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Volumn 2, Issue 1, 2008, Pages 99-107

Proteomic characterization of differentially expressed proteins in breast cancer: Expression of hnRNP H1, RKIP and GRP78 is strongly associated with HER-2/neu status

Author keywords

Breast cancer; HER 2; Neu oncogene; Tissue microarray

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR 2; GLUCOSE REGULATED PROTEIN 78; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN H1; NEU DIFFERENTIATION FACTOR; NEU DIFFERENTIATION FACTOR ALPHA1; PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN; PROTEOME; UNCLASSIFIED DRUG;

EID: 38949187296     PISSN: 18628346     EISSN: None     Source Type: Journal    
DOI: 10.1002/prca.200780099     Document Type: Article
Times cited : (20)

References (34)
  • 1
    • 0035829688 scopus 로고    scopus 로고
    • ErbB2-overexpressing human mammary carcinoma cells display an increased requirement for the phosphatidylinositol 3-kinase signaling pathway in anchorage-independent growth
    • Hermanto, U., Zong, C. S., Wang, L-H., ErbB2-overexpressing human mammary carcinoma cells display an increased requirement for the phosphatidylinositol 3-kinase signaling pathway in anchorage-independent growth. Oncogene 2001, 20, 7551-7562.
    • (2001) Oncogene , vol.20 , pp. 7551-7562
    • Hermanto, U.1    Zong, C.S.2    Wang, L.-H.3
  • 2
    • 0033106477 scopus 로고    scopus 로고
    • Heregulin beta1-activated phosphatidylinositol 3-kinase enhances aggregation of MCF-7 breast cancer cells independent of extracellular signal-regulated kinase
    • Tan, M., Grijalva, R., Yu, D., Heregulin beta1-activated phosphatidylinositol 3-kinase enhances aggregation of MCF-7 breast cancer cells independent of extracellular signal-regulated kinase. Cancer Res. 1999, 59, 1620-1625.
    • (1999) Cancer Res , vol.59 , pp. 1620-1625
    • Tan, M.1    Grijalva, R.2    Yu, D.3
  • 4
    • 0242694519 scopus 로고    scopus 로고
    • HER-2-targeted therapy. Lessons learned and future directions
    • Nahta, R., Esteva, F. J., HER-2-targeted therapy. Lessons learned and future directions. Clin. Cancer Res. 2003, 9, 5078-5084.
    • (2003) Clin. Cancer Res , vol.9 , pp. 5078-5084
    • Nahta, R.1    Esteva, F.J.2
  • 5
    • 0037516860 scopus 로고    scopus 로고
    • cDNA microarray analysis of genes associated with ERBB2 (HER2/neu) overexpression in human mammary luminal epithelial cells
    • MacKay, A., Jones, C., Dexter, T., Silva, R. L et al., cDNA microarray analysis of genes associated with ERBB2 (HER2/neu) overexpression in human mammary luminal epithelial cells. Oncogene 2003, 22, 2680-2688.
    • (2003) Oncogene , vol.22 , pp. 2680-2688
    • MacKay, A.1    Jones, C.2    Dexter, T.3    Silva, R.L.4
  • 6
    • 0036792564 scopus 로고    scopus 로고
    • Differential gene expression patterns in HER2/neu-positive and -negative breast cancer cell lines and tissues
    • Wilson, K. S., Roberts, H., Leek, R., Harris, A. L., Geradts, J., Differential gene expression patterns in HER2/neu-positive and -negative breast cancer cell lines and tissues. Am. J. Pathol. 2002, 161, 1171-1185.
    • (2002) Am. J. Pathol , vol.161 , pp. 1171-1185
    • Wilson, K.S.1    Roberts, H.2    Leek, R.3    Harris, A.L.4    Geradts, J.5
  • 7
    • 33750696663 scopus 로고    scopus 로고
    • Effects of HER2 overexpression on cell signaling networks governing proliferation and migration
    • Wolf-Yadlin, A., Kumar, N., Zhang, Y., Hautaniemi, S. et al., Effects of HER2 overexpression on cell signaling networks governing proliferation and migration. Mol. Syst Biol. 2006, 2, 54.
    • (2006) Mol. Syst Biol , vol.2 , pp. 54
    • Wolf-Yadlin, A.1    Kumar, N.2    Zhang, Y.3    Hautaniemi, S.4
  • 8
    • 33745585792 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of HER-2/neu signaling and inhibition
    • Bose, R., Molina, H., Patterson, A. S., Bitok, J. K. et al., Phosphoproteomic analysis of HER-2/neu signaling and inhibition. Proc. Natl. Acad. Sci. USA 2006, 103, 9773-9778.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 9773-9778
    • Bose, R.1    Molina, H.2    Patterson, A.S.3    Bitok, J.K.4
  • 9
    • 33846559384 scopus 로고    scopus 로고
    • Multivariable difference gel electrophoresis and mass spectrometry: A case study on transforming growth factor-beta and ERBB2 signaling
    • Friedman, D. B., Wang, S. E., Whitwell, C. W., Caprioli, R. M., Arteaga, C. L, Multivariable difference gel electrophoresis and mass spectrometry: A case study on transforming growth factor-beta and ERBB2 signaling. Mol. Cell. Proteomics 2007, 6, 150-169.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 150-169
    • Friedman, D.B.1    Wang, S.E.2    Whitwell, C.W.3    Caprioli, R.M.4    Arteaga, C.L.5
  • 10
    • 0036463947 scopus 로고    scopus 로고
    • Evaluation of two-dimensional differential gel electrophoresis for proteomic expression analysis of a model breast cancer cell system
    • Gharbi, S., Gaffney, P., Yang, A., Zvelebil, M. J. et al., Evaluation of two-dimensional differential gel electrophoresis for proteomic expression analysis of a model breast cancer cell system. Mol. Cell. Proteomics 2002, 1, 91-98.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 91-98
    • Gharbi, S.1    Gaffney, P.2    Yang, A.3    Zvelebil, M.J.4
  • 11
    • 0037226462 scopus 로고    scopus 로고
    • Transcriptome analysis of HER2 reveals a molecular connection to fatty acid synthesis
    • Kumar-Sinha, C., Ignatoski, K. W., Lippman, M. E., Ethier, S. P., Chinnaiyan, A. M., Transcriptome analysis of HER2 reveals a molecular connection to fatty acid synthesis. Cancer Res. 2003, 63, 132-139.
    • (2003) Cancer Res , vol.63 , pp. 132-139
    • Kumar-Sinha, C.1    Ignatoski, K.W.2    Lippman, M.E.3    Ethier, S.P.4    Chinnaiyan, A.M.5
  • 12
    • 18844363152 scopus 로고    scopus 로고
    • Proteomics of breast cancer: Enhanced expression of cytokeratin 19 in human epidermal growth factor receptor type 2 positive breast tumors
    • Zhang, D., Tai, L. K., Wong, L L., Sethi, S. K., Koay, E. S. C., Proteomics of breast cancer: Enhanced expression of cytokeratin 19 in human epidermal growth factor receptor type 2 positive breast tumors. Proteomics 2005, 5, 1797-1805.
    • (2005) Proteomics , vol.5 , pp. 1797-1805
    • Zhang, D.1    Tai, L.K.2    Wong, L.L.3    Sethi, S.K.4    Koay, E.S.C.5
  • 13
    • 28644439593 scopus 로고    scopus 로고
    • Proteomic study reveals that proteins involved in metabolic and detoxification pathways are highly expressed in HER-2/neu-positive breast cancer
    • Zhang, D., Tai, L. K., Wong, L L, Chiu, L-L at al., Proteomic study reveals that proteins involved in metabolic and detoxification pathways are highly expressed in HER-2/neu-positive breast cancer. Mol. Cell. Proteomics 2005, 4, 1686-1696.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1686-1696
    • Zhang, D.1    Tai, L.K.2    Wong, L.L.3    Chiu, L.-L.4    at al5
  • 14
    • 4143071652 scopus 로고    scopus 로고
    • The role of Raf kinase inhibitor protein (RKIP) in health and disease
    • Keller, E. T., Fu, Z., Brennan, M., The role of Raf kinase inhibitor protein (RKIP) in health and disease. Biochem. Pharmacol. 2004, 68, 1049-1053.
    • (2004) Biochem. Pharmacol , vol.68 , pp. 1049-1053
    • Keller, E.T.1    Fu, Z.2    Brennan, M.3
  • 15
    • 0028881190 scopus 로고
    • Cell type-specific expression of hnRNP proteins
    • Kamma, H., Portman, D. S., Droyfuss, G., Cell type-specific expression of hnRNP proteins. Exp. Cell Res. 1995, 221, 187-196.
    • (1995) Exp. Cell Res , vol.221 , pp. 187-196
    • Kamma, H.1    Portman, D.S.2    Droyfuss, G.3
  • 16
    • 0035423875 scopus 로고    scopus 로고
    • The glucose-regulated proteins: Stress induction and clinical applications
    • Lee, A. S., The glucose-regulated proteins: stress induction and clinical applications. Trends Biochem. Sci. 2001, 26, 504-510.
    • (2001) Trends Biochem. Sci , vol.26 , pp. 504-510
    • Lee, A.S.1
  • 17
    • 33947547741 scopus 로고    scopus 로고
    • Quantitative transcriptional control of ErbB receptor signaling undergoes graded to biphasic response for cell differentiation
    • Nagashima, T., Shimodaira, H., Ide, K., Nakakuki, T. et al., Quantitative transcriptional control of ErbB receptor signaling undergoes graded to biphasic response for cell differentiation. J. Biol. Chem. 2007, 282, 4045-4056.
    • (2007) J. Biol. Chem , vol.282 , pp. 4045-4056
    • Nagashima, T.1    Shimodaira, H.2    Ide, K.3    Nakakuki, T.4
  • 18
    • 0033539167 scopus 로고    scopus 로고
    • Suppression of Raf-1 kinase activity and MAP kinase signalling by RKIP
    • Yeung, K., Seitz, T., Li, S., Janosch, P. et al., Suppression of Raf-1 kinase activity and MAP kinase signalling by RKIP. Nature 1999, 401, 173-177.
    • (1999) Nature , vol.401 , pp. 173-177
    • Yeung, K.1    Seitz, T.2    Li, S.3    Janosch, P.4
  • 19
    • 0034003003 scopus 로고    scopus 로고
    • Mechanism of suppression of the Raf(MEK/extracellular signal-regulated kinase pathway by the raf kinase inhibitor protein
    • Yeung, K., Janosch, P., McFerran, B., Rose, D. W. et al., Mechanism of suppression of the Raf(MEK/extracellular signal-regulated kinase pathway by the raf kinase inhibitor protein. Mol. Cell. Biol. 2000, 20, 3079-3085.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 3079-3085
    • Yeung, K.1    Janosch, P.2    McFerran, B.3    Rose, D.W.4
  • 20
    • 0038275924 scopus 로고    scopus 로고
    • Effects of raf kinase inhibitor protein expression on suppression of prostate cancer metastasis
    • Fu, Z., Smith, P. C., Zhang, L., Rubin, M. A. et al., Effects of raf kinase inhibitor protein expression on suppression of prostate cancer metastasis. J. Natl. Cancer Inst. 2003, 95, 878-889.
    • (2003) J. Natl. Cancer Inst , vol.95 , pp. 878-889
    • Fu, Z.1    Smith, P.C.2    Zhang, L.3    Rubin, M.A.4
  • 21
    • 27144473329 scopus 로고    scopus 로고
    • Reduction of Raf-1 kinase inhibitor protein expression correlates with breast cancer metastasis
    • Hagan, S., Al-Mulla, F., Mallon, E., Olen, K. et al., Reduction of Raf-1 kinase inhibitor protein expression correlates with breast cancer metastasis. Clin. Cancer Res. 2005, 11, 7392-7397.
    • (2005) Clin. Cancer Res , vol.11 , pp. 7392-7397
    • Hagan, S.1    Al-Mulla, F.2    Mallon, E.3    Olen, K.4
  • 22
    • 0037631323 scopus 로고    scopus 로고
    • Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein
    • Corbit, K. C., Trakul, N., Eves, E. M., Diaz, B. et al., Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein. J. Biol. Chem. 2003, 278, 13061-13068.
    • (2003) J. Biol. Chem , vol.278 , pp. 13061-13068
    • Corbit, K.C.1    Trakul, N.2    Eves, E.M.3    Diaz, B.4
  • 23
    • 34249709470 scopus 로고    scopus 로고
    • Loss of raf-1 kinase inhibitor protein expression is associated with tumor progression and metastasis in colorectal cancer
    • Minoo, P., Zlobec, I., Baker, K., Tornillo, L. et al., Loss of raf-1 kinase inhibitor protein expression is associated with tumor progression and metastasis in colorectal cancer. Am. J. Clin. Pathol. 2007, 127, 820-827.
    • (2007) Am. J. Clin. Pathol , vol.127 , pp. 820-827
    • Minoo, P.1    Zlobec, I.2    Baker, K.3    Tornillo, L.4
  • 24
    • 3442894421 scopus 로고    scopus 로고
    • hnRNP H binding at the 5′ splice site correlates with the pathological effect of two intronic mutations in the NF-1 and TSH beta genes
    • Buratti, E., Baralle, M., De Conti, L., Baralle, D. et al., hnRNP H binding at the 5′ splice site correlates with the pathological effect of two intronic mutations in the NF-1 and TSH beta genes. Nucleic Acids Res. 2004, 32, 4224-4236.
    • (2004) Nucleic Acids Res , vol.32 , pp. 4224-4236
    • Buratti, E.1    Baralle, M.2    De Conti, L.3    Baralle, D.4
  • 25
    • 20744450092 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein F/H proteins modulate the alternative splicing of the apoptotic mediator Bcl-x
    • Garneau, D., Revil, T., Fisatte, J. F., Chabot B., Heterogeneous nuclear ribonucleoprotein F/H proteins modulate the alternative splicing of the apoptotic mediator Bcl-x. J. Biol. Chem. 2005, 280, 22641-22650.
    • (2005) J. Biol. Chem , vol.280 , pp. 22641-22650
    • Garneau, D.1    Revil, T.2    Fisatte, J.F.3    Chabot, B.4
  • 26
    • 0032806223 scopus 로고    scopus 로고
    • H' and F behave differently with respect to posttranslational cleavage and subcellular localization
    • Honore, B., Vorum, H., Baandrup, U., hnRNPs H, H' and F behave differently with respect to posttranslational cleavage and subcellular localization. FEBS Lett. 1999, 456, 274-280.
    • (1999) FEBS Lett , vol.456 , pp. 274-280
    • Honore, B.1    Vorum, H.2    Baandrup, U.3    hnRNPs, H.4
  • 27
    • 1242339603 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoproteins F and H/H' show differential expression in normal and selected cancer tissues
    • Honore, B., Baandrup, U., Vorum, H., Heterogeneous nuclear ribonucleoproteins F and H/H' show differential expression in normal and selected cancer tissues. Exp. Cell Res. 2004, 294, 199-209.
    • (2004) Exp. Cell Res , vol.294 , pp. 199-209
    • Honore, B.1    Baandrup, U.2    Vorum, H.3
  • 28
    • 0022780702 scopus 로고
    • Mammalian single-stranded DNA binding protein UP 1 is derived from the hnRNP core protein A1
    • Riva, S., Morandi, C., Tsoulfas, P., Pandolfo, M. et al., Mammalian single-stranded DNA binding protein UP 1 is derived from the hnRNP core protein A1. EMBO J. 1986, 5, 2267-2273.
    • (1986) EMBO J , vol.5 , pp. 2267-2273
    • Riva, S.1    Morandi, C.2    Tsoulfas, P.3    Pandolfo, M.4
  • 29
    • 15944366885 scopus 로고    scopus 로고
    • The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress
    • Lee, A. S., The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress. Methods 2005, 35, 373-381.
    • (2005) Methods , vol.35 , pp. 373-381
    • Lee, A.S.1
  • 30
    • 0038080911 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperone protein GRP78 protects calls from apoptosis induced by topoisomerase inhibitors: Role of ATP binding site in suppression of caspase-7 activation
    • Reddy, R. K., Mao, C., Baumeister, P., Austin, R. C. et al., Endoplasmic reticulum chaperone protein GRP78 protects calls from apoptosis induced by topoisomerase inhibitors: role of ATP binding site in suppression of caspase-7 activation. J. Biol. Chem. 2003, 278, 20915-20924.
    • (2003) J. Biol. Chem , vol.278 , pp. 20915-20924
    • Reddy, R.K.1    Mao, C.2    Baumeister, P.3    Austin, R.C.4
  • 31
    • 33646171070 scopus 로고    scopus 로고
    • Stress induction of GRP78/BiP and its role in cancer
    • Li, J., Lee, A. S., Stress induction of GRP78/BiP and its role in cancer. Curr. Mol. Med. 2006, 6, 45-54.
    • (2006) Curr. Mol. Med , vol.6 , pp. 45-54
    • Li, J.1    Lee, A.S.2
  • 32
    • 33748076770 scopus 로고    scopus 로고
    • GRP78 as a novel predictor of responsiveness to chemotherapy in breast cancer
    • Lee, E., Nichols, P., Spicer, D., Groshen, S. et al., GRP78 as a novel predictor of responsiveness to chemotherapy in breast cancer. Cancer Res. 2006, 66, 7849-7853.
    • (2006) Cancer Res , vol.66 , pp. 7849-7853
    • Lee, E.1    Nichols, P.2    Spicer, D.3    Groshen, S.4
  • 33
    • 0033014498 scopus 로고    scopus 로고
    • Do-regulation of GRP stress protein expression in human breast cancer cell lines
    • Gazit, G., Lu, J., Lee, A. S., Do-regulation of GRP stress protein expression in human breast cancer cell lines. Breast Cancer Res. Treat. 1999, 54, 135-146.
    • (1999) Breast Cancer Res. Treat , vol.54 , pp. 135-146
    • Gazit, G.1    Lu, J.2    Lee, A.S.3
  • 34
    • 33644941074 scopus 로고    scopus 로고
    • Decreased protein and mRNA expression of ER stress proteins GRP78 and GRP94 in HepG2 cells over-expressing CYP2E1
    • Dey, A., Kessova, I. G., Cederbaum, A. I., Decreased protein and mRNA expression of ER stress proteins GRP78 and GRP94 in HepG2 cells over-expressing CYP2E1. Arch. Biochem. Biophys. 2006, 447, 155-166.
    • (2006) Arch. Biochem. Biophys , vol.447 , pp. 155-166
    • Dey, A.1    Kessova, I.G.2    Cederbaum, A.I.3


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