메뉴 건너뛰기




Volumn 6, Issue 14, 2007, Pages 1779-1788

FHL2 regulates cell cycle-dependent and doxorubicin-induced p21 Cip1/Waf1 expression in breast cancer cells

Author keywords

Breast cancer; c Jun; Cell cycle; FHL2; MAPK signaling; p21Waf1 Cip1; Transcriptional coactivator

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; ANTHRA[1,9 CD]PYRAZOL 6(2H) ONE; CYCLIN DEPENDENT KINASE INHIBITOR 1; DOXORUBICIN; LIM PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN P53; SHORT HAIRPIN RNA;

EID: 34548216869     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.6.14.4448     Document Type: Article
Times cited : (52)

References (59)
  • 4
    • 0033574044 scopus 로고    scopus 로고
    • The LIM proteins FHL1 and FHL3 are expressed differently in skeletal muscle
    • Morgan MJ, Madgwick AJ. The LIM proteins FHL1 and FHL3 are expressed differently in skeletal muscle. Biochem Biophys Res Commun 1999; 255:245-50.
    • (1999) Biochem Biophys Res Commun , vol.255 , pp. 245-250
    • Morgan, M.J.1    Madgwick, A.J.2
  • 5
    • 0034234785 scopus 로고    scopus 로고
    • Expression patterns of FHL/SLIM family members suggest important functional roles in skeletal muscle and cardiovascular system
    • Chu PH, Ruiz-Lozano P, Zhou Q, Cai C, Chen J. Expression patterns of FHL/SLIM family members suggest important functional roles in skeletal muscle and cardiovascular system. Mech Dev 2000; 95:259-65.
    • (2000) Mech Dev , vol.95 , pp. 259-265
    • Chu, P.H.1    Ruiz-Lozano, P.2    Zhou, Q.3    Cai, C.4    Chen, J.5
  • 6
    • 0034703284 scopus 로고    scopus 로고
    • Alzheimer's disease-associated presenilin 2 interacts with DRAL, an LIM-domain protein
    • Tanahashi H, Tabira T. Alzheimer's disease-associated presenilin 2 interacts with DRAL, an LIM-domain protein. Hum Mol Genet 2000; 9:2281-9.
    • (2000) Hum Mol Genet , vol.9 , pp. 2281-2289
    • Tanahashi, H.1    Tabira, T.2
  • 7
    • 0034735595 scopus 로고    scopus 로고
    • DRAL is a p53-responsive gene whose four and a half LIM domain protein product induces apoptosis
    • Scholl FA, McLoughlin P, Ehler E, de Giovanni C, Schafer BW. DRAL is a p53-responsive gene whose four and a half LIM domain protein product induces apoptosis. J Cell Biol 2000; 151:495-506.
    • (2000) J Cell Biol , vol.151 , pp. 495-506
    • Scholl, F.A.1    McLoughlin, P.2    Ehler, E.3    de Giovanni, C.4    Schafer, B.W.5
  • 9
    • 0037020151 scopus 로고    scopus 로고
    • The LIM-only protein DRAL/ FHL2 interacts with and is a corepressor for the promyelocytic leukemia zinc finger protein
    • McLoughlin P, Ehler E, Carlile G, Licht JD, Schafer BW. The LIM-only protein DRAL/ FHL2 interacts with and is a corepressor for the promyelocytic leukemia zinc finger protein. J Biol Chem 2002; 277:37045-53.
    • (2002) J Biol Chem , vol.277 , pp. 37045-37053
    • McLoughlin, P.1    Ehler, E.2    Carlile, G.3    Licht, J.D.4    Schafer, B.W.5
  • 10
    • 0037386704 scopus 로고    scopus 로고
    • The LIM-only protein FHL2 is a serum-inducible transcriptional coactivator of AP-1
    • Morlon A, Sassone-Corsi P. The LIM-only protein FHL2 is a serum-inducible transcriptional coactivator of AP-1. Proc Natl Acad Sci USA 2003; 100:3977-82.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 3977-3982
    • Morlon, A.1    Sassone-Corsi, P.2
  • 11
    • 16344384026 scopus 로고    scopus 로고
    • Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation
    • Yang Y, Hou H, Haller EM, Nicosia SV, Bai W. Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation. EMBO J 2005; 24:1021-32.
    • (2005) EMBO J , vol.24 , pp. 1021-1032
    • Yang, Y.1    Hou, H.2    Haller, E.M.3    Nicosia, S.V.4    Bai, W.5
  • 13
    • 0037134906 scopus 로고    scopus 로고
    • TUCAN/CARDINAL and DRAL participate in a common pathway for modulation of NF-kappaB activation
    • Stilo R, Leonardi A, Formisano L, Di Jeso B, Vito P, Liguoro D. TUCAN/CARDINAL and DRAL participate in a common pathway for modulation of NF-kappaB activation. FEBS Lett 2002; 521:165-9.
    • (2002) FEBS Lett , vol.521 , pp. 165-169
    • Stilo, R.1    Leonardi, A.2    Formisano, L.3    Di Jeso, B.4    Vito, P.5    Liguoro, D.6
  • 14
    • 0034721855 scopus 로고    scopus 로고
    • The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes
    • Wixler V, Geerts D, Laplantine E, Westhoff D, Smyth N, Aumailley M, Sonnenberg A, Paulsson M. The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes. J Biol Chem 2000; 275:33669-78.
    • (2000) J Biol Chem , vol.275 , pp. 33669-33678
    • Wixler, V.1    Geerts, D.2    Laplantine, E.3    Westhoff, D.4    Smyth, N.5    Aumailley, M.6    Sonnenberg, A.7    Paulsson, M.8
  • 15
    • 0037023685 scopus 로고    scopus 로고
    • Insulin-like growth factor-binding protein 5 (IGFBP-5) interacts with a four and a half LIM protein 2 (FHL2)
    • Amaar YG, Thompson GR, Linkhart TA, Chen ST, Baylink DJ, Mohan S. Insulin-like growth factor-binding protein 5 (IGFBP-5) interacts with a four and a half LIM protein 2 (FHL2). J Biol Chem 2002; 277:12053-60.
    • (2002) J Biol Chem , vol.277 , pp. 12053-12060
    • Amaar, Y.G.1    Thompson, G.R.2    Linkhart, T.A.3    Chen, S.T.4    Baylink, D.J.5    Mohan, S.6
  • 17
    • 0037078329 scopus 로고    scopus 로고
    • Martin B, Schneider R, Janetzky S, Waibler Z, Pandur P, Kuhl M, Behrens J, von der MK, Starzinski-Powitz A, Wixler V. The LIM-only protein FHL2 interacts with beta-catenin and promotes differentiation of mouse myoblasts. J Cell Biol 2002; 159:113-22.
    • Martin B, Schneider R, Janetzky S, Waibler Z, Pandur P, Kuhl M, Behrens J, von der MK, Starzinski-Powitz A, Wixler V. The LIM-only protein FHL2 interacts with beta-catenin and promotes differentiation of mouse myoblasts. J Cell Biol 2002; 159:113-22.
  • 18
    • 33847624615 scopus 로고    scopus 로고
    • The biological relevance of FHL2 in tumour cells and its role as a putative cancer target
    • Kleiber K, Strebhardt K, Martin BT. The biological relevance of FHL2 in tumour cells and its role as a putative cancer target. Anticancer Res 2007; 27:55-61.
    • (2007) Anticancer Res , vol.27 , pp. 55-61
    • Kleiber, K.1    Strebhardt, K.2    Martin, B.T.3
  • 20
    • 0031005095 scopus 로고    scopus 로고
    • Subtractive cloning and characterization of DRAL, a novel LIM-domain protein down-regulated in rhabdomyosarcoma
    • Genini M, Schwalbe P, Scholl FA, Remppis A, Mattei MG, Schafer BW. Subtractive cloning and characterization of DRAL, a novel LIM-domain protein down-regulated in rhabdomyosarcoma. DNA Cell Biol 1997; 16:433-42.
    • (1997) DNA Cell Biol , vol.16 , pp. 433-442
    • Genini, M.1    Schwalbe, P.2    Scholl, F.A.3    Remppis, A.4    Mattei, M.G.5    Schafer, B.W.6
  • 21
    • 2442521380 scopus 로고    scopus 로고
    • Focal adhesion kinase interacts with the transcriptional coactivator FHL2 and both are overexpressed in epithelial ovarian cancer
    • Gabriel B, Mildenberger S, Weisser CW, Metzger E, Gitsch G, Schule R, Muller JM. Focal adhesion kinase interacts with the transcriptional coactivator FHL2 and both are overexpressed in epithelial ovarian cancer. Anticancer Res 2004; 24:921-7.
    • (2004) Anticancer Res , vol.24 , pp. 921-927
    • Gabriel, B.1    Mildenberger, S.2    Weisser, C.W.3    Metzger, E.4    Gitsch, G.5    Schule, R.6    Muller, J.M.7
  • 26
    • 33847754623 scopus 로고    scopus 로고
    • The JNK signal transduction pathway
    • Weston CR, Davis RJ. The JNK signal transduction pathway. Curr Opin Cell Biol 2007; 19:142-9.
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 142-149
    • Weston, C.R.1    Davis, R.J.2
  • 27
    • 17144371848 scopus 로고    scopus 로고
    • JNK2: A negative regulator of cellular proliferation
    • Sabapathy K, Wagner EF. JNK2: A negative regulator of cellular proliferation. Cell Cycle 2004; 3:1520-3.
    • (2004) Cell Cycle , vol.3 , pp. 1520-1523
    • Sabapathy, K.1    Wagner, E.F.2
  • 28
    • 0035971432 scopus 로고    scopus 로고
    • AP-1 in mouse development and tumorigenesis
    • Jochum W, Passegue E, Wagner EF. AP-1 in mouse development and tumorigenesis. Oncogene 2001; 20:2401-12.
    • (2001) Oncogene , vol.20 , pp. 2401-2412
    • Jochum, W.1    Passegue, E.2    Wagner, E.F.3
  • 29
    • 0035971506 scopus 로고    scopus 로고
    • Jun, the oncoprotein
    • Vogt PK. Jun, the oncoprotein. Oncogene 2001; 20:2365-77.
    • (2001) Oncogene , vol.20 , pp. 2365-2377
    • Vogt, P.K.1
  • 30
    • 1642458404 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase 2 interacts with and is negatively regulated by the LIM-only protein FHL2 in cardiomyocytes
    • Purcell NH, Darwis D, Bueno OF, Muller JM, Schule R, Molkentin JD. Extracellular signal-regulated kinase 2 interacts with and is negatively regulated by the LIM-only protein FHL2 in cardiomyocytes. Mol Cell Biol 2004; 24:1081-95.
    • (2004) Mol Cell Biol , vol.24 , pp. 1081-1095
    • Purcell, N.H.1    Darwis, D.2    Bueno, O.F.3    Muller, J.M.4    Schule, R.5    Molkentin, J.D.6
  • 31
    • 16244403039 scopus 로고    scopus 로고
    • Cancer incidence and mortality in Europe, 2004
    • Boyle P, Ferlay J. Cancer incidence and mortality in Europe, 2004. Ann Oncol 2005; 16:481-8.
    • (2005) Ann Oncol , vol.16 , pp. 481-488
    • Boyle, P.1    Ferlay, J.2
  • 32
    • 0141571284 scopus 로고    scopus 로고
    • BRCA1 interacts with FHL2 and enhances FHL2 transactivation function
    • Yan J, Zhu J, Zhong H, Lu Q, Huang C, Ye Q. BRCA1 interacts with FHL2 and enhances FHL2 transactivation function. FEBS Lett 2003; 553:183-9.
    • (2003) FEBS Lett , vol.553 , pp. 183-189
    • Yan, J.1    Zhu, J.2    Zhong, H.3    Lu, Q.4    Huang, C.5    Ye, Q.6
  • 33
    • 1342326910 scopus 로고    scopus 로고
    • Relevance of breast cancer cell lines as models for breast tumours: An update
    • Lacroix M, Leclercq G. Relevance of breast cancer cell lines as models for breast tumours: An update. Breast Cancer Res Treat 2004; 83:249-89.
    • (2004) Breast Cancer Res Treat , vol.83 , pp. 249-289
    • Lacroix, M.1    Leclercq, G.2
  • 34
    • 0036581755 scopus 로고    scopus 로고
    • Linking DNA damage to cell cycle checkpoints
    • Samuel T, Weber HO, Funk JO. Linking DNA damage to cell cycle checkpoints. Cell Cycle 2002; 1:162-8.
    • (2002) Cell Cycle , vol.1 , pp. 162-168
    • Samuel, T.1    Weber, H.O.2    Funk, J.O.3
  • 35
    • 3843093015 scopus 로고    scopus 로고
    • Role of p21WAF1 in the cellular response to UV
    • Fotedar R, Bendjennat M, Fotedar A. Role of p21WAF1 in the cellular response to UV. Cell Cycle 2004; 3:134-7.
    • (2004) Cell Cycle , vol.3 , pp. 134-137
    • Fotedar, R.1    Bendjennat, M.2    Fotedar, A.3
  • 36
    • 20144384882 scopus 로고    scopus 로고
    • Gartel AL, Radhakrishnan SK. Lost in transcription: p21 repression, mechanisms, and consequences. Cancer Res 2005; 65:3980-5.
    • Gartel AL, Radhakrishnan SK. Lost in transcription: p21 repression, mechanisms, and consequences. Cancer Res 2005; 65:3980-5.
  • 37
    • 0032214980 scopus 로고    scopus 로고
    • Overexpression of ErbB2 blocks Taxol-induced apoptosis by upregulation of p21Cip1, which inhibits p34Cdc2 kinase
    • Yu D, Jing T, Liu B, Yao J, Tan M, McDonnell TJ, Hung MC. Overexpression of ErbB2 blocks Taxol-induced apoptosis by upregulation of p21Cip1, which inhibits p34Cdc2 kinase. Mol Cell 1998; 2:581-91.
    • (1998) Mol Cell , vol.2 , pp. 581-591
    • Yu, D.1    Jing, T.2    Liu, B.3    Yao, J.4    Tan, M.5    McDonnell, T.J.6    Hung, M.C.7
  • 38
    • 0037780825 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus encoded vFLIP induces cellular IL-6 expression: The role of the NF-kappaB and JNK/AP1 pathways
    • An J, Sun Y, Sun R, Rettig MB. Kaposi's sarcoma-associated herpesvirus encoded vFLIP induces cellular IL-6 expression: The role of the NF-kappaB and JNK/AP1 pathways. Oncogene 2003; 22:3371-85.
    • (2003) Oncogene , vol.22 , pp. 3371-3385
    • An, J.1    Sun, Y.2    Sun, R.3    Rettig, M.B.4
  • 39
    • 0032823313 scopus 로고    scopus 로고
    • Induction of interleukin-8 synthesis integrates effects on transcription and mRNA degradation from at least three different cytokine- or stress-activated signal transduction pathways
    • Holtmann H, Winzen R, Holland P, Eickemeier S, Hoffmann E, Wallach D, Malinin NL, Cooper JA, Resch K, Kracht M. Induction of interleukin-8 synthesis integrates effects on transcription and mRNA degradation from at least three different cytokine- or stress-activated signal transduction pathways. Mol Cell Biol 1999; 19:6742-53.
    • (1999) Mol Cell Biol , vol.19 , pp. 6742-6753
    • Holtmann, H.1    Winzen, R.2    Holland, P.3    Eickemeier, S.4    Hoffmann, E.5    Wallach, D.6    Malinin, N.L.7    Cooper, J.A.8    Resch, K.9    Kracht, M.10
  • 41
    • 0034707053 scopus 로고    scopus 로고
    • In search of the tumour-suppressor functions of BRCA1 and BRCA2
    • Scully R, Livingston DM. In search of the tumour-suppressor functions of BRCA1 and BRCA2. Nature 2000; 408:429-32.
    • (2000) Nature , vol.408 , pp. 429-432
    • Scully, R.1    Livingston, D.M.2
  • 42
    • 0035945656 scopus 로고    scopus 로고
    • Estrogen and the risk of breast cancer
    • Clemons M, Goss P. Estrogen and the risk of breast cancer. N Engl J Med 2001; 344:276-85.
    • (2001) N Engl J Med , vol.344 , pp. 276-285
    • Clemons, M.1    Goss, P.2
  • 45
    • 0242671511 scopus 로고    scopus 로고
    • An antisense oligodeoxynucleotide to p21(Waf1/Cip1) causes apoptosis in human breast cancer cells
    • Fan Y, Borowsky AD, Weiss RH. An antisense oligodeoxynucleotide to p21(Waf1/Cip1) causes apoptosis in human breast cancer cells. Mol Cancer Ther 2003; 2:773-82.
    • (2003) Mol Cancer Ther , vol.2 , pp. 773-782
    • Fan, Y.1    Borowsky, A.D.2    Weiss, R.H.3
  • 48
    • 33751309077 scopus 로고    scopus 로고
    • Hui L, Zheng Y, Yan Y, Bargonetti J, Foster DA. Mutant p53 in MDA-MB-231 breast cancer cells is stabilized by elevated phospholipase D activity and contributes to survival signals generated by phospholipase D. Oncogene 2006; 25:7305-10.
    • Hui L, Zheng Y, Yan Y, Bargonetti J, Foster DA. Mutant p53 in MDA-MB-231 breast cancer cells is stabilized by elevated phospholipase D activity and contributes to survival signals generated by phospholipase D. Oncogene 2006; 25:7305-10.
  • 49
    • 21444438367 scopus 로고    scopus 로고
    • Cyclin-dependent kinase inhibitors and JNK act as molecular switches, regulating the choice between growth arrest and apoptosis induced by galectin-8
    • Arbel-Goren R, Levy Y, Ronen D, Zick Y. Cyclin-dependent kinase inhibitors and JNK act as molecular switches, regulating the choice between growth arrest and apoptosis induced by galectin-8. J Biol Chem 2005; 280:19105-14.
    • (2005) J Biol Chem , vol.280 , pp. 19105-19114
    • Arbel-Goren, R.1    Levy, Y.2    Ronen, D.3    Zick, Y.4
  • 50
    • 0035958630 scopus 로고    scopus 로고
    • Prolonged Jun N-terminal kinase (JNK) activation and the upregulation of p53 and p21(WAF1/CIP1) preceded apoptosis in hepatocytes after partial hepatectomy and cisplatin
    • Kobayashi K, Tsukamoto I. Prolonged Jun N-terminal kinase (JNK) activation and the upregulation of p53 and p21(WAF1/CIP1) preceded apoptosis in hepatocytes after partial hepatectomy and cisplatin. Biochim Biophys Acta 2001; 1537:79-88.
    • (2001) Biochim Biophys Acta , vol.1537 , pp. 79-88
    • Kobayashi, K.1    Tsukamoto, I.2
  • 51
    • 0042197268 scopus 로고    scopus 로고
    • Are p27 and p21 cytoplasmic oncoproteins?
    • Blagosklonny MV. Are p27 and p21 cytoplasmic oncoproteins? Cell Cycle 2002; 1:391-3.
    • (2002) Cell Cycle , vol.1 , pp. 391-393
    • Blagosklonny, M.V.1
  • 52
    • 0033894919 scopus 로고    scopus 로고
    • Procaspase 3/p21 complex formation to resist fas-mediated cell death is initiated as a result of the phosphorylation of p21 by protein kinase A
    • Suzuki A, Kawano H, Hayashida M, Hayasaki Y, Tsutomi Y, Akahane K. Procaspase 3/p21 complex formation to resist fas-mediated cell death is initiated as a result of the phosphorylation of p21 by protein kinase A. Cell Death Differ 2000; 7:721-8.
    • (2000) Cell Death Differ , vol.7 , pp. 721-728
    • Suzuki, A.1    Kawano, H.2    Hayashida, M.3    Hayasaki, Y.4    Tsutomi, Y.5    Akahane, K.6
  • 53
    • 0037042177 scopus 로고    scopus 로고
    • Oncogenic functions of tumour suppressor p21(Waf1/Cip1/Sdi1): Association with cell senescence and tumour-promoting activities of stromal fibroblasts
    • Roninson IB. Oncogenic functions of tumour suppressor p21(Waf1/Cip1/Sdi1): Association with cell senescence and tumour-promoting activities of stromal fibroblasts. Cancer Lett 2002; 179:1-14.
    • (2002) Cancer Lett , vol.179 , pp. 1-14
    • Roninson, I.B.1
  • 54
    • 0037192852 scopus 로고    scopus 로고
    • Li Y, Dowbenko D, Lasky LA. AKT/PKB phosphorylation of p21Cip/WAF1 enhances protein stability of p21Cip/WAF1 and promotes cell survival. J Biol Chem 2002; 277:11352-61.
    • Li Y, Dowbenko D, Lasky LA. AKT/PKB phosphorylation of p21Cip/WAF1 enhances protein stability of p21Cip/WAF1 and promotes cell survival. J Biol Chem 2002; 277:11352-61.
  • 56
    • 0037427570 scopus 로고    scopus 로고
    • Suppression of breast cancer growth and angiogenesis by an antisense oligodeoxynucleotide to p21(Waf1/ Cip1)
    • Weiss RH, Marshall D, Howard L, Corbacho AM, Cheung AT, Sawai ET. Suppression of breast cancer growth and angiogenesis by an antisense oligodeoxynucleotide to p21(Waf1/ Cip1). Cancer Lett 2003; 189:39-48.
    • (2003) Cancer Lett , vol.189 , pp. 39-48
    • Weiss, R.H.1    Marshall, D.2    Howard, L.3    Corbacho, A.M.4    Cheung, A.T.5    Sawai, E.T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.