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Volumn 2, Issue 1, 2011, Pages 165-176

Protein signatures in human MDA-MB-231 breast cancer cells indicating a more invasive phenotype following knockdown of human endometase/matrilysin-2 by siRNA

Author keywords

Breast cancer metastasis suppressor 1; Invasion and metastasis; Mass spectrometry; Matrix metalloproteinase (MMP); MMP 26; Proteomics; Putative protein biomarkers

Indexed keywords

ALPHA TUBULIN; BETA ACTIN; BREAST CANCER METASTASIS SUPPRESSOR 1 PROTEIN; CYSTATIN C; GLUCOSE REGULATED PROTEIN 78; HEAT SHOCK PROTEIN 90; LIPOCORTIN 5; MATRIX METALLOPROTEINASE 26; PEROXIREDOXIN 2; SMALL INTERFERING RNA; TROPOMYOSIN; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG;

EID: 84873714360     PISSN: None     EISSN: 18379664     Source Type: Journal    
DOI: 10.7150/jca.2.165     Document Type: Article
Times cited : (8)

References (72)
  • 1
    • 12144285600 scopus 로고    scopus 로고
    • Proteases, extracellular matrix, and cancer: a workshop of the path B study section
    • DeClerck YA, Mercurio AM, Stack MS, et al. Proteases, extracellular matrix, and cancer: a workshop of the path B study section. Am J Pathol 2004;164:1131-9.
    • (2004) Am J Pathol , vol.164 , pp. 1131-1139
    • DeClerck, Y.A.1    Mercurio, A.M.2    Stack, M.S.3
  • 2
    • 4444304939 scopus 로고    scopus 로고
    • Regulation of matrix biology by matrix metalloproteinases
    • Mott JD, Werb Z. Regulation of matrix biology by matrix metalloproteinases. Curr Opin Cell Biol 2004;16:558-64.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 558-564
    • Mott, J.D.1    Werb, Z.2
  • 3
    • 31344458952 scopus 로고    scopus 로고
    • Structure and function of matrix metalloproteinases and TIMPs
    • Nagase H, Visse R and Murphy G. Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc Res 2006;69:562-73.
    • (2006) Cardiovasc Res , vol.69 , pp. 562-573
    • Nagase, H.1    Visse, R.2    Murphy, G.3
  • 4
    • 0033952145 scopus 로고    scopus 로고
    • The biology of cell locomotion within three-dimensional extracellular matrix
    • Friedl P, Brocker EB. The biology of cell locomotion within three-dimensional extracellular matrix. Cell Mol Life Sci 2000;57:41-64.
    • (2000) Cell Mol Life Sci , vol.57 , pp. 41-64
    • Friedl, P.1    Brocker, E.B.2
  • 5
    • 0037455576 scopus 로고    scopus 로고
    • Compensation mechanism in tumor cell migration: mesenchymal-amoeboid transition after blocking of pericellular proteolysis
    • Wolf K, Mazo I, Leung H, et al. Compensation mechanism in tumor cell migration: mesenchymal-amoeboid transition after blocking of pericellular proteolysis. J Cell Biol 2003;160:267-77.
    • (2003) J Cell Biol , vol.160 , pp. 267-277
    • Wolf, K.1    Mazo, I.2    Leung, H.3
  • 6
    • 0034123653 scopus 로고    scopus 로고
    • Interactions between tumour cells and stromal cells and proteolytic modification of the extracellular matrix by metalloproteinases in cancer
    • DeClerck YA. Interactions between tumour cells and stromal cells and proteolytic modification of the extracellular matrix by metalloproteinases in cancer. Eur J Cancer 2000;36:1258-68.
    • (2000) Eur J Cancer , vol.36 , pp. 1258-1268
    • DeClerck, Y.A.1
  • 7
    • 33646593786 scopus 로고    scopus 로고
    • Modifying the soil to affect the seed: role of stromal-derived matrix metalloproteinases in cancer progression
    • Jodele S, Blavier L, Yoon JM and DeClerck YA. Modifying the soil to affect the seed: role of stromal-derived matrix metalloproteinases in cancer progression. Cancer Metastasis Rev 2006;25:35-43.
    • (2006) Cancer Metastasis Rev , vol.25 , pp. 35-43
    • Jodele, S.1    Blavier, L.2    Yoon, J.M.3    DeClerck, Y.A.4
  • 8
    • 0035479845 scopus 로고    scopus 로고
    • Matrix metalloproteinases: they're not just for matrix anymore!
    • McCawley LJ, Matrisian LM. Matrix metalloproteinases: they're not just for matrix anymore! Curr Opin Cell Biol 2001;13:534-40.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 534-540
    • McCawley, L.J.1    Matrisian, L.M.2
  • 9
    • 16844374843 scopus 로고    scopus 로고
    • Matrilysin-2 (matrix met-alloproteinase-26) is upregulated in keratinocytes during wound repair and early skin carcinogenesis
    • Ahokas K, Skoog T, Suomela S, et al. Matrilysin-2 (matrix met-alloproteinase-26) is upregulated in keratinocytes during wound repair and early skin carcinogenesis. J Invest Dermatol 2005;124:849-56.
    • (2005) J Invest Dermatol , vol.124 , pp. 849-856
    • Ahokas, K.1    Skoog, T.2    Suomela, S.3
  • 10
    • 4043163351 scopus 로고    scopus 로고
    • Metastasis markers in bladder cancer: a review of the literature and clinical considerations
    • Gontero P, Banisadr S, Frea B and Brausi M. Metastasis markers in bladder cancer: a review of the literature and clinical considerations. Eur Urol 2004;46:296-311.
    • (2004) Eur Urol , vol.46 , pp. 296-311
    • Gontero, P.1    Banisadr, S.2    Frea, B.3    Brausi, M.4
  • 11
    • 33748712425 scopus 로고    scopus 로고
    • Coordinated peak ex-pression of MMP-26 and TIMP-4 in preinvasive human prostate tumor
    • Lee S, Desai KK, Iczkowski KA, et al. Coordinated peak ex-pression of MMP-26 and TIMP-4 in preinvasive human prostate tumor. Cell Res 2006;16:750-8.
    • (2006) Cell Res , vol.16 , pp. 750-758
    • Lee, S.1    Desai, K.K.2    Iczkowski, K.A.3
  • 12
    • 34147171102 scopus 로고    scopus 로고
    • Calcium regulates tertiary structure and enzymatic activity of human endometase/matrilysin-2 and its role in promoting human breast cancer cell invasion
    • Lee S, Park HI and Sang QX. Calcium regulates tertiary structure and enzymatic activity of human endometase/matrilysin-2 and its role in promoting human breast cancer cell invasion. Biochem J 2007;403:31-42.
    • (2007) Biochem J , vol.403 , pp. 31-42
    • Lee, S.1    Park, H.I.2    Sang, Q.X.3
  • 13
    • 0035875151 scopus 로고    scopus 로고
    • Characterization of matrix metalloproteinase-26, a novel metalloproteinase widely expressed in cancer cells of epithelial origin
    • Marchenko GN, Ratnikov BI, Rozanov DV, Godzik A, Deryugina EI and Strongin AY. Characterization of matrix metalloproteinase-26, a novel metalloproteinase widely expressed in cancer cells of epithelial origin. Biochem J 2001;356:705-18.
    • (2001) Biochem J , vol.356 , pp. 705-718
    • Marchenko, G.N.1    Ratnikov, B.I.2    Rozanov, D.V.3    Godzik, A.4    Deryugina, E.I.5    Strongin, A.Y.6
  • 14
    • 0034617262 scopus 로고    scopus 로고
    • Identification and characterization of human endometase (Matrix metalloproteinase-26) from endometrial tumor
    • Park HI, Ni J, Gerkema FE, Liu D, Belozerov VE and Sang QX. Identification and characterization of human endometase (Matrix metalloproteinase-26) from endometrial tumor. J Biol Chem 2000;275:20540-4.
    • (2000) J Biol Chem , vol.275 , pp. 20540-20544
    • Park, H.I.1    Ni, J.2    Gerkema, F.E.3    Liu, D.4    Belozerov, V.E.5    Sang, Q.X.6
  • 15
    • 0034283015 scopus 로고    scopus 로고
    • a new matrix metalloproteinase expressed in human tumors and showing the minimal domain organization required for secretion, latency, and activity
    • Uria JA, Lopez-Otin C. Matrilysin-2, a new matrix metalloproteinase expressed in human tumors and showing the minimal domain organization required for secretion, latency, and activity. Cancer Res 2000;60:4745-51.
    • (2000) Cancer Res , vol.60 , pp. 4745-4751
    • Uria, J.A.1    Lopez-Otin, C.2    Matrilysin-23
  • 16
    • 0038351013 scopus 로고    scopus 로고
    • Activation of pro-gelatinase B by endometase/matrilysin-2 promotes invasion of human prostate cancer cells
    • Zhao YG, Xiao AZ, Newcomer RG, et al. Activation of pro-gelatinase B by endometase/matrilysin-2 promotes invasion of human prostate cancer cells. J Biol Chem 2003;278:15056-64.
    • (2003) J Biol Chem , vol.278 , pp. 15056-15064
    • Zhao, Y.G.1    Xiao, A.Z.2    Newcomer, R.G.3
  • 17
    • 33645046096 scopus 로고    scopus 로고
    • Matrix metalloproteinase 26 proteolysis of the NH2-terminal domain of the estrogen receptor beta correlates with the survival of breast cancer patients
    • Savinov AY, Remacle AG, Golubkov VS, et al. Matrix metalloproteinase 26 proteolysis of the NH2-terminal domain of the estrogen receptor beta correlates with the survival of breast cancer patients. Cancer Res 2006;66:2716-24.
    • (2006) Cancer Res , vol.66 , pp. 2716-2724
    • Savinov, A.Y.1    Remacle, A.G.2    Golubkov, V.S.3
  • 18
    • 1642556794 scopus 로고    scopus 로고
    • Endometase/matrilysin-2 in human breast ductal carcinoma in situ and its inhibition by tissue inhibitors of metalloproteinases-2 and -4: a putative role in the initiation of breast cancer invasion
    • Zhao YG, Xiao AZ, Park HI, et al. Endometase/matrilysin-2 in human breast ductal carcinoma in situ and its inhibition by tissue inhibitors of metalloproteinases-2 and -4: a putative role in the initiation of breast cancer invasion. Cancer Res 2004;64:590-8.
    • (2004) Cancer Res , vol.64 , pp. 590-598
    • Zhao, Y.G.1    Xiao, A.Z.2    Park, H.I.3
  • 19
    • 33747876774 scopus 로고    scopus 로고
    • Breast cancer metastasis suppressor 1 (BRMS1) is stabilized by the Hsp90 chaperone
    • Hurst DR, Mehta A, Moore BP, et al. Breast cancer metastasis suppressor 1 (BRMS1) is stabilized by the Hsp90 chaperone. Biochem Biophys Res Commun 2006;348:1429-35.
    • (2006) Biochem Biophys Res Commun , vol.348 , pp. 1429-1435
    • Hurst, D.R.1    Mehta, A.2    Moore, B.P.3
  • 20
    • 9244223110 scopus 로고    scopus 로고
    • Matrix metalloproteinase-26 is associated with estrogen-dependent malignancies and targets alpha1-antitrypsin serpin
    • Li W, Savinov AY, Rozanov DV, et al. Matrix metalloproteinase-26 is associated with estrogen-dependent malignancies and targets alpha1-antitrypsin serpin. Cancer Res 2004;64:8657-65.
    • (2004) Cancer Res , vol.64 , pp. 8657-8665
    • Li, W.1    Savinov, A.Y.2    Rozanov, D.V.3
  • 21
    • 43149092915 scopus 로고    scopus 로고
    • Alterations of BRMS1-ARID4A interaction modify gene expression but still suppress metastasis in human breast cancer cells
    • Hurst DR, Xie Y, Vaidya KS, et al. Alterations of BRMS1-ARID4A interaction modify gene expression but still suppress metastasis in human breast cancer cells. J Biol Chem 2008;283:7438-44.
    • (2008) J Biol Chem , vol.283 , pp. 7438-7444
    • Hurst, D.R.1    Xie, Y.2    Vaidya, K.S.3
  • 22
    • 40449094341 scopus 로고    scopus 로고
    • BRMS1 suppresses breast cancer experimental metastasis to multiple organs by inhibiting several steps of the metastatic process
    • Phadke PA, Vaidya KS, Nash KT, Hurst DR and Welch DR. BRMS1 suppresses breast cancer experimental metastasis to multiple organs by inhibiting several steps of the metastatic process. Am J Pathol 2008;172:809-17.
    • (2008) Am J Pathol , vol.172 , pp. 809-817
    • Phadke, P.A.1    Vaidya, K.S.2    Nash, K.T.3    Hurst, D.R.4    Welch, D.R.5
  • 23
    • 0035685003 scopus 로고    scopus 로고
    • Analysis of mechanisms underlying BRMS1 suppression of metastasis
    • Samant RS, Seraj MJ, Saunders MM, et al. Analysis of mechanisms underlying BRMS1 suppression of metastasis. Clin Exp Metastasis 2000;18:683-93.
    • (2000) Clin Exp Metastasis , vol.18 , pp. 683-693
    • Samant, R.S.1    Seraj, M.J.2    Saunders, M.M.3
  • 24
    • 0036061134 scopus 로고    scopus 로고
    • Suppression of human melanoma metastasis by the metastasis suppressor gene, BRMS1
    • Shevde LA, Samant RS, Goldberg SF, et al. Suppression of human melanoma metastasis by the metastasis suppressor gene, BRMS1. Exp Cell Res 2002;273:229-39.
    • (2002) Exp Cell Res , vol.273 , pp. 229-239
    • Shevde, L.A.1    Samant, R.S.2    Goldberg, S.F.3
  • 25
    • 33646037353 scopus 로고    scopus 로고
    • Suppression of human ovarian carcinoma metastasis by the metastasis-suppressor gene, BRMS1
    • Zhang S, Lin QD and Di W. Suppression of human ovarian carcinoma metastasis by the metastasis-suppressor gene, BRMS1. Int J Gynecol Cancer 2006;16:522-31.
    • (2006) Int J Gynecol Cancer , vol.16 , pp. 522-531
    • Zhang, S.1    Lin, Q.D.2    Di, W.3
  • 26
    • 61349201417 scopus 로고    scopus 로고
    • Breast cancer metastasis suppressor 1 (BRMS1) suppresses metastasis and correlates with improved patient survival in non-small cell lung cancer
    • Smith PW, Liu Y, Siefert SA, Moskaluk CA, Petroni GR and Jones DR. Breast cancer metastasis suppressor 1 (BRMS1) suppresses metastasis and correlates with improved patient survival in non-small cell lung cancer. Cancer Lett 2009;276:196-203.
    • (2009) Cancer Lett , vol.276 , pp. 196-203
    • Smith, P.W.1    Liu, Y.2    Siefert, S.A.3    Moskaluk, C.A.4    Petroni, G.R.5    Jones, D.R.6
  • 28
    • 35648989121 scopus 로고    scopus 로고
    • Proteomics-based strategy to delineate the molecular mechanisms of the metastasis suppressor gene BRMS1
    • Rivera J, Megias D and Bravo J. Proteomics-based strategy to delineate the molecular mechanisms of the metastasis suppressor gene BRMS1. J Proteome Res 2007;6:4006-18.
    • (2007) J Proteome Res , vol.6 , pp. 4006-4018
    • Rivera, J.1    Megias, D.2    Bravo, J.3
  • 29
    • 0347723868 scopus 로고    scopus 로고
    • Breast cancer metas-tasis suppressor 1 (BRMS1) forms complexes with retinoblastoma-binding protein 1 (RBP1) and the mSin3 histone deacetylase complex and represses transcription
    • Meehan WJ, Samant RS, Hopper JE, et al. Breast cancer metastasis suppressor 1 (BRMS1) forms complexes with retinoblastoma-binding protein 1 (RBP1) and the mSin3 histone deacetylase complex and represses transcription. J Biol Chem 2004;279:1562-9.
    • (2004) J Biol Chem , vol.279 , pp. 1562-1569
    • Meehan, W.J.1    Samant, R.S.2    Hopper, J.E.3
  • 30
    • 33846993367 scopus 로고    scopus 로고
    • Breast cancer metas-tasis suppressor 1 (BRMS1) inhibits osteopontin transcription by abrogating NF-kappaB activation
    • Samant RS, Clark DW, Fillmore RA, et al. Breast cancer metas-tasis suppressor 1 (BRMS1) inhibits osteopontin transcription by abrogating NF-kappaB activation. Mol Cancer 2007;6:6.
    • (2007) Mol Cancer , vol.6 , pp. 6
    • Samant, R.S.1    Clark, D.W.2    Fillmore, R.A.3
  • 31
    • 0037150683 scopus 로고    scopus 로고
    • Disassembly of transcriptional regulatory complexes by molecular chaperones
    • Freeman BC, Yamamoto KR. Disassembly of transcriptional regulatory complexes by molecular chaperones. Science 2002;296:2232-5.
    • (2002) Science , vol.296 , pp. 2232-2235
    • Freeman, B.C.1    Yamamoto, K.R.2
  • 32
    • 0035423875 scopus 로고    scopus 로고
    • The glucose-regulated proteins: stress induction and clinical applications
    • Lee AS. The glucose-regulated proteins: stress induction and clinical applications. Trends Biochem Sci 2001;26:504-10.
    • (2001) Trends Biochem Sci , vol.26 , pp. 504-510
    • Lee, A.S.1
  • 33
    • 0030765016 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperones GRP78 and calreticulin prevent oxidative stress, Ca2+ disturbances, and cell death in renal epithelial cells
    • Liu H, Bowes RC3rd, van de Water B, Sillence C, Nagelkerke JF and Stevens JL. Endoplasmic reticulum chaperones GRP78 and calreticulin prevent oxidative stress, Ca2+ disturbances, and cell death in renal epithelial cells. J Biol Chem 1997;272:21751-9.
    • (1997) J Biol Chem , vol.272 , pp. 21751-21759
    • Liu, H.1    Bowes 3rd., R.C.2    van de Water, B.3    Sillence, C.4    Nagelkerke, J.F.5    Stevens, J.L.6
  • 35
    • 1642471825 scopus 로고    scopus 로고
    • Heat-shock proteins as regulators of apoptosis
    • Takayama S, Reed JC and Homma S. Heat-shock proteins as regulators of apoptosis. Oncogene 2003;22:9041-7.
    • (2003) Oncogene , vol.22 , pp. 9041-9047
    • Takayama, S.1    Reed, J.C.2    Homma, S.3
  • 36
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell L, Lindquist SL. HSP90 and the chaperoning of cancer. Nat Rev Cancer 2005;5:761-72.
    • (2005) Nat Rev Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 37
    • 3242879188 scopus 로고    scopus 로고
    • "The stress of dying": the role of heat shock proteins in the regulation of apoptosis
    • Beere HM. "The stress of dying": the role of heat shock proteins in the regulation of apoptosis. J Cell Sci 2004;117:2641-51.
    • (2004) J Cell Sci , vol.117 , pp. 2641-2651
    • Beere, H.M.1
  • 38
    • 67651171392 scopus 로고    scopus 로고
    • Hsp90 is an essential regulator of EphA2 receptor stability and signaling: implications for cancer cell migration and metastasis
    • Annamalai B, Liu X, Gopal U and Isaacs JS. Hsp90 is an essential regulator of EphA2 receptor stability and signaling: implications for cancer cell migration and metastasis. Mol Cancer Res 2009;7:1021-32.
    • (2009) Mol Cancer Res , vol.7 , pp. 1021-1032
    • Annamalai, B.1    Liu, X.2    Gopal, U.3    Isaacs, J.S.4
  • 39
    • 38349132541 scopus 로고    scopus 로고
    • A critical role for HSP90 in cancer cell invasion involves interaction with the extracellular domain of HER-2
    • Sidera K, Gaitanou M, Stellas D, Matsas R and Patsavoudi E. A critical role for HSP90 in cancer cell invasion involves interaction with the extracellular domain of HER-2. J Biol Chem 2008;283:2031-41.
    • (2008) J Biol Chem , vol.283 , pp. 2031-2041
    • Sidera, K.1    Gaitanou, M.2    Stellas, D.3    Matsas, R.4    Patsavoudi, E.5
  • 40
    • 42049084486 scopus 로고    scopus 로고
    • A small molecule cell-impermeant Hsp90 antagonist inhibits tumor cell motility and invasion
    • Tsutsumi S, Scroggins B, Koga F, et al. A small molecule cell-impermeant Hsp90 antagonist inhibits tumor cell motility and invasion. Oncogene 2008;27:2478-87.
    • (2008) Oncogene , vol.27 , pp. 2478-2487
    • Tsutsumi, S.1    Scroggins, B.2    Koga, F.3
  • 41
    • 67649950623 scopus 로고    scopus 로고
    • Participation of the lipoprotein receptor LRP1 in hypoxia-HSP90alpha autocrine signaling to promote keratinocyte migration
    • Woodley DT, Fan J, Cheng CF, et al. Participation of the lipoprotein receptor LRP1 in hypoxia-HSP90alpha autocrine signaling to promote keratinocyte migration. J Cell Sci 2009;122:1495-8.
    • (2009) J Cell Sci , vol.122 , pp. 1495-1498
    • Woodley, D.T.1    Fan, J.2    Cheng, C.F.3
  • 42
    • 27144503120 scopus 로고    scopus 로고
    • 17-AAG, an Hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration
    • Waza M, Adachi H, Katsuno M, et al. 17-AAG, an Hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration. Nat Med 2005;11:1088-95.
    • (2005) Nat Med , vol.11 , pp. 1088-1095
    • Waza, M.1    Adachi, H.2    Katsuno, M.3
  • 43
    • 0034605446 scopus 로고    scopus 로고
    • Role of the heat shock response and molecular chaperones in oncogenesis and cell death
    • Jolly C, Morimoto RI. Role of the heat shock response and molecular chaperones in oncogenesis and cell death. J Natl Cancer Inst 2000;92:1564-72.
    • (2000) J Natl Cancer Inst , vol.92 , pp. 1564-1572
    • Jolly, C.1    Morimoto, R.I.2
  • 44
    • 0344467338 scopus 로고    scopus 로고
    • Significance of expression of heat shock protein90alpha in human gastric cancer
    • Zuo DS, Dai J, Bo AH, Fan J and Xiao XY. Significance of expression of heat shock protein90alpha in human gastric cancer. World J Gastroenterol 2003;9:2616-8.
    • (2003) World J Gastroenterol , vol.9 , pp. 2616-2618
    • Zuo, D.S.1    Dai, J.2    Bo, A.H.3    Fan, J.4    Xiao, X.Y.5
  • 45
    • 0034021399 scopus 로고    scopus 로고
    • Overexpression of the glucose-regulated stress gene GRP78 in malignant but not benign human breast lesions
    • Fernandez PM, Tabbara SO, Jacobs LK, et al. Overexpression of the glucose-regulated stress gene GRP78 in malignant but not benign human breast lesions. Breast Cancer Res Treat 2000;59:15-26.
    • (2000) Breast Cancer Res Treat , vol.59 , pp. 15-26
    • Fernandez, P.M.1    Tabbara, S.O.2    Jacobs, L.K.3
  • 46
    • 0027958873 scopus 로고
    • The glucose-regulated proteins (GRP78 and GRP94): functions, gene regulation, and applications
    • Little E, Ramakrishnan M, Roy B, Gazit G and Lee AS. The glucose-regulated proteins (GRP78 and GRP94): functions, gene regulation, and applications. Crit Rev Eukaryot Gene Expr 1994;4:1-18.
    • (1994) Crit Rev Eukaryot Gene Expr , vol.4 , pp. 1-18
    • Little, E.1    Ramakrishnan, M.2    Roy, B.3    Gazit, G.4    Lee, A.S.5
  • 47
    • 0038216621 scopus 로고    scopus 로고
    • Activation of the ATF6, XBP1 and grp78 genes in human hepatocellular carcinoma: a possible involvement of the ER stress pathway in hepatocarcinogenesis
    • Shuda M, Kondoh N, Imazeki N, et al. Activation of the ATF6, XBP1 and grp78 genes in human hepatocellular carcinoma: a possible involvement of the ER stress pathway in hepatocarcinogenesis. J Hepatol 2003;38:605-14.
    • (2003) J Hepatol , vol.38 , pp. 605-614
    • Shuda, M.1    Kondoh, N.2    Imazeki, N.3
  • 48
    • 0348147644 scopus 로고    scopus 로고
    • Proteomic profiling of heat shock protein 70 family members as biomarkers for hepatitis C virus-related hepatocellular carcinoma
    • Takashima M, Kuramitsu Y, Yokoyama Y, et al. Proteomic profiling of heat shock protein 70 family members as biomarkers for hepatitis C virus-related hepatocellular carcinoma. Proteomics 2003;3:2487-93.
    • (2003) Proteomics , vol.3 , pp. 2487-2493
    • Takashima, M.1    Kuramitsu, Y.2    Yokoyama, Y.3
  • 51
    • 0034674703 scopus 로고    scopus 로고
    • Role of peroxiredoxins in regulating intracellular hydrogen peroxide and hydrogen peroxide-induced apoptosis in thyroid cells
    • Kim H, Lee TH, Park ES, et al. Role of peroxiredoxins in regulating intracellular hydrogen peroxide and hydrogen peroxide-induced apoptosis in thyroid cells. J Biol Chem 2000;275:18266-70.
    • (2000) J Biol Chem , vol.275 , pp. 18266-18270
    • Kim, H.1    Lee, T.H.2    Park, E.S.3
  • 52
    • 16344381930 scopus 로고    scopus 로고
    • Proteomic profiling for cancer progression: Differential display analysis for the expression of intracellular proteins between regressive and progressive cancer cell lines
    • Hayashi E, Kuramitsu Y, Okada F, et al. Proteomic profiling for cancer progression: Differential display analysis for the expression of intracellular proteins between regressive and progressive cancer cell lines. Proteomics 2005;5:1024-32.
    • (2005) Proteomics , vol.5 , pp. 1024-1032
    • Hayashi, E.1    Kuramitsu, Y.2    Okada, F.3
  • 53
    • 0036190624 scopus 로고    scopus 로고
    • Overexpression of peroxiredoxins I, II, III, V, and VI in malignant mesothelioma
    • Kinnula VL, Lehtonen S, Sormunen R, et al. Overexpression of peroxiredoxins I, II, III, V, and VI in malignant mesothelioma. J Pathol 2002;196:316-23.
    • (2002) J Pathol , vol.196 , pp. 316-323
    • Kinnula, V.L.1    Lehtonen, S.2    Sormunen, R.3
  • 54
    • 3843146451 scopus 로고    scopus 로고
    • Peroxiredoxins, a novel protein family in lung cancer
    • Lehtonen ST, Svensk AM, Soini Y, et al. Peroxiredoxins, a novel protein family in lung cancer. Int J Cancer 2004;111:514-21.
    • (2004) Int J Cancer , vol.111 , pp. 514-521
    • Lehtonen, S.T.1    Svensk, A.M.2    Soini, Y.3
  • 55
    • 0030952278 scopus 로고    scopus 로고
    • Annexin V-mediated calcium flux across membranes is dependent on the lipid composition: implications for cartilage mineralization
    • Kirsch T, Nah HD, Demuth DR, et al. Annexin V-mediated calcium flux across membranes is dependent on the lipid composition: implications for cartilage mineralization. Biochemistry 1997;36:3359-67.
    • (1997) Biochemistry , vol.36 , pp. 3359-3367
    • Kirsch, T.1    Nah, H.D.2    Demuth, D.R.3
  • 56
    • 15044352161 scopus 로고    scopus 로고
    • and terminal differentiation of growth plate chondrocytes
    • Wang W, Xu J and Kirsch T. Annexin V and terminal differentiation of growth plate chondrocytes. Exp Cell Res 2005;305:156-65.
    • (2005) Exp Cell Res , vol.305 , pp. 156-165
    • Wang, W.1    Xu, J.2    Kirsch, T.3    Annexin, V.4
  • 57
    • 0842265979 scopus 로고    scopus 로고
    • Expression, subcellular localization and phosphorylation status of annexins 1 and 5 in human pituitary adenomas and a growth hormone-secreting carcinoma
    • Mulla A, Christian HC, Solito E, Mendoza N, Morris JF and Buckingham JC. Expression, subcellular localization and phosphorylation status of annexins 1 and 5 in human pituitary adenomas and a growth hormone-secreting carcinoma. Clin Endocrinol (Oxf) 2004;60:107-19.
    • (2004) Clin Endocrinol (Oxf) , vol.60 , pp. 107-119
    • Mulla, A.1    Christian, H.C.2    Solito, E.3    Mendoza, N.4    Morris, J.F.5    Buckingham, J.C.6
  • 58
    • 0037031320 scopus 로고    scopus 로고
    • Actin dynamics: tropomyosin provides stability
    • Cooper JA. Actin dynamics: tropomyosin provides stability. Curr Biol 2002;12:R523-5.
    • (2002) Curr Biol , vol.12
    • Cooper, J.A.1
  • 59
    • 0032426217 scopus 로고    scopus 로고
    • Structural interactions between actin, tropomyosin, caldesmon and calcium binding protein and the regulation of smooth muscle thin filaments
    • Marston S, Burton D, Copeland O, et al. Structural interactions between actin, tropomyosin, caldesmon and calcium binding protein and the regulation of smooth muscle thin filaments. Acta Physiol Scand 1998;164:401-14.
    • (1998) Acta Physiol Scand , vol.164 , pp. 401-414
    • Marston, S.1    Burton, D.2    Copeland, O.3
  • 60
    • 85045351537 scopus 로고    scopus 로고
    • The coordination between actin filaments and adhesion in mesenchymal migration
    • O'Neill GM. The coordination between actin filaments and adhesion in mesenchymal migration. Cell Adh Migr 2009;3:355-7.
    • (2009) Cell Adh Migr , vol.3 , pp. 355-357
    • O'Neill, G.M.1
  • 61
    • 0030583279 scopus 로고    scopus 로고
    • Decreased expression of a single tropomyosin isoform, TM5/TM30nm, results in reduction in motility of highly metastatic B16-F10 mouse melanoma cells
    • Miyado K, Kimura M and Taniguchi S. Decreased expression of a single tropomyosin isoform, TM5/TM30nm, results in reduction in motility of highly metastatic B16-F10 mouse melanoma cells. Biochem Biophys Res Commun 1996;225:427-35.
    • (1996) Biochem Biophys Res Commun , vol.225 , pp. 427-435
    • Miyado, K.1    Kimura, M.2    Taniguchi, S.3
  • 62
    • 14644419579 scopus 로고    scopus 로고
    • Green tea extract modulates actin remodeling via Rho activity in an in vitro multistep carcinogenic model
    • Lu QY, Jin YS, Pantuck A, et al. Green tea extract modulates actin remodeling via Rho activity in an in vitro multistep carcinogenic model. Clin Cancer Res 2005;11:1675-83.
    • (2005) Clin Cancer Res , vol.11 , pp. 1675-1683
    • Lu, Q.Y.1    Jin, Y.S.2    Pantuck, A.3
  • 63
    • 29644432909 scopus 로고    scopus 로고
    • Suppression of cancer phenotypes through a multifunctional actin-binding protein, calponin, that attacks cancer cells and simultaneously protects the host from invasion
    • Taniguchi S. Suppression of cancer phenotypes through a multifunctional actin-binding protein, calponin, that attacks cancer cells and simultaneously protects the host from invasion. Cancer Sci 2005;96:738-46.
    • (2005) Cancer Sci , vol.96 , pp. 738-746
    • Taniguchi, S.1
  • 65
    • 0035916216 scopus 로고    scopus 로고
    • Identification by mass spectrometry of a new alpha-tubulin isotype expressed in human breast and lung carcinoma cell lines
    • Rao S, Aberg F, Nieves E, Band Horwitz S and Orr GA. Identification by mass spectrometry of a new alpha-tubulin isotype expressed in human breast and lung carcinoma cell lines. Biochemistry 2001;40:2096-103.
    • (2001) Biochemistry , vol.40 , pp. 2096-2103
    • Rao, S.1    Aberg, F.2    Nieves, E.3    Band Horwitz, S.4    Orr, G.A.5
  • 67
    • 3843133014 scopus 로고    scopus 로고
    • Three steps to cancer: how phosphorylation of tubulin, tubulin tyrosine ligase and P-glycoprotein may generate and sustain cancer
    • Idriss HT. Three steps to cancer: how phosphorylation of tubulin, tubulin tyrosine ligase and P-glycoprotein may generate and sustain cancer. Cancer Chemother Pharmacol 2004;54:101-4.
    • (2004) Cancer Chemother Pharmacol , vol.54 , pp. 101-104
    • Idriss, H.T.1
  • 68
    • 0035393707 scopus 로고    scopus 로고
    • Tubulin detyrosination is a frequent occurrence in breast cancers of poor prognosis
    • Mialhe A, Lafanechere L, Treilleux I, et al. Tubulin detyrosination is a frequent occurrence in breast cancers of poor prognosis. Cancer Res 2001;61:5024-7.
    • (2001) Cancer Res , vol.61 , pp. 5024-5027
    • Mialhe, A.1    Lafanechere, L.2    Treilleux, I.3
  • 69
    • 0036842141 scopus 로고    scopus 로고
    • Sali-vary cystatins induce interleukin-6 expression via cell surface molecules in human gingival fibroblasts
    • Kato T, Imatani T, Minaguchi K, Saitoh E and Okuda K. Sali-vary cystatins induce interleukin-6 expression via cell surface molecules in human gingival fibroblasts. Mol Immunol 2002;39:423-30.
    • (2002) Mol Immunol , vol.39 , pp. 423-430
    • Kato, T.1    Imatani, T.2    Minaguchi, K.3    Saitoh, E.4    Okuda, K.5
  • 70
    • 0024692293 scopus 로고
    • Tissue distribution of RNAs for cystatins, histatins, statherin, and proline-rich salivary proteins in humans and macaques
    • Sabatini LM, Warner TF, Saitoh E and Azen EA. Tissue distribution of RNAs for cystatins, histatins, statherin, and proline-rich salivary proteins in humans and macaques. J Dent Res 1989;68:1138-45.
    • (1989) J Dent Res , vol.68 , pp. 1138-1145
    • Sabatini, L.M.1    Warner, T.F.2    Saitoh, E.3    Azen, E.A.4
  • 71
    • 2942716692 scopus 로고    scopus 로고
    • Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasiveness
    • Eustace BK, Sakurai T, Stewart JK, et al. Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasiveness. Nat Cell Biol 2004;6:507-14.
    • (2004) Nat Cell Biol , vol.6 , pp. 507-514
    • Eustace, B.K.1    Sakurai, T.2    Stewart, J.K.3
  • 72
    • 33646580678 scopus 로고    scopus 로고
    • Mislocalization and unconventional functions of cellular MMPs in cancer
    • Strongin AY. Mislocalization and unconventional functions of cellular MMPs in cancer. Cancer Metastasis Rev 2006;25:87-98.
    • (2006) Cancer Metastasis Rev , vol.25 , pp. 87-98
    • Strongin, A.Y.1


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