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Volumn 291, Issue 5, 2006, Pages

Disruption of α-actinin-integrin interactions at focal adhesions renders osteoblasts susceptible to apoptosis

Author keywords

Cytoskeleton; Nuclear factor B; Survival; Tumor necrosis factor

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; ALPHA ACTIN; ALPHA INTEGRIN; CASPASE 3; GREEN FLUORESCENT PROTEIN; HISTONE H2A; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN BCL 2; PROTEIN KINASE B; VINCULIN;

EID: 33751091524     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00113.2006     Document Type: Article
Times cited : (47)

References (56)
  • 1
    • 26444448463 scopus 로고    scopus 로고
    • The survival kinases Akt and Pim as potential pharmacological targets
    • Amaravadi R and Thompson CB. The survival kinases Akt and Pim as potential pharmacological targets. J Clin Invest 115: 2618-2624, 2005.
    • (2005) J Clin Invest , vol.115 , pp. 2618-2624
    • Amaravadi, R.1    Thompson, C.B.2
  • 2
    • 0034601436 scopus 로고    scopus 로고
    • The integrin-linked kinase (ILK) suppresses anoikis
    • Attwell S, Roskelley C, and Dedhar S. The integrin-linked kinase (ILK) suppresses anoikis. Oncogene 19: 3811-3815, 2000.
    • (2000) Oncogene , vol.19 , pp. 3811-3815
    • Attwell, S.1    Roskelley, C.2    Dedhar, S.3
  • 4
    • 0023196997 scopus 로고
    • Interaction of iodinated vinculin, metavinculin and α-actinin with cytoskeletal proteins
    • Belkin AM and Koteliansky VE. Interaction of iodinated vinculin, metavinculin and α-actinin with cytoskeletal proteins. FEBS Lett 220: 291-294, 1987.
    • (1987) FEBS Lett , vol.220 , pp. 291-294
    • Belkin, A.M.1    Koteliansky, V.E.2
  • 6
    • 0037204948 scopus 로고    scopus 로고
    • TNF-R1 signaling: A beautiful pathway
    • Chen G and Goeddel DV. TNF-R1 signaling: a beautiful pathway. Science 296: 1634-1635, 2002.
    • (2002) Science , vol.296 , pp. 1634-1635
    • Chen, G.1    Goeddel, D.V.2
  • 7
    • 0033046706 scopus 로고    scopus 로고
    • MEKK1 interacts with α-actinin and localizes to stress fibers and focal adhesions
    • Christerson LB, Vanderbilt CA, and Cobb MH. MEKK1 interacts with α-actinin and localizes to stress fibers and focal adhesions. Cell Motil Cytoskeleton 43: 186-198, 1999.
    • (1999) Cell Motil Cytoskeleton , vol.43 , pp. 186-198
    • Christerson, L.B.1    Vanderbilt, C.A.2    Cobb, M.H.3
  • 9
    • 33745726220 scopus 로고    scopus 로고
    • Trichostatin a sensitizes TRAIL-resistant myeloma cells by downregulation of the antiapoptotic Bcl-2 proteins
    • Fandy TE and Srivastava RK. Trichostatin A sensitizes TRAIL-resistant myeloma cells by downregulation of the antiapoptotic Bcl-2 proteins. Cancer Chemother Pharmacol: 1-7, 2006.
    • (2006) Cancer Chemother Pharmacol , pp. 1-7
    • Fandy, T.E.1    Srivastava, R.K.2
  • 10
    • 0034986471 scopus 로고    scopus 로고
    • Growth defects induced by perturbation of β1-integrin function in the mammary gland epithelium result from a lack of MAPK activation via the Shc and Akt pathways
    • Faraldo MM, Deugnier MA, Thiery JP, and Glukhova MA. Growth defects induced by perturbation of β1-integrin function in the mammary gland epithelium result from a lack of MAPK activation via the Shc and Akt pathways. EMBO Rep 2: 431-437, 2001.
    • (2001) EMBO Rep , vol.2 , pp. 431-437
    • Faraldo, M.M.1    Deugnier, M.A.2    Thiery, J.P.3    Glukhova, M.A.4
  • 11
    • 0034108868 scopus 로고    scopus 로고
    • MAP kinase pathway signalling is essential for extracellular matrix determined mammary epithelial cell survival
    • Finlay D, Healy V, Furlong F, O'Connell FC, Keon NK, and Martin F. MAP kinase pathway signalling is essential for extracellular matrix determined mammary epithelial cell survival. Cell Death Differ 7: 302-313, 2000.
    • (2000) Cell Death Differ , vol.7 , pp. 302-313
    • Finlay, D.1    Healy, V.2    Furlong, F.3    O'Connell, F.C.4    Keon, N.K.5    Martin, F.6
  • 12
    • 0035163237 scopus 로고    scopus 로고
    • Cooperative control of Akt phosphorylation, bcl-2 expression, and apoptosis by cytoskeletal microfilaments and microtubules in capillary endothelial cells
    • Flusberg DA, Numaguchi Y, and Ingber DE. Cooperative control of Akt phosphorylation, bcl-2 expression, and apoptosis by cytoskeletal microfilaments and microtubules in capillary endothelial cells. Mol Biol Cell 12: 3087-3094, 2001.
    • (2001) Mol Biol Cell , vol.12 , pp. 3087-3094
    • Flusberg, D.A.1    Numaguchi, Y.2    Ingber, D.E.3
  • 13
    • 0028057613 scopus 로고
    • Disruption of epithelial cell-matrix interactions induces apoptosis
    • Frisch SM and Francis H. Disruption of epithelial cell-matrix interactions induces apoptosis. J Cell Biol 124: 619-626, 1994.
    • (1994) J Cell Biol , vol.124 , pp. 619-626
    • Frisch, S.M.1    Francis, H.2
  • 15
    • 0030458602 scopus 로고    scopus 로고
    • A role for Jun-N-terminal kinase in anoikis; suppression by bcl-2 and crmA
    • Frisch SM, Vuori K, Kelaita D, and Sicks S. A role for Jun-N-terminal kinase in anoikis; suppression by bcl-2 and crmA. J Cell Biol 135: 1377-1382, 1996.
    • (1996) J Cell Biol , vol.135 , pp. 1377-1382
    • Frisch, S.M.1    Vuori, K.2    Kelaita, D.3    Sicks, S.4
  • 16
    • 0042707525 scopus 로고    scopus 로고
    • Tumor necrosis factor-induced nuclear factor κB activation is impaired in focal adhesion kinase-deficient fibroblasts
    • Funakoshi-Tago M, Sonoda Y, Tanaka S, Hashimoto K, Tago K, Tominaga S, and Kasahara T. Tumor necrosis factor-induced nuclear factor κB activation is impaired in focal adhesion kinase-deficient fibroblasts. J Biol Chem 278: 29359-29365, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 29359-29365
    • Funakoshi-Tago, M.1    Sonoda, Y.2    Tanaka, S.3    Hashimoto, K.4    Tago, K.5    Tominaga, S.6    Kasahara, T.7
  • 17
    • 0034879150 scopus 로고    scopus 로고
    • Transcriptional regulation of the BCL-X gene by NF-κB is an element of hypoxic responses in the rat brain
    • Glasgow JN, Qiu J, Rassin D, Grafe M, Wood T, and Perez-Pol JR. Transcriptional regulation of the BCL-X gene by NF-κB is an element of hypoxic responses in the rat brain. Neurochem Res 26: 647-659, 2001.
    • (2001) Neurochem Res , vol.26 , pp. 647-659
    • Glasgow, J.N.1    Qiu, J.2    Rassin, D.3    Grafe, M.4    Wood, T.5    Perez-Pol, J.R.6
  • 18
    • 0035800777 scopus 로고    scopus 로고
    • The cytoskeletal/non-muscle isoform of alphaactinin is phosphorylated on its actin-binding domain by the focal adhesion kinase
    • Izaguirre G, Aguirre L, Hu YP, Lee HY, Schlaepfer DD, Aneskievich BJ, and Haimovich B. The cytoskeletal/non-muscle isoform of alphaactinin is phosphorylated on its actin-binding domain by the focal adhesion kinase. J Biol Chem 276: 28676-28685, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 28676-28685
    • Izaguirre, G.1    Aguirre, L.2    Hu, Y.P.3    Lee, H.Y.4    Schlaepfer, D.D.5    Aneskievich, B.J.6    Haimovich, B.7
  • 19
    • 0028321948 scopus 로고
    • Aberrant gene expression in cultured mammalian bone cells demonstrates an osteoblast defect in osteopetrosis
    • Jackson ME, Shalhoub V, Lian JB, Stein GS, and Marks SC Jr. Aberrant gene expression in cultured mammalian bone cells demonstrates an osteoblast defect in osteopetrosis. J Cell Biochem 55: 366-372, 1994.
    • (1994) J Cell Biochem , vol.55 , pp. 366-372
    • Jackson, M.E.1    Shalhoub, V.2    Lian, J.B.3    Stein, G.S.4    Marks Jr., S.C.5
  • 20
    • 0035970008 scopus 로고    scopus 로고
    • Integrin-mediated mechanotransduction requires its dynamic interaction with specific extracellular matrix (ECM) ligands
    • Jalali S, del Pozo MA, Chen K, Miao H, Li Y, Schwartz MA, Shyy JY, and Chien S. Integrin-mediated mechanotransduction requires its dynamic interaction with specific extracellular matrix (ECM) ligands. Proc Natl Acad Sci USA 98: 1042-1046, 2001.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1042-1046
    • Jalali, S.1    Del Pozo, M.A.2    Chen, K.3    Miao, H.4    Li, Y.5    Schwartz, M.A.6    Shyy, J.Y.7    Chien, S.8
  • 21
    • 0031976864 scopus 로고    scopus 로고
    • Osteoblast programmed cell death (apoptosis): Modulation by growth factors and cytokines
    • Jilka RL, Weinstein RS, Bellido T, Parfitt AM, and Manolagas SC. Osteoblast programmed cell death (apoptosis): modulation by growth factors and cytokines. J Bone Miner Res 13: 793-802., 1998.
    • (1998) J Bone Miner Res , vol.13 , pp. 793-802
    • Jilka, R.L.1    Weinstein, R.S.2    Bellido, T.3    Parfitt, A.M.4    Manolagas, S.C.5
  • 22
    • 12544254440 scopus 로고    scopus 로고
    • αvβ Integrins play an essential role in BMP-2 induction of osteoblast differentiation
    • Lai CF and Cheng SL. αvβ Integrins play an essential role in BMP-2 induction of osteoblast differentiation. J Bone Miner Res 20: 330-340, 2005.
    • (2005) J Bone Miner Res , vol.20 , pp. 330-340
    • Lai, C.F.1    Cheng, S.L.2
  • 23
    • 0033571710 scopus 로고    scopus 로고
    • Extracellular regulated kinase (ERK) interaction with actin and the calponin homology (CH) domain of actin-binding proteins
    • Leinweber BD, Leavis PC, Grabarek Z, Wang CL, and Morgan KG. Extracellular regulated kinase (ERK) interaction with actin and the calponin homology (CH) domain of actin-binding proteins. Biochem J 344: 117-123, 1999.
    • (1999) Biochem J , vol.344 , pp. 117-123
    • Leinweber, B.D.1    Leavis, P.C.2    Grabarek, Z.3    Wang, C.L.4    Morgan, K.G.5
  • 25
    • 3042830441 scopus 로고    scopus 로고
    • Regulation of Bcl-2 proteins during anoikis and amorphosis
    • Martin SS and Vuori K. Regulation of Bcl-2 proteins during anoikis and amorphosis. Biochim Biophys Acta 1692: 145-157, 2004.
    • (2004) Biochim Biophys Acta , vol.1692 , pp. 145-157
    • Martin, S.S.1    Vuori, K.2
  • 27
    • 0242409906 scopus 로고    scopus 로고
    • Tumor necrosis factor-α: Molecular and cellular mechanisms in skeletal pathology
    • Nanes MS. Tumor necrosis factor-α: molecular and cellular mechanisms in skeletal pathology. Gene 321: 1-15, 2003.
    • (2003) Gene , vol.321 , pp. 1-15
    • Nanes, M.S.1
  • 28
    • 2442481067 scopus 로고    scopus 로고
    • α-Actinin revisited: A fresh look at an old player
    • Otey CA and Carpen O. α-Actinin revisited: a fresh look at an old player. Cell Motil Cytoskeleton 58: 104-111, 2004.
    • (2004) Cell Motil Cytoskeleton , vol.58 , pp. 104-111
    • Otey, C.A.1    Carpen, O.2
  • 29
    • 0025291522 scopus 로고
    • An interaction between α-actinin and the β1 integrin subunit in vitro
    • Otey CA, Pavalko FM, and Burridge K. An interaction between α-actinin and the β1 integrin subunit in vitro. J Cell Biol 111: 721-729, 1990.
    • (1990) J Cell Biol , vol.111 , pp. 721-729
    • Otey, C.A.1    Pavalko, F.M.2    Burridge, K.3
  • 30
    • 0034618039 scopus 로고    scopus 로고
    • Characterization of palladin, a novel protein localized to stress fibers and cell adhesions
    • Parast MM and Otey CA. Characterization of palladin, a novel protein localized to stress fibers and cell adhesions. J Cell Biol 150: 643-656, 2000.
    • (2000) J Cell Biol , vol.150 , pp. 643-656
    • Parast, M.M.1    Otey, C.A.2
  • 31
    • 0025734407 scopus 로고
    • Disruption of the actin cytoskeleton after microinjection of proteolytic fragments of alpha-actinin
    • Pavalko FM and Burridge K. Disruption of the actin cytoskeleton after microinjection of proteolytic fragments of alpha-actinin. J Cell Biol 114: 481-491, 1991.
    • (1991) J Cell Biol , vol.114 , pp. 481-491
    • Pavalko, F.M.1    Burridge, K.2
  • 34
    • 0030760375 scopus 로고    scopus 로고
    • CRP1, a LIM domain protein implicated in muscle differentiation, interacts with α-actinin
    • Pomies P, Louis HA, and Beckerle MC. CRP1, a LIM domain protein implicated in muscle differentiation, interacts with α-actinin. J Cell Biol 139: 157-168, 1997.
    • (1997) J Cell Biol , vol.139 , pp. 157-168
    • Pomies, P.1    Louis, H.A.2    Beckerle, M.C.3
  • 35
    • 3042558631 scopus 로고    scopus 로고
    • Formation of focal adhesions on fibronectin promotes fluid shear stress induction of COX-2 and PGE2 release in MC3T3-E1 osteoblasts
    • Ponik SM and Pavalko FM. Formation of focal adhesions on fibronectin promotes fluid shear stress induction of COX-2 and PGE2 release in MC3T3-E1 osteoblasts. J Appl Physiol 97: 135-142, 2004.
    • (2004) J Appl Physiol , vol.97 , pp. 135-142
    • Ponik, S.M.1    Pavalko, F.M.2
  • 36
    • 0032847386 scopus 로고    scopus 로고
    • Physiology and pathophysiology of bone remodeling
    • Raisz LG. Physiology and pathophysiology of bone remodeling. Clin Chem 45: 1353-1358, 1999.
    • (1999) Clin Chem , vol.45 , pp. 1353-1358
    • Raisz, L.G.1
  • 38
    • 0028049088 scopus 로고
    • FAK) and paxillin tyrosine phosphorylation in Swiss 3T3 cells. Bell-shaped dose response and cross-talk with bombesin
    • FAK) and paxillin tyrosine phosphorylation in Swiss 3T3 cells. Bell-shaped dose response and cross-talk with bombesin. J Biol Chem 269: 704-710, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 704-710
    • Rankin, S.1    Rozengurt, E.2
  • 39
    • 30944438284 scopus 로고    scopus 로고
    • Sensitization of prostate carcinoma cells to Apo2L/TRAIL by a Bcl-2 family protein inhibitor
    • Ray S, Bucur O, and Almasan A. Sensitization of prostate carcinoma cells to Apo2L/TRAIL by a Bcl-2 family protein inhibitor. Apoptosis 10: 1411-1418, 2005.
    • (2005) Apoptosis , vol.10 , pp. 1411-1418
    • Ray, S.1    Bucur, O.2    Almasan, A.3
  • 40
    • 4344568083 scopus 로고    scopus 로고
    • Bone safety of long-term bisphosphonate treatment
    • Rodan G, Reszka A, Golub E, and Rizzoli R. Bone safety of long-term bisphosphonate treatment. Curr Med Res Opin 20: 1291-1300, 2004.
    • (2004) Curr Med Res Opin , vol.20 , pp. 1291-1300
    • Rodan, G.1    Reszka, A.2    Golub, E.3    Rizzoli, R.4
  • 41
    • 0023198311 scopus 로고
    • A solid-phase method for the quantitation of protein in the presence of sodium dodecyl sulfate and other interfering substances
    • Sheffield JB, Graff D, and Li HP. A solid-phase method for the quantitation of protein in the presence of sodium dodecyl sulfate and other interfering substances. Anal Biochem 166: 49-54, 1987.
    • (1987) Anal Biochem , vol.166 , pp. 49-54
    • Sheffield, J.B.1    Graff, D.2    Li, H.P.3
  • 43
    • 0036796781 scopus 로고    scopus 로고
    • Get a ligand, get a life: Integrins, signaling and cell survival
    • Stupack DG and Cheresh DA. Get a ligand, get a life: integrins, signaling and cell survival. J Cell Sci 115: 3729-3738, 2002.
    • (2002) J Cell Sci , vol.115 , pp. 3729-3738
    • Stupack, D.G.1    Cheresh, D.A.2
  • 45
    • 0023766145 scopus 로고
    • Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II
    • Sturgill TW, Ray LB, Erikson E, and Maller JL. Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II. Nature 334: 715-718, 1988.
    • (1988) Nature , vol.334 , pp. 715-718
    • Sturgill, T.W.1    Ray, L.B.2    Erikson, E.3    Maller, J.L.4
  • 46
    • 0036689830 scopus 로고    scopus 로고
    • NF-κB activation and inhibition: A review
    • Sun Z and Andersson R. NF-κB activation and inhibition: a review. Shock 18: 99-106, 2002.
    • (2002) Shock , vol.18 , pp. 99-106
    • Sun, Z.1    Andersson, R.2
  • 48
    • 0345561544 scopus 로고    scopus 로고
    • Tumor necrosis factor induces Bcl-2 and Bcl-x expression through NFκB activation in primary hippocampal neurons
    • Tamatani M, Che YH, Matsuzaki H, Ogawa S, Okado H, Miyake S, Mizuno T, and Tohyama M. Tumor necrosis factor induces Bcl-2 and Bcl-x expression through NFκB activation in primary hippocampal neurons. J Biol Chem 274: 8531-8538, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 8531-8538
    • Tamatani, M.1    Che, Y.H.2    Matsuzaki, H.3    Ogawa, S.4    Okado, H.5    Miyake, S.6    Mizuno, T.7    Tohyama, M.8
  • 49
    • 33644793352 scopus 로고    scopus 로고
    • Adenoviral transgene expression enhanced by cotreatment with etoposide in cultured cells
    • 828, 830, passim
    • Triplett JW, Herring BP, and Pavalko FM. Adenoviral transgene expression enhanced by cotreatment with etoposide in cultured cells. Biotechniques 39: 826, 828, 830, passim, 2005.
    • (2005) Biotechniques , vol.39 , pp. 826
    • Triplett, J.W.1    Herring, B.P.2    Pavalko, F.M.3
  • 50
    • 0036672790 scopus 로고    scopus 로고
    • The inner lives of focal adhesions
    • Wehrle-Haller B and Imhof B. The inner lives of focal adhesions. Trends Cell Biol 12: 382-389, 2002.
    • (2002) Trends Cell Biol , vol.12 , pp. 382-389
    • Wehrle-Haller, B.1    Imhof, B.2
  • 52
    • 3543023861 scopus 로고    scopus 로고
    • Focal adhesion kinase is upstream of phosphatidylinositol 3-kinase/Akt in regulating fibroblast survival in response to contraction of type I collagen matrices via a β1 integrin viability signaling pathway
    • Xia H, Nho RS, Kahm J, Kleidon J, and Henke CA. Focal adhesion kinase is upstream of phosphatidylinositol 3-kinase/Akt in regulating fibroblast survival in response to contraction of type I collagen matrices via a β1 integrin viability signaling pathway. J Biol Chem 279: 33024-33034, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 33024-33034
    • Xia, H.1    Nho, R.S.2    Kahm, J.3    Kleidon, J.4    Henke, C.A.5
  • 55
    • 0028983407 scopus 로고
    • The α5β 1 integrin supports survival of cells on fibronectin and up-regulates Bcl-2 expression
    • Zhang Z, Vuori K, Reed JC, and Ruoslahti E. The α5β 1 integrin supports survival of cells on fibronectin and up-regulates Bcl-2 expression. Proc Natl Acad Sci USA 92: 6161-6165, 1995.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6161-6165
    • Zhang, Z.1    Vuori, K.2    Reed, J.C.3    Ruoslahti, E.4
  • 56
    • 0033558215 scopus 로고    scopus 로고
    • The prosurvival Bcl-2 homolog Bfl-1/A1 is a direct transcriptional target of NF-κB that blocks TNFα-induced apoptosis
    • Zong WX, Edelstein LC, Chen C, Bash J, and Gelinas C. The prosurvival Bcl-2 homolog Bfl-1/A1 is a direct transcriptional target of NF-κB that blocks TNFα-induced apoptosis. Genes Dev 13: 382-387, 1999.
    • (1999) Genes Dev , vol.13 , pp. 382-387
    • Zong, W.X.1    Edelstein, L.C.2    Chen, C.3    Bash, J.4    Gelinas, C.5


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