., and Brugge J.S. Integrins and signal transduction pathways: The road taken. Science 268 (1995) 233-239
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 16
    • 0033962672 scopus 로고    scopus 로고
    • Focal adhesions - The cytoskeletal connection
    • Critchley D.R. Focal adhesions - The cytoskeletal connection. Curr. Opin. Cell. Biol. 12 (2000) 133-139
    • (2000) Curr. Opin. Cell. Biol. , vol.12 , pp. 133-139
    • Critchley, D.R.1
  • 17
    • 0025860227 scopus 로고
    • Presence of an SH2 domain in the actin-binding protein tensin
    • Davis M.L., Lu S.H., Lo S., Lin J.A., Butler B.J., Druker T.M., et al. Presence of an SH2 domain in the actin-binding protein tensin. Science 252 (1991) 712-715
    • (1991) Science , vol.252 , pp. 712-715
    • Davis, M.L.1    Lu, S.H.2    Lo, S.3    Lin, J.A.4    Butler, B.J.5    Druker, T.M.6
  • 19
  • 20
    • 0030220528 scopus 로고    scopus 로고
    • Okadaic acid induces changes in the organization of F-actin in intestinal cells
    • Fiorentini C., Matarrese P., Fattorossi A., and Donelli G. Okadaic acid induces changes in the organization of F-actin in intestinal cells. Toxicon 34 (1996) 937-945
    • (1996) Toxicon , vol.34 , pp. 937-945
    • Fiorentini, C.1    Matarrese, P.2    Fattorossi, A.3    Donelli, G.4
  • 21
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • Giancotti F.G., and Ruoslahti E. Integrin signaling. Science 285 (1999) 1028-1032
    • (1999) Science , vol.285 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 22
    • 0024382542 scopus 로고
    • Novel tyrosine kinase substrates from Rous sarcoma virus-transformed cells are present in the membrane skeleton
    • Glenney J.R., and Zockas L. Novel tyrosine kinase substrates from Rous sarcoma virus-transformed cells are present in the membrane skeleton. J. Cell Biol. 108 (1989) 2401-2408
    • (1989) J. Cell Biol. , vol.108 , pp. 2401-2408
    • Glenney, J.R.1    Zockas, L.2
  • 23
    • 21044450363 scopus 로고    scopus 로고
    • A role for actin in aging and apoptosis
    • Gourlay C.W., and Ayscough K.R. A role for actin in aging and apoptosis. J. Cell Sci. 118 (2005) 2119-2132
    • (2005) J. Cell Sci. , vol.118 , pp. 2119-2132
    • Gourlay, C.W.1    Ayscough, K.R.2
  • 24
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall A. Rho GTPases and the actin cytoskeleton. Science 279 (1998)
    • (1998) Science , vol.279
    • Hall, A.1
  • 26
    • 0029562867 scopus 로고
    • The assembly of integrin adhesions complexes requires both extracellular matrix and intracellular Rho/Rac GTPases
    • Hotchin N.A., and Hall A. The assembly of integrin adhesions complexes requires both extracellular matrix and intracellular Rho/Rac GTPases. J. Cell Biol. 131 (1995) 1857-1865
    • (1995) J. Cell Biol. , vol.131 , pp. 1857-1865
    • Hotchin, N.A.1    Hall, A.2
  • 28
    • 0023673239 scopus 로고
    • Cellular transformation, tyrosine kinase, and the cellular adhesion plaque
    • Kellie S. Cellular transformation, tyrosine kinase, and the cellular adhesion plaque. Bioessays 8 (1988) 25-30
    • (1988) Bioessays , vol.8 , pp. 25-30
    • Kellie, S.1
  • 29
    • 0037470777 scopus 로고    scopus 로고
    • Caspase-dependent cleavage of tensin induces disruption of actin cytoskeleton during apoptosis
    • Kook S., Do Hoon K., Shim S.R., Wook K., Chun J.S., and Song W.K. Caspase-dependent cleavage of tensin induces disruption of actin cytoskeleton during apoptosis. Biochem. Biophys. Res. Commun. 303 (2003) 37-45
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , pp. 37-45
    • Kook, S.1    Do Hoon, K.2    Shim, S.R.3    Wook, K.4    Chun, J.S.5    Song, W.K.6
  • 30
    • 0026493689 scopus 로고
    • Protein phosphatase inhibitors okadaic acid and calyculin A alter cell shape and F-actin distribution and inhibit stimulus-dependent increases in cytoskeletal actin of human neutrophils
    • Kreienbühl P., Keller H., and Niggli V. Protein phosphatase inhibitors okadaic acid and calyculin A alter cell shape and F-actin distribution and inhibit stimulus-dependent increases in cytoskeletal actin of human neutrophils. Blood 80 (1992) 2911-2919
    • (1992) Blood , vol.80 , pp. 2911-2919
    • Kreienbühl, P.1    Keller, H.2    Niggli, V.3
  • 31
    • 0033393450 scopus 로고    scopus 로고
    • Role of gelsolin in the active filament regulation of cardiac L-type calcium channels
    • Lader A.S., Kwiatkowski D.J., and Cantiello H.F. Role of gelsolin in the active filament regulation of cardiac L-type calcium channels. Am. J. Physiol. Cell Physiol. 277 6 (1999) 1277-1283
    • (1999) Am. J. Physiol. Cell Physiol. , vol.277 , Issue.6 , pp. 1277-1283
    • Lader, A.S.1    Kwiatkowski, D.J.2    Cantiello, H.F.3
  • 32
    • 0035018838 scopus 로고    scopus 로고
    • Apoptotic events induced by the phosphatase inhibitor okadaic acid in normal human lung fibroblasts
    • Leira F., Vieites M.R., and Botana L.M. Apoptotic events induced by the phosphatase inhibitor okadaic acid in normal human lung fibroblasts. Toxicol. in Vitro 15 (2001) 199-208
    • (2001) Toxicol. in Vitro , vol.15 , pp. 199-208
    • Leira, F.1    Vieites, M.R.2    Botana, L.M.3
  • 33
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex Initiates an apoptotic protease cascade
    • Li P., Nijhawan D., Budihardjo I., Srinivasula S., Ahmad M., Alnemri E.S., et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex Initiates an apoptotic protease cascade. Cell 91 (1997) 479-489
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.4    Ahmad, M.5    Alnemri, E.S.6
  • 34
    • 0027931203 scopus 로고
    • Molecular cloning of chick cardiac muscle tensin. Full-length cDNA sequence. Expression and characterization
    • Lo S.H., Bao S., Wong W., Liu Y., Janmey P.A., Hartwig J.A., et al. Molecular cloning of chick cardiac muscle tensin. Full-length cDNA sequence. Expression and characterization. J. Biol. Chem. 269 (1994) 22310-22319
    • (1994) J. Biol. Chem. , vol.269 , pp. 22310-22319
    • Lo, S.H.1    Bao, S.2    Wong, W.3    Liu, Y.4    Janmey, P.A.5    Hartwig, J.A.6
  • 35
    • 0028533592 scopus 로고
    • Tensin: A potential link between the cytoskeleton and signal transduction
    • Lo S.H., Weisberg E., and Chen L.B.H. Tensin: A potential link between the cytoskeleton and signal transduction. Bioessays 16 (1994) 817-823
    • (1994) Bioessays , vol.16 , pp. 817-823
    • Lo, S.H.1    Weisberg, E.2    Chen, L.B.H.3
  • 36
    • 0033902814 scopus 로고    scopus 로고
    • Intestinal restitution: Progression of actin cytoskeleton rearrangements and integrin function in a model of epithelial wound healing
    • Lotz M., Rabinovitz I., and Mercurio A.M. Intestinal restitution: Progression of actin cytoskeleton rearrangements and integrin function in a model of epithelial wound healing. Am. J. Pathol. 156 (2000) 985-996
    • (2000) Am. J. Pathol. , vol.156 , pp. 985-996
    • Lotz, M.1    Rabinovitz, I.2    Mercurio, A.M.3
  • 37
    • 0036690406 scopus 로고    scopus 로고
    • Caspase activation and death induced by yessotoxin in HeLa cells
    • Malaguti C., Ciminiello P., Fattorusso E., and Rossini G.P. Caspase activation and death induced by yessotoxin in HeLa cells. Toxicol. in Vitro 16 4 (2002) 357-363
    • (2002) Toxicol. in Vitro , vol.16 , Issue.4 , pp. 357-363
    • Malaguti, C.1    Ciminiello, P.2    Fattorusso, E.3    Rossini, G.P.4
  • 39
    • 0033756542 scopus 로고    scopus 로고
    • Morphological changes in the nucleus and actin cytoskeleton in the process of Fas-induced apoptosis in Jurkat T-cells
    • Maruyama W., Irie S., and Sato T.A. Morphological changes in the nucleus and actin cytoskeleton in the process of Fas-induced apoptosis in Jurkat T-cells. Histochem. J. 32 (2000) 495-503
    • (2000) Histochem. J. , vol.32 , pp. 495-503
    • Maruyama, W.1    Irie, S.2    Sato, T.A.3
  • 40
    • 0028961293 scopus 로고
    • Rho, rac and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia and filopodia
    • Nobes C.D., and Hall A. Rho, rac and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia and filopodia. Cell 7 (1995)
    • (1995) Cell , vol.7
    • Nobes, C.D.1    Hall, A.2
  • 41
    • 0032911020 scopus 로고    scopus 로고
    • Bidirectional signaling between the cytoskeleton and integrins
    • Schoenwaelder S.M., and Burridge K. Bidirectional signaling between the cytoskeleton and integrins. Curr. Opin. Cell. Biol. 11 (1999) 274-286
    • (1999) Curr. Opin. Cell. Biol. , vol.11 , pp. 274-286
    • Schoenwaelder, S.M.1    Burridge, K.2
  • 43
    • 0036616438 scopus 로고    scopus 로고
    • Factors influencing nominal effective concentrations of chemical compounds in vitro: Medium protein concentration
    • Seibert H., Mrchel S., and Gulden M. Factors influencing nominal effective concentrations of chemical compounds in vitro: Medium protein concentration. Toxicol. in Vitro 16 (2002) 289-297
    • (2002) Toxicol. in Vitro , vol.16 , pp. 289-297
    • Seibert, H.1    Mrchel, S.2    Gulden, M.3
  • 44
  • 46
    • 33749859921 scopus 로고    scopus 로고
    • Suárez Korsnes, M., Lem Hetland, D., Espenes, A., Aune, T. in press. Induction of apoptosis by YTX in myoblast cell lines via mitochondrial signalling transduction pathway. Toxicol. in Vitro, doi:10.1016/j.tiv.2006.06.015.
  • 48
    • 0025325167 scopus 로고
    • Cadherins: A molecular family important in selective cell-cell adhesion
    • Takeichi M. Cadherins: A molecular family important in selective cell-cell adhesion. Ann. Rev. Biochem. 59 (1990) 237-252
    • (1990) Ann. Rev. Biochem. , vol.59 , pp. 237-252
    • Takeichi, M.1
  • 50
    • 0032575750 scopus 로고    scopus 로고
    • Caspases enemies within
    • Thornbery N.A., and Lazebnik Y. Caspases enemies within. Science 281 (1998) 1312-1316
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornbery, N.A.1    Lazebnik, Y.2
  • 52
    • 0034682797 scopus 로고    scopus 로고
    • Cleavage of the actin-capping protein a-adducin at Asp-Asp-Ser-Asp633-Ala by caspase-3 is preceded by its phosphorylation on serine726 in cisplatin-induced apoptosis of renal epithelial cells
    • Van de Water B., Tijdens I.B., Verbrugge A., and Huigsloot M. Cleavage of the actin-capping protein a-adducin at Asp-Asp-Ser-Asp633-Ala by caspase-3 is preceded by its phosphorylation on serine726 in cisplatin-induced apoptosis of renal epithelial cells. J. Biol. Chem. 275 (2000) 25805-25813
    • (2000) J. Biol. Chem. , vol.275 , pp. 25805-25813
    • Van de Water, B.1    Tijdens, I.B.2    Verbrugge, A.3    Huigsloot, M.4
  • 53
    • 0025818032 scopus 로고
    • Genetic manipulation of E-cadherin expression by epithelial tumour cells reveals an invasion suppressor role
    • Vleminckx K., Vakaet L., Mareel M., Fiers W., and Van Roy F. Genetic manipulation of E-cadherin expression by epithelial tumour cells reveals an invasion suppressor role. Cell 66 (1991) 107-119
    • (1991) Cell , vol.66 , pp. 107-119
    • Vleminckx, K.1    Vakaet, L.2    Mareel, M.3    Fiers, W.4    Van Roy, F.5
  • 54
    • 0022512056 scopus 로고
    • A re-examination of the interaction of vinculin with actin
    • Wilkins J.A., and Lin S. A re-examination of the interaction of vinculin with actin. J. Cell Biol. 102 (1986)
    • (1986) J. Cell Biol. , vol.102
    • Wilkins, J.A.1    Lin, S.2
  • 55
    • 0031050449 scopus 로고    scopus 로고
    • Molecular interactions in cell adhesion complexes
    • Yamada K.M., and Geiger B. Molecular interactions in cell adhesion complexes. Curr. Opin. Cell. Biol. 9 76-85 (1997)
    • (1997) Curr. Opin. Cell. Biol. , vol.9 , Issue.76-85
    • Yamada, K.M.1    Geiger, B.2
  • 56
    • 0031440104 scopus 로고    scopus 로고
    • Molecular and functional analysis of cadherin-based adherens junctions
    • Yap A.S., Brieher W.M., and Gumbiner B.M. Molecular and functional analysis of cadherin-based adherens junctions. Ann. Rev. Cell. Dev. Biol. 13 119-146 (1997)
    • (1997) Ann. Rev. Cell. Dev. Biol. , vol.13 , Issue.119-146
    • Yap, A.S.1    Brieher, W.M.2    Gumbiner, B.M.3
  • 57
    • 0034757893 scopus 로고    scopus 로고
    • Components of cell matrix adhesions
    • Zamir E., and Geiger B. Components of cell matrix adhesions. J. Cell Sci. 114 (2001) 3577-3579
    • (2001) J. Cell Sci. , vol.114 , pp. 3577-3579
    • Zamir, E.1    Geiger, B.2
  • 59
    • 0033790713 scopus 로고    scopus 로고
    • Dynamics and segregation of cell-matrix adhesions in cultured fibroblasts
    • Zamir E., Katz M., Posen Y., Erez N., Yamada K.M., Katz B., et al. Dynamics and segregation of cell-matrix adhesions in cultured fibroblasts. Nature Cell Biol. 2 (2000) 191-196
    • (2000) Nature Cell Biol. , vol.2 , pp. 191-196
    • Zamir, E.1    Katz, M.2    Posen, Y.3    Erez, N.4    Yamada, K.M.5    Katz, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.