메뉴 건너뛰기




Volumn 290, Issue 42, 2015, Pages 25356-25373

Tumor necrosis factor-α (TNFα)-induced ceramide generation via ceramide synthases regulates loss of focal adhesion kinase (FAK) and programmed cell death

Author keywords

[No Author keywords available]

Indexed keywords

ADHESION; BIOCHEMISTRY; CELL DEATH; CELL MEMBRANES; CELLS; CYTOLOGY; ENZYMES;

EID: 84944407529     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.658658     Document Type: Article
Times cited : (55)

References (94)
  • 1
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr, J. F., Wyllie, A. H., and Currie, A. R. (1972) Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26, 239-257
    • (1972) Br. J.Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 2
    • 58149296552 scopus 로고    scopus 로고
    • Tumor resistance to apoptosis
    • Fulda, S. (2009) Tumor resistance to apoptosis. Int. J. Cancer 124, 511-515
    • (2009) Int. J.Cancer , vol.124 , pp. 511-515
    • Fulda, S.1
  • 3
    • 0019225636 scopus 로고
    • Cell death: The significance of apoptosis
    • Wyllie, A. H., Kerr, J. F., and Currie, A. R. (1980) Cell death: the significance of apoptosis. Int. Rev. Cytol. 68, 251-306
    • (1980) Int. Rev.Cytol. , vol.68 , pp. 251-306
    • Wyllie, A.H.1    Kerr, J.F.2    Currie, A.R.3
  • 4
    • 78249253033 scopus 로고    scopus 로고
    • Secondary necrosis: The natural outcome of the complete apoptotic program
    • Silva, M. T. (2010) Secondary necrosis: the natural outcome of the complete apoptotic program. FEBS Lett. 584, 4491-4499
    • (2010) FEBS Lett , vol.584 , pp. 4491-4499
    • Silva, M.T.1
  • 5
    • 0018071383 scopus 로고
    • Morphological aspects of glucocorticoid-induced cell death in human lymphoblastoid cells
    • Robertson, A. M., Bird, C. C., Waddell, A. W., and Currie, A. R. (1978) Morphological aspects of glucocorticoid-induced cell death in human lymphoblastoid cells. J. Pathol. 126, 181-187
    • (1978) J. Pathol. , vol.126 , pp. 181-187
    • Robertson, A.M.1    Bird, C.C.2    Waddell, A.W.3    Currie, A.R.4
  • 8
    • 33845294390 scopus 로고    scopus 로고
    • A house divided: Ceramide, sphingosine, and sphingosine-1-phosphate in programmed cell death
    • Taha, T. A., Mullen, T. D., and Obeid, L. M. (2006) A house divided: ceramide, sphingosine, and sphingosine-1-phosphate in programmed cell death. Biochim. Biophys. Acta 1758, 2027-2036
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 2027-2036
    • Taha, T.A.1    Mullen, T.D.2    Obeid, L.M.3
  • 9
    • 0037203342 scopus 로고    scopus 로고
    • Ceramide in apoptosis: N overview and current perspectives
    • Pettus, B. J., Chalfant, C. E., and Hannun, Y. A. (2002) Ceramide in apoptosis: n overview and current perspectives. Biochim. Biophys. Acta 1585, 114-125
    • (2002) Biochim. Biophys.Acta , vol.1585 , pp. 114-125
    • Pettus, B.J.1    Chalfant, C.E.2    Hannun, Y.A.3
  • 10
    • 79955533796 scopus 로고    scopus 로고
    • Ceramide synthase-dependent ceramide generation and programmed cell death: Involvement of salvage pathway in regulating postmitochondrial events
    • Mullen, T. D., Jenkins, R. W., Clarke, C. J., Bielawski, J., Hannun, Y. A., and Obeid, L. M. (2011) Ceramide synthase-dependent ceramide generation and programmed cell death: involvement of salvage pathway in regulating postmitochondrial events. J. Biol. Chem. 286, 15929-15942
    • (2011) J. Biol. Chem. , vol.286 , pp. 15929-15942
    • Mullen, T.D.1    Jenkins, R.W.2    Clarke, C.J.3    Bielawski, J.4    Hannun, Y.A.5    Obeid, L.M.6
  • 11
    • 84860507660 scopus 로고    scopus 로고
    • Ceramide and apoptosis: Exploring the enigmatic connections between sphingolipid metabolism and programmed cell death
    • Mullen, T. D., and Obeid, L. M. (2012) Ceramide and apoptosis: exploring the enigmatic connections between sphingolipid metabolism and programmed cell death. Anti-cancer Agents Med. Chem. 12, 340-363
    • (2012) Anti-Cancer Agents Med. Chem. , vol.12 , pp. 340-363
    • Mullen, T.D.1    Obeid, L.M.2
  • 14
    • 42249105215 scopus 로고    scopus 로고
    • The sphingolipid salvage pathway in ceramide metabolism and signaling
    • Kitatani, K., Idkowiak-Baldys, J., and Hannun, Y. A. (2008) The sphingolipid salvage pathway in ceramide metabolism and signaling. Cell. Signal. 20, 1010-1018
    • (2008) Cell. Signal. , vol.20 , pp. 1010-1018
    • Kitatani, K.1    Idkowiak-Baldys, J.2    Hannun, Y.A.3
  • 15
    • 80051514415 scopus 로고    scopus 로고
    • Many ceramides
    • Hannun, Y. A., and Obeid, L. M. (2011) Many ceramides. J. Biol. Chem. 286, 27855-27862
    • (2011) J. Biol.Chem. , vol.286 , pp. 27855-27862
    • Hannun, Y.A.1    Obeid, L.M.2
  • 16
    • 0038641944 scopus 로고    scopus 로고
    • Killing tumours by ceramide-induced apoptosis: A critique of available drugs
    • Radin, N. S. (2003) Killing tumours by ceramide-induced apoptosis: a critique of available drugs. Biochem. J. 371, 243-256
    • (2003) Biochem. J. , vol.371 , pp. 243-256
    • Radin, N.S.1
  • 17
    • 78049498376 scopus 로고    scopus 로고
    • Ceramide synthases: Roles in cell physiology and signaling
    • Stiban, J., Tidhar, R., and Futerman, A. H. (2010) Ceramide synthases: roles in cell physiology and signaling. Adv. Exp. Med. Biol. 688, 60-71
    • (2010) Adv. Exp.Med. Biol. , vol.688 , pp. 60-71
    • Stiban, J.1    Tidhar, R.2    Futerman, A.H.3
  • 18
    • 0037144554 scopus 로고    scopus 로고
    • Upstream of growth and differentiation factor 1 (uog1), a mammalian homolog of the yeast longevity assurance gene 1 (LAG1), regulates N-stearoyl-sphinganine (C18-(dihydro)ceramide) synthesis in a fumonisin B1-independent manner in mammalian cells
    • Venkataraman, K., Riebeling, C., Bodennec, J., Riezman, H., Allegood, J. C., Sullards, M. C., Merrill, A. H., Jr., and Futerman, A. H. (2002) Upstream of growth and differentiation factor 1 (uog1), a mammalian homolog of the yeast longevity assurance gene 1 (LAG1), regulates N-stearoyl-sphinganine (C18-(dihydro)ceramide) synthesis in a fumonisin B1-independent manner in mammalian cells. J. Biol. Chem. 277, 35642-35649
    • (2002) J. Biol. Chem. , vol.277 , pp. 35642-35649
    • Venkataraman, K.1    Riebeling, C.2    Bodennec, J.3    Riezman, H.4    Allegood, J.C.5    Sullards, M.C.6    Merrill, J.A.H.7    Futerman, A.H.8
  • 19
    • 41949140023 scopus 로고    scopus 로고
    • Characterization of ceramide synthase 2: Tissue distribution, substrate specificity, and inhibition by sphingosine 1-phosphate
    • Laviad, E. L., Albee, L., Pankova-Kholmyansky, I., Epstein, S., Park, H., Merrill, A. H., Jr., and Futerman, A. H. (2008) Characterization of ceramide synthase 2: tissue distribution, substrate specificity, and inhibition by sphingosine 1-phosphate. J. Biol. Chem. 283, 5677-5684
    • (2008) J. Biol. Chem. , vol.283 , pp. 5677-5684
    • Laviad, E.L.1    Albee, L.2    Pankova-Kholmyansky, I.3    Epstein, S.4    Park, H.5    Merrill, J.A.H.6    Futerman, A.H.7
  • 20
    • 0242353271 scopus 로고    scopus 로고
    • Two mammalian longevity assurance gene (LAG1) family members, trh1 and trh4, regulate dihydroceramide synthesis using different fatty acyl-CoA donors
    • Riebeling, C., Allegood, J. C., Wang, E., Merrill, A. H., Jr., and Futerman, A. H. (2003) Two mammalian longevity assurance gene (LAG1) family members, trh1 and trh4, regulate dihydroceramide synthesis using different fatty acyl-CoA donors. J. Biol. Chem. 278, 43452-43459
    • (2003) J. Biol. Chem. , vol.278 , pp. 43452-43459
    • Riebeling, C.1    Allegood, J.C.2    Wang, E.3    Merrill, J.A.H.4    Futerman, A.H.5
  • 21
    • 23944483995 scopus 로고    scopus 로고
    • Mammalian Lass6 and its related family members regulate synthesis of specific ceramides
    • Mizutani, Y., Kihara, A., and Igarashi, Y. (2005) Mammalian Lass6 and its related family members regulate synthesis of specific ceramides. Biochem. J. 390, 263-271
    • (2005) Biochem. J. , vol.390 , pp. 263-271
    • Mizutani, Y.1    Kihara, A.2    Igarashi, Y.3
  • 22
    • 0029148660 scopus 로고
    • Ceramide synthase mediates daunorubicin-induced apoptosis: An alternative mechanism for generating death signals
    • Bose, R., Verheij, M., Haimovitz-Friedman, A., Scotto, K., Fuks, Z., and Kolesnick, R. (1995) Ceramide synthase mediates daunorubicin-induced apoptosis: an alternative mechanism for generating death signals. Cell 82, 405-414
    • (1995) Cell , vol.82 , pp. 405-414
    • Bose, R.1    Verheij, M.2    Haimovitz-Friedman, A.3    Scotto, K.4    Fuks, Z.5    Kolesnick, R.6
  • 23
    • 59649110566 scopus 로고    scopus 로고
    • De novo ceramide synthesis is responsible for the anti-tumor properties of camptothecin and doxorubicin in follicular thyroid carcinoma
    • Rath, G., Schneider, C., Langlois, B., Sartelet, H., Morjani, H., Btaouri, H. E., Dedieu, S., and Martiny, L. (2009) De novo ceramide synthesis is responsible for the anti-tumor properties of camptothecin and doxorubicin in follicular thyroid carcinoma. Int. J. Biochem. Cell Biol. 41, 1165-1172
    • (2009) Int. J.Biochem. Cell Biol. , vol.41 , pp. 1165-1172
    • Rath, G.1    Schneider, C.2    Langlois, B.3    Sartelet, H.4    Morjani, H.5    Btaouri, H.E.6    Dedieu, S.7    Martiny, L.8
  • 24
    • 0033551661 scopus 로고    scopus 로고
    • Involvement of protein kinase C-β and ceramide in tumor necrosis factor-α-induced but not Fas-induced apoptosis of human myeloid leukemia cells
    • Laouar, A., Glesne, D., and Huberman, E. (1999) Involvement of protein kinase C-β and ceramide in tumor necrosis factor-α-induced but not Fas-induced apoptosis of human myeloid leukemia cells. J. Biol. Chem. 274, 23526-23534
    • (1999) J. Biol. Chem. , vol.274 , pp. 23526-23534
    • Laouar, A.1    Glesne, D.2    Huberman, E.3
  • 26
    • 61349193762 scopus 로고    scopus 로고
    • Ceramide synthase 6 modulates TRAIL sensitivity and nuclear translocation of active caspase-3 in colon cancer cells
    • White-Gilbertson, S., Mullen, T., Senkal, C., Lu, P., Ogretmen, B., Obeid, L., and Voelkel-Johnson, C. (2009) Ceramide synthase 6 modulates TRAIL sensitivity and nuclear translocation of active caspase-3 in colon cancer cells. Oncogene 28, 1132-1141
    • (2009) Oncogene , vol.28 , pp. 1132-1141
    • White-Gilbertson, S.1    Mullen, T.2    Senkal, C.3    Lu, P.4    Ogretmen, B.5    Obeid, L.6    Voelkel-Johnson, C.7
  • 28
    • 0026445719 scopus 로고
    • Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: A role in cytoskeletal assembly
    • Burridge, K., Turner, C. E., and Romer, L. H. (1992) Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly. J. Cell Biol. 119, 893-903
    • (1992) J. Cell Biol. , vol.119 , pp. 893-903
    • Burridge, K.1    Turner, C.E.2    Romer, L.H.3
  • 29
    • 0031257749 scopus 로고    scopus 로고
    • Focal adhesion kinase in integrin signaling
    • Guan, J. L. (1997) Focal adhesion kinase in integrin signaling. Matrix Biol. 16, 195-200
    • (1997) Matrix Biol. , vol.16 , pp. 195-200
    • Guan, J.L.1
  • 30
    • 84897437048 scopus 로고    scopus 로고
    • Targeting FAK in human cancer: From finding to first clinical trials
    • Golubovskaya, V. M. (2014) Targeting FAK in human cancer: from finding to first clinical trials. Front. Biosci. 19, 687-706
    • (2014) Front. Biosci. , vol.19 , pp. 687-706
    • Golubovskaya, V.M.1
  • 31
    • 69349085098 scopus 로고    scopus 로고
    • The direct effect of focal adhesion kinase (FAK), dominant-negative FAK, FAK-CD and FAK siRNA on gene expression and human MCF-7 breast cancer cell tumorigenesis
    • Golubovskaya, V. M., Zheng, M., Zhang, L., Li, J. L., and Cance, W. G. (2009) The direct effect of focal adhesion kinase (FAK), dominant-negative FAK, FAK-CD and FAK siRNA on gene expression and human MCF-7 breast cancer cell tumorigenesis. BMC Cancer 9, 280
    • (2009) BMC Cancer , vol.9 , pp. 280
    • Golubovskaya, V.M.1    Zheng, M.2    Zhang, L.3    Li, J.L.4    Cance, W.G.5
  • 33
    • 33745684527 scopus 로고    scopus 로고
    • Metastasis: A question of life or death
    • Mehlen, P., and Puisieux, A. (2006) Metastasis: a question of life or death. Nat. Rev. Cancer 6, 449-458
    • (2006) Nat. Rev.Cancer , vol.6 , pp. 449-458
    • Mehlen, P.1    Puisieux, A.2
  • 34
    • 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, E. W. (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
  • 35
    • 84898850082 scopus 로고    scopus 로고
    • Inhibition of focal adhesion kinase induces apoptosis in human osteosarcoma SAOS-2 cells
    • Wang, J., Zu, J., Xu, G., Zhao, W., and Jinglong, Y. (2014) Inhibition of focal adhesion kinase induces apoptosis in human osteosarcoma SAOS-2 cells. Tumour Biol. 35, 1551-1556
    • (2014) Tumour Biol. , vol.35 , pp. 1551-1556
    • Wang, J.1    Zu, J.2    Xu, G.3    Zhao, W.4    Jinglong, Y.5
  • 36
    • 0038005805 scopus 로고    scopus 로고
    • Focal adhesion kinase N-terminus in breast carcinoma cells induces rounding, detachment and apoptosis
    • Beviglia, L., Golubovskaya, V., Xu, L., Yang, X., Craven, R. J., and Cance, W. G. (2003) Focal adhesion kinase N-terminus in breast carcinoma cells induces rounding, detachment and apoptosis. Biochem. J. 373, 201-210
    • (2003) Biochem. J. , vol.373 , pp. 201-210
    • Beviglia, L.1    Golubovskaya, V.2    Xu, L.3    Yang, X.4    Craven, R.J.5    Cance, W.G.6
  • 37
    • 0030867842 scopus 로고    scopus 로고
    • Cleavage of focal adhesion kinase by caspases during apoptosis
    • Wen, L. P., Fahrni, J. A., Troie, S., Guan, J. L., Orth, K., and Rosen, G. D. (1997) Cleavage of focal adhesion kinase by caspases during apoptosis. J. Biol. Chem. 272, 26056-26061
    • (1997) J. Biol.Chem. , vol.272 , pp. 26056-26061
    • Wen, L.P.1    Fahrni, J.A.2    Troie, S.3    Guan, J.L.4    Orth, K.5    Rosen, G.D.6
  • 39
    • 0032479435 scopus 로고    scopus 로고
    • Caspases cleave focal adhesion kinase during apoptosis to generate a FRNK-like polypeptide
    • Gervais, F. G., Thornberry, N. A., Ruffolo, S. C., Nicholson, D. W., and Roy, S. (1998) Caspases cleave focal adhesion kinase during apoptosis to generate a FRNK-like polypeptide. J. Biol. Chem. 273, 17102-17108
    • (1998) J. Biol. Chem. , vol.273 , pp. 17102-17108
    • Gervais, F.G.1    Thornberry, N.A.2    Ruffolo, S.C.3    Nicholson, D.W.4    Roy, S.5
  • 40
    • 33746271951 scopus 로고    scopus 로고
    • Simultaneous quantitative analysis of bioactive sphingolipids by high-performance liquid chromatography-tandem mass spectrometry
    • Bielawski, J., Szulc, Z. M., Hannun, Y. A., and Bielawska, A. (2006) Simultaneous quantitative analysis of bioactive sphingolipids by high-performance liquid chromatography-tandem mass spectrometry. Methods 39, 82-91
    • (2006) Methods , vol.39 , pp. 82-91
    • Bielawski, J.1    Szulc, Z.M.2    Hannun, Y.A.3    Bielawska, A.4
  • 42
    • 33847376437 scopus 로고    scopus 로고
    • Role of human longevity assurance gene 1 and C18-ceramide in chemotherapy-inducedcell death in human head and neck squamous cell carcinomas
    • Senkal, C. E., Ponnusamy, S., Rossi, M. J., Bialewski, J., Sinha, D., Jiang, J. C., Jazwinski, S. M., Hannun, Y. A., and Ogretmen, B. (2007) Role of human longevity assurance gene 1 and C18-ceramide in chemotherapy-inducedcell death in human head and neck squamous cell carcinomas. Mol. Cancer Ther. 6, 712-722
    • (2007) Mol. Cancer Ther. , vol.6 , pp. 712-722
    • Senkal, C.E.1    Ponnusamy, S.2    Rossi, M.J.3    Bialewski, J.4    Sinha, D.5    Jiang, J.C.6    Jazwinski, S.M.7    Hannun, Y.A.8    Ogretmen, B.9
  • 43
    • 84877139062 scopus 로고    scopus 로고
    • Folate stress induces apoptosis via p53-dependent de novo ceramide synthesis and up-regulation of ceramide synthase 6
    • Hoeferlin, L. A., Fekry, B., Ogretmen, B., Krupenko, S. A., and Krupenko, N. I. (2013) Folate stress induces apoptosis via p53-dependent de novo ceramide synthesis and up-regulation of ceramide synthase 6. J. Biol. Chem. 288, 12880-12890
    • (2013) J. Biol. Chem. , vol.288 , pp. 12880-12890
    • Hoeferlin, L.A.1    Fekry, B.2    Ogretmen, B.3    Krupenko, S.A.4    Krupenko, N.I.5
  • 44
    • 0035920146 scopus 로고    scopus 로고
    • Activation of pro-death Bcl-2 family proteins and mitochondria apoptosis pathway in tumor necrosis factor-ô-induced liver injury
    • Zhao, Y., Li, S., Childs, E. E., Kuharsky, D. K., and Yin, X. M. (2001) Activation of pro-death Bcl-2 family proteins and mitochondria apoptosis pathway in tumor necrosis factor-ô-induced liver injury. J. Biol. Chem. 276, 27432-27440
    • (2001) J. Biol. Chem. , vol.276 , pp. 27432-27440
    • Zhao, Y.1    Li, S.2    Childs, E.E.3    Kuharsky, D.K.4    Yin, X.M.5
  • 45
    • 0033534446 scopus 로고    scopus 로고
    • Caspase cleaved BID targets mitochondria and is required for cytochrome c release, while BCL-XL prevents this release but not tumor necrosis factor- R1/Fas death
    • Gross, A., Yin, X. M., Wang, K., Wei, M. C., Jockel, J., Milliman, C., Erdjument-Bromage, H., Tempst, P., and Korsmeyer, S. J. (1999) Caspase cleaved BID targets mitochondria and is required for cytochrome c release, while BCL-XL prevents this release but not tumor necrosis factor- R1/Fas death. J. Biol. Chem. 274, 1156-1163
    • (1999) J. Biol. Chem. , vol.274 , pp. 1156-1163
    • Gross, A.1    Yin, X.M.2    Wang, K.3    Wei, M.C.4    Jockel, J.5    Milliman, C.6    Erdjument-Bromage, H.7    Tempst, P.8    Korsmeyer, S.J.9
  • 46
    • 34250308322 scopus 로고    scopus 로고
    • Apoptosis: A review of programmed cell death
    • Elmore, S. (2007) Apoptosis: a review of programmed cell death. Toxicol. Pathol. 35, 495-516
    • (2007) Toxicol. Pathol. , vol.35 , pp. 495-516
    • Elmore, S.1
  • 47
    • 0034440818 scopus 로고    scopus 로고
    • Proteases for cell suicide: Functions and regulation of caspases
    • Chang, H. Y., and Yang, X. (2000) Proteases for cell suicide: functions and regulation of caspases. Microbiol. Mol. Biol. Rev. 64, 821-846
    • (2000) Microbiol. Mol.Biol. Rev. , vol.64 , pp. 821-846
    • Chang, H.Y.1    Yang, X.2
  • 48
    • 0034730632 scopus 로고    scopus 로고
    • The focal adhesion kinase suppresses transformation-associated, anchorage-independent apoptosis in human breast cancer cells: Involvement of death receptor-related signaling pathways
    • Xu, L. H., Yang, X., Bradham, C. A., Brenner, D. A., Baldwin, A. S., Jr., Craven, R. J., and Cance, W. G. (2000) The focal adhesion kinase suppresses transformation-associated, anchorage-independent apoptosis in human breast cancer cells: involvement of death receptor-related signaling pathways. J. Biol. Chem. 275, 30597-30604
    • (2000) J. Biol. Chem. , vol.275 , pp. 30597-30604
    • Xu, L.H.1    Yang, X.2    Bradham, C.A.3    Brenner, D.A.4    Baldwin, S.A.5    Craven, R.J.6    Cance, W.G.7
  • 49
    • 0032443850 scopus 로고    scopus 로고
    • The COOH-terminal domain of the focal adhesion kinase induces loss of adhesion and cell death in human tumor cells
    • Xu, L. H., Yang, X., Craven, R. J., and Cance, W. G. (1998) The COOH-terminal domain of the focal adhesion kinase induces loss of adhesion and cell death in human tumor cells. Cell Growth Differ. 9, 999-1005
    • (1998) Cell Growth Differ. , vol.9 , pp. 999-1005
    • Xu, L.H.1    Yang, X.2    Craven, R.J.3    Cance, W.G.4
  • 50
    • 0041426730 scopus 로고    scopus 로고
    • Simultaneous inhibition of focal adhesion kinase and SRC enhances detachment and apoptosis in colon cancer cell lines
    • Golubovskaya, V. M., Gross, S., Kaur, A. S., Wilson, R. I., Xu, L. H., Yang, X. H., and Cance, W. G. (2003) Simultaneous inhibition of focal adhesion kinase and SRC enhances detachment and apoptosis in colon cancer cell lines. Mol. Cancer Res. 1, 755-764
    • (2003) Mol. Cancer Res. , vol.1 , pp. 755-764
    • Golubovskaya, V.M.1    Gross, S.2    Kaur, A.S.3    Wilson, R.I.4    Xu, L.H.5    Yang, X.H.6    Cance, W.G.7
  • 51
    • 33845569198 scopus 로고    scopus 로고
    • Analysis of phosphorylation sites on focal adhesion kinase using nanospray liquid chromatography/ multiple reaction monitoring mass spectrometry
    • Ciccimaro, E., Hevko, J., and Blair, I. A. (2006) Analysis of phosphorylation sites on focal adhesion kinase using nanospray liquid chromatography/ multiple reaction monitoring mass spectrometry. Rapid Commun. Mass Spectrom. 20, 3681-3692
    • (2006) Rapid Commun.Mass Spectrom , vol.20 , pp. 3681-3692
    • Ciccimaro, E.1    Hevko, J.2    Blair, I.A.3
  • 53
    • 2942581328 scopus 로고    scopus 로고
    • Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex I of the electron transport chain
    • Ricci, J. E., Muñoz-Pinedo, C., Fitzgerald, P., Bailly-Maitre, B., Perkins, G. A., Yadava, N., Scheffler, I. E., Ellisman, M. H., and Green, D. R. (2004) Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex I of the electron transport chain. Cell 117, 773-786
    • (2004) Cell , vol.117 , pp. 773-786
    • Ricci, J.E.1    Muñoz-Pinedo, C.2    Fitzgerald, P.3    Bailly-Maitre, B.4    Perkins, G.A.5    Yadava, N.6    Scheffler, I.E.7    Ellisman, M.H.8    Green, D.R.9
  • 55
    • 84930926871 scopus 로고    scopus 로고
    • In vivo toxicity, metabolism and pharmacokinetic properties of FAK inhibitor 14 or Y15 (1,2,4,5-benzenetetramine tetrahydrochloride)
    • Golubovskaya, V., Curtin, L., Groman, A., Sexton, S., and Cance, W. G. (2015) In vivo toxicity, metabolism and pharmacokinetic properties of FAK inhibitor 14 or Y15 (1,2,4,5-benzenetetramine tetrahydrochloride). Arch. Toxicol. 89, 1095-1101
    • (2015) Arch. Toxicol. , vol.89 , pp. 1095-1101
    • Golubovskaya, V.1    Curtin, L.2    Groman, A.3    Sexton, S.4    Cance, W.G.5
  • 56
    • 84874031013 scopus 로고    scopus 로고
    • Pharmacologic blockade of FAK autophosphorylation decreases human glioblastoma tumor growth and synergizes with temozolomide
    • Golubovskaya, V. M., Huang, G., Ho, B., Yemma, M., Morrison, C. D., Lee, J., Eliceiri, B. P., and Cance, W. G. (2013) Pharmacologic blockade of FAK autophosphorylation decreases human glioblastoma tumor growth and synergizes with temozolomide. Mol. Cancer Ther. 12, 162-172
    • (2013) Mol. Cancer Ther. , vol.12 , pp. 162-172
    • Golubovskaya, V.M.1    Huang, G.2    Ho, B.3    Yemma, M.4    Morrison, C.D.5    Lee, J.6    Eliceiri, B.P.7    Cance, W.G.8
  • 57
    • 84907494469 scopus 로고    scopus 로고
    • FAK inhibition with small molecule inhibitor Y15 decreases viability, clonogenicity, and cell attachment in thyroid cancer cell lines and synergizes with targeted therapeutics
    • O'Brien, S., Golubovskaya, V. M., Conroy, J., Liu, S., Wang, D., Liu, B., and Cance, W. G. (2014) FAK inhibition with small molecule inhibitor Y15 decreases viability, clonogenicity, and cell attachment in thyroid cancer cell lines and synergizes with targeted therapeutics. Oncotarget 5, 7945-7959
    • (2014) Oncotarget , vol.5 , pp. 7945-7959
    • O'Brien, S.1    Golubovskaya, V.M.2    Conroy, J.3    Liu, S.4    Wang, D.5    Liu, B.6    Cance, W.G.7
  • 62
    • 70849112199 scopus 로고    scopus 로고
    • AMPK inhibitor Compound C stimulates ceramide production and promotes Bax redistribution and apoptosis in MCF7 breast carcinoma cells
    • Jin, J., Mullen, T. D., Hou, Q., Bielawski, J., Bielawska, A., Zhang, X., Obeid, L. M., Hannun, Y. A., and Hsu, Y. T. (2009) AMPK inhibitor Compound C stimulates ceramide production and promotes Bax redistribution and apoptosis in MCF7 breast carcinoma cells. J. Lipid Res. 50, 2389-2397
    • (2009) J. Lipid Res. , vol.50 , pp. 2389-2397
    • Jin, J.1    Mullen, T.D.2    Hou, Q.3    Bielawski, J.4    Bielawska, A.5    Zhang, X.6    Obeid, L.M.7    Hannun, Y.A.8    Hsu, Y.T.9
  • 63
    • 0036300687 scopus 로고    scopus 로고
    • Persistence and reversibility of the elevation in free sphingoid bases induced by fumonisin inhibition of ceramide ynthase
    • Enongene, E. N., Sharma, R. P., Bhandari, N., Miller, J. D., Meredith, F. I., Voss, K. A., and Riley, R. T. (2002) Persistence and reversibility of the elevation in free sphingoid bases induced by fumonisin inhibition of ceramide ynthase. Toxicol. Sci. 67, 173-181
    • (2002) Toxicol. Sci. , vol.67 , pp. 173-181
    • Enongene, E.N.1    Sharma, R.P.2    Bhandari, N.3    Miller, J.D.4    Meredith, F.I.5    Voss, K.A.6    Riley, R.T.7
  • 66
    • 0037066756 scopus 로고    scopus 로고
    • Biochemical mecha- nisms of the generation of endogenous long chain ceramide in response to exogenous short chain ceramide in the A549 human lung adenocarcinoma cell line: Role for endogenous ceramide in mediating the action of exogenous ceramide
    • Ogretmen, B., Pettus, B. J., Rossi, M. J., Wood, R., Usta, J., Szulc, Z., Bielawska, A., Obeid, L. M., and Hannun, Y. A. (2002) Biochemical mecha- nisms of the generation of endogenous long chain ceramide in response to exogenous short chain ceramide in the A549 human lung adenocarcinoma cell line: role for endogenous ceramide in mediating the action of exogenous ceramide. J. Biol. Chem. 277, 12960-12969
    • (2002) J. Biol. Chem. , vol.277 , pp. 12960-12969
    • Ogretmen, B.1    Pettus, B.J.2    Rossi, M.J.3    Wood, R.4    Usta, J.5    Szulc, Z.6    Bielawska, A.7    Obeid, L.M.8    Hannun, Y.A.9
  • 67
    • 33645304602 scopus 로고    scopus 로고
    • Apoptosis occurs via the ceramide recycling pathway in human HaCaT keratinocytes
    • Takeda, S., Mitsutake, S., Tsuji, K., and Igarashi, Y. (2006) Apoptosis occurs via the ceramide recycling pathway in human HaCaT keratinocytes. J. Biochem. 139, 255-262
    • (2006) J. Biochem. , vol.139 , pp. 255-262
    • Takeda, S.1    Mitsutake, S.2    Tsuji, K.3    Igarashi, Y.4
  • 68
    • 25444443570 scopus 로고    scopus 로고
    • Principles of lysosomal membrane digestion: Stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids
    • Kolter, T., and Sandhoff, K. (2005) Principles of lysosomal membrane digestion: stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids. Annu. Rev. Cell Dev. Biol. 21, 81-103
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 81-103
    • Kolter, T.1    Sandhoff, K.2
  • 69
    • 0031928816 scopus 로고    scopus 로고
    • Metabolic fate of exogenous sphingosine in neuroblastoma neuro2A cells: Dose-dependence and biological effects
    • Riboni, L., Bassi, R., Caminiti, A., Prinetti, A., Viani, P., and Tettamanti, G. (1998) Metabolic fate of exogenous sphingosine in neuroblastoma neuro2A cells: dose-dependence and biological effects. Ann. N.Y. Acad. Sci. 845, 46-56
    • (1998) Ann. N.Y. Acad. Sci. , vol.845 , pp. 46-56
    • Riboni, L.1    Bassi, R.2    Caminiti, A.3    Prinetti, A.4    Viani, P.5    Tettamanti, G.6
  • 70
    • 84880616651 scopus 로고    scopus 로고
    • The complexity of sphingolipid biosynthesis in the endoplasmic reticulum
    • Tidhar, R., and Futerman, A. H. (2013) The complexity of sphingolipid biosynthesis in the endoplasmic reticulum. Biochim. Biophys. Acta 1833, 2511-2518
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 2511-2518
    • Tidhar, R.1    Futerman, A.H.2
  • 71
    • 33748665711 scopus 로고    scopus 로고
    • Golgi alkaline ceramidase regulates cell proliferation and survival by controlling levels of sphingosine and S1P
    • Xu, R., Jin, J., Hu, W., Sun, W., Bielawski, J., Szulc, Z., Taha, T., Obeid, L. M., and Mao, C. (2006) Golgi alkaline ceramidase regulates cell proliferation and survival by controlling levels of sphingosine and S1P. FASEB J. 20, 1813-1825
    • (2006) FASEB J. , vol.20 , pp. 1813-1825
    • Xu, R.1    Jin, J.2    Hu, W.3    Sun, W.4    Bielawski, J.5    Szulc, Z.6    Taha, T.7    Obeid, L.M.8    Mao, C.9
  • 72
    • 0343646886 scopus 로고
    • Human acid β-glucosidase: Isolation and amino acid sequence of a peptide containing the catalytic site
    • Dinur, T., Osiecki, K. M., Legler, G., Gatt, S., Desnick, R. J., and Grabowski, G. A. (1986) Human acid β-glucosidase: isolation and amino acid sequence of a peptide containing the catalytic site. Proc. Natl. Acad. Sci. U.S.A. 83, 1660-1664
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 1660-1664
    • Dinur, T.1    Osiecki, K.M.2    Legler, G.3    Gatt, S.4    Desnick, R.J.5    Grabowski, G.A.6
  • 73
    • 67649752327 scopus 로고    scopus 로고
    • Acid βglucosidase 1 counteracts p38delta-dependent induction of interleukin-6: Possible role for ceramide as an anti-inflammatory lipid
    • Kitatani, K., Sheldon, K., Anelli, V., Jenkins, R. W., Sun, Y., Grabowski, G. A., Obeid, L. M., and Hannun, Y. A. (2009) Acid βglucosidase 1 counteracts p38delta-dependent induction of interleukin-6: possible role for ceramide as an anti-inflammatory lipid. J. Biol. Chem. 284, 12979-12988
    • (2009) J. Biol. Chem. , vol.284 , pp. 12979-12988
    • Kitatani, K.1    Sheldon, K.2    Anelli, V.3    Jenkins, R.W.4    Sun, Y.5    Grabowski, G.A.6    Obeid, L.M.7    Hannun, Y.A.8
  • 75
    • 0028070326 scopus 로고
    • Identification of arachidonic acid as a mediator of sphingomyelin hydrolysis in response to tumor necrosis factor ∝
    • Jayadev, S., Linardic, C. M., and Hannun, Y. A. (1994) Identification of arachidonic acid as a mediator of sphingomyelin hydrolysis in response to tumor necrosis factor ∝ J. Biol. Chem. 269, 5757-5763
    • (1994) J. Biol. Chem. , vol.269 , pp. 5757-5763
    • Jayadev, S.1    Linardic, C.M.2    Hannun, Y.A.3
  • 76
    • 0031041448 scopus 로고    scopus 로고
    • Cytokine response modifier A (CrmA) inhibits ceramide formation in response to tumor necrosis factor (TNF)-∝ CrmA and Bcl-2 target distinct components in the apoptotic pathway
    • Dbaibo, G. S., Perry, D. K., Gamard, C. J., Platt, R., Poirier, G. G., Obeid, L. M., and Hannun, Y. A. (1997) Cytokine response modifier A (CrmA) inhibits ceramide formation in response to tumor necrosis factor (TNF)-∝ CrmA and Bcl-2 target distinct components in the apoptotic pathway. J. Exp. Med. 185, 481-490
    • (1997) J. Exp. Med. , vol.185 , pp. 481-490
    • Dbaibo, G.S.1    Perry, D.K.2    Gamard, C.J.3    Platt, R.4    Poirier, G.G.5    Obeid, L.M.6    Hannun, Y.A.7
  • 77
    • 20444506408 scopus 로고    scopus 로고
    • Tumor necrosis factor induces the loss of sphingosine kinase-1 by a cathepsin B-dependent mechanism
    • Taha, T. A., Kitatani, K., Bielawski, J., Cho, W., Hannun, Y. A., and Obeid, L. M. (2005) Tumor necrosis factor induces the loss of sphingosine kinase-1 by a cathepsin B-dependent mechanism. J. Biol. Chem. 280, 17196-17202
    • (2005) J. Biol. Chem. , vol.280 , pp. 17196-17202
    • Taha, T.A.1    Kitatani, K.2    Bielawski, J.3    Cho, W.4    Hannun, Y.A.5    Obeid, L.M.6
  • 78
    • 0031923446 scopus 로고    scopus 로고
    • Alterations in focal adhesion and cytoskeletal proteins during apoptosis
    • Marushige, Y., and Marushige, K. (1998) Alterations in focal adhesion and cytoskeletal proteins during apoptosis. Anticancer Res. 18, 301-307
    • (1998) Anticancer Res , vol.18 , pp. 301-307
    • Marushige, Y.1    Marushige, K.2
  • 79
    • 0037121579 scopus 로고    scopus 로고
    • Ordering ceramide-induced cell detachment and apoptosis in human neuroepithelioma
    • Di Bartolomeo, S., and Spinedi, A. (2002) Ordering ceramide-induced cell detachment and apoptosis in human neuroepithelioma. Neurosci. Lett. 334, 149-152
    • (2002) Neurosci. Lett. , vol.334 , pp. 149-152
    • Di Bartolomeo, S.1    Spinedi, A.2
  • 80
    • 84876990097 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A target for anticancer therapy
    • Perrotti, D., and Neviani, P. (2013) Protein phosphatase 2A: a target for anticancer therapy. Lancet Oncol. 14, e229- e238
    • (2013) Lancet Oncol , vol.14 , pp. e229-e238
    • Perrotti, D.1    Neviani, P.2
  • 81
    • 0034044795 scopus 로고    scopus 로고
    • Immunohistochemical analyses of focal adhesion kinase expression in benign and malignant human breast and colon tissues: Correlation with preinvasive and invasive phenotypes
    • Cance, W. G., Harris, J. E., Iacocca, M. V., Roche, E., Yang, X., Chang, J., Simkins, S., and Xu, L. (2000) Immunohistochemical analyses of focal adhesion kinase expression in benign and malignant human breast and colon tissues: correlation with preinvasive and invasive phenotypes. Clin. Cancer Res. 6, 2417-2423
    • (2000) Clin. Cancer Res , vol.6 , pp. 2417-2423
    • Cance, W.G.1    Harris, J.E.2    Iacocca, M.V.3    Roche, E.4    Yang, X.5    Chang, J.6    Simkins, S.7    Xu, L.8
  • 83
    • 0037343388 scopus 로고    scopus 로고
    • Focal adhesion kinase as a marker of malignant phenotype in breast and cervical carcinomas
    • Oktay, M. H., Oktay, K., Hamele-Bena, D., Buyuk, A., and Koss, L. G. (2003) Focal adhesion kinase as a marker of malignant phenotype in breast and cervical carcinomas. Hum. Pathol. 34, 240-245
    • (2003) Hum. Pathol. , vol.34 , pp. 240-245
    • Oktay, M.H.1    Oktay, K.2    Hamele-Bena, D.3    Buyuk, A.4    Koss, L.G.5
  • 84
    • 0029739950 scopus 로고    scopus 로고
    • Control of adhesion-dependent cell survival by focal adhesion kinase
    • Frisch, S. M., Vuori, K., Ruoslahti, E., and Chan-Hui, P. Y. (1996) Control of adhesion-dependent cell survival by focal adhesion kinase. J. Cell Biol. 134, 793-799
    • (1996) J. Cell Biol. , vol.134 , pp. 793-799
    • Frisch, S.M.1    Vuori, K.2    Ruoslahti, E.3    Chan-Hui, P.Y.4
  • 85
    • 79952752679 scopus 로고    scopus 로고
    • Evolving therapies and FAK inhibitors for the treatment of cancer
    • Dunn, K. B., Heffler, M., and Golubovskaya, V. M. (2010) Evolving therapies and FAK inhibitors for the treatment of cancer. Anticancer Agents Med. Chem. 10, 722-734
    • (2010) Anticancer Agents Med. Chem. , vol.10 , pp. 722-734
    • Dunn, K.B.1    Heffler, M.2    Golubovskaya, V.M.3
  • 88
    • 84876718333 scopus 로고    scopus 로고
    • FAK and HAS inhibition synergistically decrease colon cancer cell viability and affect expression of critical genes
    • Heffler, M., Golubovskaya, V. M., Conroy, J., Liu, S., Wang, D., Cance, W. G., and Dunn, K. B. (2013) FAK and HAS inhibition synergistically decrease colon cancer cell viability and affect expression of critical genes. Anticancer Agents Med. Chem. 13, 584-594
    • (2013) Anticancer Agents Med. Chem. , vol.13 , pp. 584-594
    • Heffler, M.1    Golubovskaya, V.M.2    Conroy, J.3    Liu, S.4    Wang, D.5    Cance, W.G.6    Dunn, K.B.7
  • 91
    • 0034283578 scopus 로고    scopus 로고
    • Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8
    • Stennicke, H. R., Renatus, M., Meldal, M., and Salvesen, G. S. (2000) Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8. Biochem. J. 350, 563-568
    • (2000) Biochem. J. , vol.350 , pp. 563-568
    • Stennicke, H.R.1    Renatus, M.2    Meldal, M.3    Salvesen, G.S.4
  • 92
    • 0037376788 scopus 로고    scopus 로고
    • Cell surface death receptor signaling in normal and cancer cells
    • Ozören, N., and El-Deiry, W. S. (2003) Cell surface death receptor signaling in normal and cancer cells. Semin. Cancer Biol. 13, 135-147
    • (2003) Semin. Cancer Biol. , vol.13 , pp. 135-147
    • Ozören, N.1    El-Deiry, W.S.2
  • 93
    • 0035525733 scopus 로고    scopus 로고
    • Cellular stress response and apoptosis in cancer therapy
    • Herr, I., and Debatin, K. M. (2001) Cellular stress response and apoptosis in cancer therapy. Blood 98, 2603-2614
    • (2001) Blood , vol.98 , pp. 2603-2614
    • Herr, I.1    Debatin, K.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.