메뉴 건너뛰기




Volumn 439, Issue 2, 2013, Pages 203-208

EpCAM associates with endoplasmic reticulum aminopeptidase 2 (ERAP2) in breast cancer cells

Author keywords

Cleavage; Co localization; EpCAM; ERAP2; Glycosylation

Indexed keywords

ENDOPLASMIC RETICULUM AMINOPEPTIDASE 2; EPITHELIAL CELL ADHESION MOLECULE; PROTEINASE; UNCLASSIFIED DRUG;

EID: 84884283268     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.08.059     Document Type: Article
Times cited : (18)

References (32)
  • 1
    • 0034767957 scopus 로고    scopus 로고
    • Cancer burden in the year 2000. The global picture
    • Parkin D.M., Bray F.I., Devesa S.S. Cancer burden in the year 2000. The global picture. Eur. J. Cancer 2001, 37(Suppl.8):S4-S66.
    • (2001) Eur. J. Cancer , vol.37 , Issue.SUPPL.8
    • Parkin, D.M.1    Bray, F.I.2    Devesa, S.S.3
  • 3
    • 0028350104 scopus 로고
    • Ep-CAM: a human epithelial antigen is a homophilic cell-cell adhesion molecule
    • Litvinov S.V., Velders M.P., Bakker H.A., et al. Ep-CAM: a human epithelial antigen is a homophilic cell-cell adhesion molecule. J. Cell Biol. 1994, 125:437-446.
    • (1994) J. Cell Biol. , vol.125 , pp. 437-446
    • Litvinov, S.V.1    Velders, M.P.2    Bakker, H.A.3
  • 4
    • 33846804010 scopus 로고    scopus 로고
    • EpCAM (CD326) finding its role in cancer
    • Baeuerle P.A., Gires O. EpCAM (CD326) finding its role in cancer. Br. J. Cancer 2007, 96:417-423.
    • (2007) Br. J. Cancer , vol.96 , pp. 417-423
    • Baeuerle, P.A.1    Gires, O.2
  • 6
    • 0028144072 scopus 로고
    • Evidence for a role of the epithelial glycoprotein 40 (Ep-CAM) in epithelial cell-cell adhesion
    • Litvinov S.V., Bakker H.A., Gourevitch M.M., et al. Evidence for a role of the epithelial glycoprotein 40 (Ep-CAM) in epithelial cell-cell adhesion. Cell Adhes. Commun. 1994, 2:417-428.
    • (1994) Cell Adhes. Commun. , vol.2 , pp. 417-428
    • Litvinov, S.V.1    Bakker, H.A.2    Gourevitch, M.M.3
  • 7
    • 0031827033 scopus 로고    scopus 로고
    • Cytoplasmic tail regulates the intercellular adhesion function of the epithelial cell adhesion molecule
    • Balzar M., Bakker H.A., Briaire-de-Bruijn I.H., et al. Cytoplasmic tail regulates the intercellular adhesion function of the epithelial cell adhesion molecule. Mol. Cell. Biol. 1998, 18:4833-4843.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4833-4843
    • Balzar, M.1    Bakker, H.A.2    Briaire-de-Bruijn, I.H.3
  • 8
    • 0035105519 scopus 로고    scopus 로고
    • Epidermal growth factor-like repeats mediate lateral and reciprocal interactions of Ep-CAM molecules in homophilic adhesions
    • Balzar M., Briaire-de Bruijn I.H., Rees-Bakker H.A., et al. Epidermal growth factor-like repeats mediate lateral and reciprocal interactions of Ep-CAM molecules in homophilic adhesions. Mol. Cell. Biol. 2001, 21:2570-2580.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2570-2580
    • Balzar, M.1    Briaire-de Bruijn, I.H.2    Rees-Bakker, H.A.3
  • 9
    • 59749103834 scopus 로고    scopus 로고
    • Nuclear signalling by tumour-associated antigen EpCAM
    • Maetzel D., Denzel S., Mack B., et al. Nuclear signalling by tumour-associated antigen EpCAM. Nat. Cell Biol. 2009, 11:162-171.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 162-171
    • Maetzel, D.1    Denzel, S.2    Mack, B.3
  • 10
    • 0025362976 scopus 로고
    • Association of the 323/A3 surface glycoprotein with tumor characteristics and behavior in human breast cancer
    • Tandon A.K., Clark G.M., Chamness G.C., et al. Association of the 323/A3 surface glycoprotein with tumor characteristics and behavior in human breast cancer. Cancer Res. 1990, 50:3317-3321.
    • (1990) Cancer Res. , vol.50 , pp. 3317-3321
    • Tandon, A.K.1    Clark, G.M.2    Chamness, G.C.3
  • 11
    • 33750165279 scopus 로고    scopus 로고
    • Overexpression of epithelial cell adhesion molecule (Ep-CAM) is an independent prognostic marker for reduced survival of patients with epithelial ovarian cancer
    • Spizzo G., Went P., Dirnhofer S., et al. Overexpression of epithelial cell adhesion molecule (Ep-CAM) is an independent prognostic marker for reduced survival of patients with epithelial ovarian cancer. Gynecol. Oncol. 2006, 103:483-488.
    • (2006) Gynecol. Oncol. , vol.103 , pp. 483-488
    • Spizzo, G.1    Went, P.2    Dirnhofer, S.3
  • 12
    • 60649111501 scopus 로고    scopus 로고
    • EpCAM: another surface-to-nucleus missile
    • Carpenter G., Red Brewer M. EpCAM: another surface-to-nucleus missile. Cancer Cell 2009, 15:165-166.
    • (2009) Cancer Cell , vol.15 , pp. 165-166
    • Carpenter, G.1    Red Brewer, M.2
  • 13
    • 4143065769 scopus 로고    scopus 로고
    • The carcinoma-associated antigen EpCAM upregulates c-myc and induces cell proliferation
    • Munz M., Kieu C., Mack B., et al. The carcinoma-associated antigen EpCAM upregulates c-myc and induces cell proliferation. Oncogene 2004, 23:5748-5758.
    • (2004) Oncogene , vol.23 , pp. 5748-5758
    • Munz, M.1    Kieu, C.2    Mack, B.3
  • 14
    • 67651003100 scopus 로고    scopus 로고
    • The emerging role of EpCAM in cancer and stem cell signaling
    • Munz M., Baeuerle P.A., Gires O. The emerging role of EpCAM in cancer and stem cell signaling. Cancer Res. 2009, 69:5627-5629.
    • (2009) Cancer Res. , vol.69 , pp. 5627-5629
    • Munz, M.1    Baeuerle, P.A.2    Gires, O.3
  • 15
    • 0042357061 scopus 로고    scopus 로고
    • Human leukocyte-derived arginine aminopeptidase. The third member of the oxytocinase subfamily of aminopeptidases
    • Tanioka T., Hattori A., Masuda S., et al. Human leukocyte-derived arginine aminopeptidase. The third member of the oxytocinase subfamily of aminopeptidases. J. Biol. Chem. 2003, 278:32275-32283.
    • (2003) J. Biol. Chem. , vol.278 , pp. 32275-32283
    • Tanioka, T.1    Hattori, A.2    Masuda, S.3
  • 16
    • 77955332608 scopus 로고    scopus 로고
    • Endoplasmic reticulum aminopeptidases: biology and pathogenic potential
    • Haroon N., Inman R.D. Endoplasmic reticulum aminopeptidases: biology and pathogenic potential. Nat. Rev. Rheumatol. 2010, 6:461-467.
    • (2010) Nat. Rev. Rheumatol. , vol.6 , pp. 461-467
    • Haroon, N.1    Inman, R.D.2
  • 17
    • 22144442460 scopus 로고    scopus 로고
    • Concerted peptide trimming by human ERAP1 and ERAP2 aminopeptidase complexes in the endoplasmic reticulum
    • Saveanu L., Carroll O., Lindo V., et al. Concerted peptide trimming by human ERAP1 and ERAP2 aminopeptidase complexes in the endoplasmic reticulum. Nat. Immunol. 2005, 6:689-697.
    • (2005) Nat. Immunol. , vol.6 , pp. 689-697
    • Saveanu, L.1    Carroll, O.2    Lindo, V.3
  • 18
    • 0037015624 scopus 로고    scopus 로고
    • ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum
    • Serwold T., Gonzalez F., Kim J., Jacob R., et al. ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum. Nature 2002, 419:480-483.
    • (2002) Nature , vol.419 , pp. 480-483
    • Serwold, T.1    Gonzalez, F.2    Kim, J.3    Jacob, R.4
  • 19
    • 58549113573 scopus 로고    scopus 로고
    • Anti-epithelial cell adhesion molecule antibodies and the detection of circulating normal-like breast tumor cells
    • Sieuwerts A.M., Kraan J., Bolt J., et al. Anti-epithelial cell adhesion molecule antibodies and the detection of circulating normal-like breast tumor cells. J. Natl. Cancer Inst. 2009, 101:61-66.
    • (2009) J. Natl. Cancer Inst. , vol.101 , pp. 61-66
    • Sieuwerts, A.M.1    Kraan, J.2    Bolt, J.3
  • 20
    • 33845209913 scopus 로고    scopus 로고
    • A collection of breast cancer cell lines for the study of functionally distinct cancer subtypes
    • Neve R.M., Chin K., Fridlyand J., et al. A collection of breast cancer cell lines for the study of functionally distinct cancer subtypes. Cancer Cell 2006, 10:515-527.
    • (2006) Cancer Cell , vol.10 , pp. 515-527
    • Neve, R.M.1    Chin, K.2    Fridlyand, J.3
  • 21
    • 0024394362 scopus 로고
    • Context effects and inefficient initiation at non-AUG codons in eucaryotic cell-free translation systems
    • Kozak M. Context effects and inefficient initiation at non-AUG codons in eucaryotic cell-free translation systems. Mol. Cell. Biol. 1989, 9:5073-5080.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 5073-5080
    • Kozak, M.1
  • 22
    • 33645966850 scopus 로고    scopus 로고
    • Membrane topology of the human seipin protein
    • Lundin C., Nordstrom R., Wagner K., et al. Membrane topology of the human seipin protein. FEBS Lett. 2006, 580:2281-2284.
    • (2006) FEBS Lett. , vol.580 , pp. 2281-2284
    • Lundin, C.1    Nordstrom, R.2    Wagner, K.3
  • 23
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for cotranslational protein translocation
    • Walter P., Blobel G. Preparation of microsomal membranes for cotranslational protein translocation. Methods Enzymol. 1983, 96:84-93.
    • (1983) Methods Enzymol. , vol.96 , pp. 84-93
    • Walter, P.1    Blobel, G.2
  • 24
    • 0027263346 scopus 로고
    • Positively charged amino acids placed next to a signal sequence block protein translocation more efficiently in Escherichia coli than in mammalian microsomes
    • Johansson M., Nilsson I., von Heijne G. Positively charged amino acids placed next to a signal sequence block protein translocation more efficiently in Escherichia coli than in mammalian microsomes. Mol. Gen. Genet. 1993, 239:251-256.
    • (1993) Mol. Gen. Genet. , vol.239 , pp. 251-256
    • Johansson, M.1    Nilsson, I.2    von Heijne, G.3
  • 25
    • 13444262028 scopus 로고    scopus 로고
    • Recognition of transmembrane helices by the endoplasmic reticulum translocon
    • Hessa T., Kim H., Bihlmaier K., et al. Recognition of transmembrane helices by the endoplasmic reticulum translocon. Nature 2005, 433:377-381.
    • (2005) Nature , vol.433 , pp. 377-381
    • Hessa, T.1    Kim, H.2    Bihlmaier, K.3
  • 26
    • 0035937123 scopus 로고    scopus 로고
    • Determination of disulfide bond assignments and N-glycosylation sites of the human gastrointestinal carcinoma antigen GA733-2 (CO17-1A, EGP, KS1-4, KSA, and Ep-CAM)
    • Chong J.M., Speicher D.W. Determination of disulfide bond assignments and N-glycosylation sites of the human gastrointestinal carcinoma antigen GA733-2 (CO17-1A, EGP, KS1-4, KSA, and Ep-CAM). J. Biol. Chem. 2001, 276:5804-5813.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5804-5813
    • Chong, J.M.1    Speicher, D.W.2
  • 27
    • 42649142623 scopus 로고    scopus 로고
    • Glycosylation is crucial for stability of tumour and cancer stem cell antigen EpCAM
    • Munz M., Fellinger K., Hofmann T., et al. Glycosylation is crucial for stability of tumour and cancer stem cell antigen EpCAM. Front. Biosci. 2008, 13:5195-5201.
    • (2008) Front. Biosci. , vol.13 , pp. 5195-5201
    • Munz, M.1    Fellinger, K.2    Hofmann, T.3
  • 28
    • 57349168025 scopus 로고    scopus 로고
    • Molecular code for protein insertion in the endoplasmic reticulum membrane is similar for N(in)-C(out) and N(out)-C(in) transmembrane helices
    • Lundin C., Kim H., Nilsson I., White S.H. Molecular code for protein insertion in the endoplasmic reticulum membrane is similar for N(in)-C(out) and N(out)-C(in) transmembrane helices. Proc. Natl. Acad. Sci. USA 2008, 105:15702-15707.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 15702-15707
    • Lundin, C.1    Kim, H.2    Nilsson, I.3    White, S.H.4
  • 29
    • 0028101487 scopus 로고
    • The COOH-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase
    • Nilsson I., Whitley P., von Heijne G. The COOH-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase. J. Cell Biol. 1994, 126:1127-1132.
    • (1994) J. Cell Biol. , vol.126 , pp. 1127-1132
    • Nilsson, I.1    Whitley, P.2    von Heijne, G.3
  • 30
    • 84880586512 scopus 로고    scopus 로고
    • N-linked protein glycosylation in the ER
    • Aebi M. N-linked protein glycosylation in the ER. Biochim. Biophys. Acta. 2013.
    • (2013) Biochim. Biophys. Acta.
    • Aebi, M.1
  • 31
    • 0036679366 scopus 로고    scopus 로고
    • Identification of ARTS-1 as a novel TNFR1-binding protein that promotes TNFR1 ectodomain shedding
    • Cui X., Hawari F., Alsaaty S., et al. Identification of ARTS-1 as a novel TNFR1-binding protein that promotes TNFR1 ectodomain shedding. J. Clin. Invest. 2002, 110:515-526.
    • (2002) J. Clin. Invest. , vol.110 , pp. 515-526
    • Cui, X.1    Hawari, F.2    Alsaaty, S.3
  • 32
    • 0030048075 scopus 로고    scopus 로고
    • Expression of gp40, the murine homologue of human epithelial cell adhesion molecule (Ep-CAM), by murine dendritic cells
    • Borkowski T.A., Nelson A.J., Farr A.G., et al. Expression of gp40, the murine homologue of human epithelial cell adhesion molecule (Ep-CAM), by murine dendritic cells. Eur. J. Immunol. 1996, 26:110-114.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 110-114
    • Borkowski, T.A.1    Nelson, A.J.2    Farr, A.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.