메뉴 건너뛰기




Volumn 3, Issue 5, 2008, Pages

The metalloprotease meprinβ processes E-cadherin and weakens intercellular adhesion

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CATENIN; ALPHA SECRETASE; BETA CATENIN; MATRILYSIN; MEPRIN; MEPRIN BETA; PLAKOGLOBIN; UVOMORULIN; CADHERIN; MEPRIN B; METALLOPROTEINASE; RECOMBINANT PROTEIN;

EID: 47749097160     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0002153     Document Type: Article
Times cited : (64)

References (56)
  • 1
    • 0022885050 scopus 로고
    • Metalloendopeptidases of the mouse kidney brush border: Meprin and endopeptidase-24.11
    • Bond JS, Butler PE, Beynon RJ (1986) Metalloendopeptidases of the mouse kidney brush border: meprin and endopeptidase-24.11. Biomed Biochim Acta 45: 1515-1521.
    • (1986) Biomed Biochim Acta , vol.45 , pp. 1515-1521
    • Bond, J.S.1    Butler, P.E.2    Beynon, R.J.3
  • 2
    • 0023688437 scopus 로고
    • N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase: A metalloendopeptidase of the human intestinal microvillus membrane which degrades biologically active peptides
    • Sterchi EE, Naim HY, Lentze MJ, Hauri HP, Fransen JA (1988) N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase: a metalloendopeptidase of the human intestinal microvillus membrane which degrades biologically active peptides. Arch Biochem Biophys 265: 105-118.
    • (1988) Arch Biochem Biophys , vol.265 , pp. 105-118
    • Sterchi, E.E.1    Naim, H.Y.2    Lentze, M.J.3    Hauri, H.P.4    Fransen, J.A.5
  • 3
    • 0037462760 scopus 로고    scopus 로고
    • Structure of homo- and hetero-oligomeric meprin metalloproteases. Dimers, tetramers, and high molecular mass multimers
    • Bertenshaw GP, Norcum MT, Bond JS (2003) Structure of homo- and hetero-oligomeric meprin metalloproteases. Dimers, tetramers, and high molecular mass multimers. J Biol Chem 278: 2522-2532.
    • (2003) J Biol Chem , vol.278 , pp. 2522-2532
    • Bertenshaw, G.P.1    Norcum, M.T.2    Bond, J.S.3
  • 4
    • 0027360581 scopus 로고
    • Cloning of the PABA peptide hydrolase alpha subunit (PPH alpha) from human small intestine and its expression in COS-1 cells
    • Dumermuth E, Eldering JA, Grünberg J, Jiang W, Sterchi EE (1993) Cloning of the PABA peptide hydrolase alpha subunit (PPH alpha) from human small intestine and its expression in COS-1 cells. FEBS Lett 335: 367-375.
    • (1993) FEBS Lett , vol.335 , pp. 367-375
    • Dumermuth, E.1    Eldering, J.A.2    Grünberg, J.3    Jiang, W.4    Sterchi, E.E.5
  • 5
    • 0030789739 scopus 로고    scopus 로고
    • Polarised expression of human intestinal N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase (human meprin) alpha and beta subunits in Madin-Darby canine kidney cells
    • Eldering JA, Grünberg J, Hahn D, Croes HJ, Fransen JA, et al. (1997) Polarised expression of human intestinal N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase (human meprin) alpha and beta subunits in Madin-Darby canine kidney cells. Eur J Biochem 247: 920-932.
    • (1997) Eur J Biochem , vol.247 , pp. 920-932
    • Eldering, J.A.1    Grünberg, J.2    Hahn, D.3    Croes, H.J.4    Fransen, J.A.5
  • 6
    • 0013043261 scopus 로고    scopus 로고
    • N-Benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase beta (human meprinbeta). A 13-amino-acid sequence is required for proteolyticprocessing and subsequent secretion
    • Pischitzis A, Hahn D, Leuenberger B, Sterchi EE (1999) N-Benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase beta (human meprinbeta). A 13-amino-acid sequence is required for proteolyticprocessing and subsequent secretion. Eur J Biochem 261: 421-429.
    • (1999) Eur J Biochem , vol.261 , pp. 421-429
    • Pischitzis, A.1    Hahn, D.2    Leuenberger, B.3    Sterchi, E.E.4
  • 7
    • 0027361420 scopus 로고
    • Expression of the alpha subunit of PABA peptide hydrolase (EC 3.4.24.18) in MDCK cells. Synthesis and secretion of an enzymatically inactive homodimer
    • Grünberg J, Dumermuth E, Eldering JA, Sterchi EE (1993) Expression of the alpha subunit of PABA peptide hydrolase (EC 3.4.24.18) in MDCK cells. Synthesis and secretion of an enzymatically inactive homodimer. FEBS Lett 335: 376-379.
    • (1993) FEBS Lett , vol.335 , pp. 376-379
    • Grünberg, J.1    Dumermuth, E.2    Eldering, J.A.3    Sterchi, E.E.4
  • 8
    • 0037174846 scopus 로고    scopus 로고
    • Activation of human meprin-alpha in a cell culture model of colorectal cancer is triggered by the plasminogen-activating system
    • Rösmann S, Hahn D, Lottaz D, Kruse MN, Stöcker W, et al. (2002) Activation of human meprin-alpha in a cell culture model of colorectal cancer is triggered by the plasminogen-activating system. J Biol Chem 277: 40650-40658.
    • (2002) J Biol Chem , vol.277 , pp. 40650-40658
    • Rösmann, S.1    Hahn, D.2    Lottaz, D.3    Kruse, M.N.4    Stöcker, W.5
  • 9
    • 0031031671 scopus 로고    scopus 로고
    • Unveiling the substrate specificity of meprin beta on the basis of the site in protein kinase A cleaved by the kinase splitting membranal proteinase
    • Chestukhin A, Litovchick L, Muradov K, Batkin M, Shaltiel S (1997) Unveiling the substrate specificity of meprin beta on the basis of the site in protein kinase A cleaved by the kinase splitting membranal proteinase. J Biol Chem 272: 3153-3160.
    • (1997) J Biol Chem , vol.272 , pp. 3153-3160
    • Chestukhin, A.1    Litovchick, L.2    Muradov, K.3    Batkin, M.4    Shaltiel, S.5
  • 10
    • 23944491189 scopus 로고    scopus 로고
    • Generation of biologically active interleukin-1beta by meprin B
    • Herzog C, Kaushal GP, Haun RS (2005) Generation of biologically active interleukin-1beta by meprin B. Cytokine 31: 394-403.
    • (2005) Cytokine , vol.31 , pp. 394-403
    • Herzog, C.1    Kaushal, G.P.2    Haun, R.S.3
  • 11
    • 1642362446 scopus 로고    scopus 로고
    • Human meprin alpha and beta homo-oligomers: Cleavage of basement membrane proteins and sensitivity to metalloprotease inhibitors
    • Kruse MN, Becker C, Lottaz D, Köhler D, Yiallouros I, et al. (2004) Human meprin alpha and beta homo-oligomers: cleavage of basement membrane proteins and sensitivity to metalloprotease inhibitors. Biochem J 378: 383-389.
    • (2004) Biochem J , vol.378 , pp. 383-389
    • Kruse, M.N.1    Becker, C.2    Lottaz, D.3    Köhler, D.4    Yiallouros, I.5
  • 12
    • 0037622285 scopus 로고    scopus 로고
    • Heterologously overexpressed, affinity-purified human meprin alpha is functionally active and cleaves components of the basement membrane in vitro
    • Köhler D, Kruse M, Stöcker W, Sterchi EE (2000) Heterologously overexpressed, affinity-purified human meprin alpha is functionally active and cleaves components of the basement membrane in vitro. FEBS Lett 465: 2-7.
    • (2000) FEBS Lett , vol.465 , pp. 2-7
    • Köhler, D.1    Kruse, M.2    Stöcker, W.3    Sterchi, E.E.4
  • 13
    • 0035918152 scopus 로고    scopus 로고
    • Marked differences between metalloproteases meprin A and B in substrate and peptide bond specificity
    • Bertenshaw GP, Turk BE, Hubbard SJ, Matters GL, Bylander JE, et al. (2001) Marked differences between metalloproteases meprin A and B in substrate and peptide bond specificity. J Biol Chem 276: 13248-13255.
    • (2001) J Biol Chem , vol.276 , pp. 13248-13255
    • Bertenshaw, G.P.1    Turk, B.E.2    Hubbard, S.J.3    Matters, G.L.4    Bylander, J.E.5
  • 14
    • 0033104363 scopus 로고    scopus 로고
    • Nonpolarized secretion of human meprin alpha in colorectal cancer generates an increased proteolytic potential in the stroma
    • Lottaz D, Maurer CA, Hahn D, Büchler MW, Sterchi EE (1999) Nonpolarized secretion of human meprin alpha in colorectal cancer generates an increased proteolytic potential in the stroma. Cancer Res 59: 1127-1133.
    • (1999) Cancer Res , vol.59 , pp. 1127-1133
    • Lottaz, D.1    Maurer, C.A.2    Hahn, D.3    Büchler, M.W.4    Sterchi, E.E.5
  • 16
    • 1642373361 scopus 로고    scopus 로고
    • Deletion of the mouse meprin beta metalloprotease gene diminishes the ability of leukocytes to disseminate through extracellular matrix
    • Crisman JM, Zhang B, Norman LP, Bond JS (2004) Deletion of the mouse meprin beta metalloprotease gene diminishes the ability of leukocytes to disseminate through extracellular matrix. J Immunol 172: 4510-4519.
    • (2004) J Immunol , vol.172 , pp. 4510-4519
    • Crisman, J.M.1    Zhang, B.2    Norman, L.P.3    Bond, J.S.4
  • 17
    • 25444454560 scopus 로고    scopus 로고
    • Inhibitors of polyamine biosynthesis decrease the expression of the metalloproteases meprin alpha and MMP-7 in hormone-independent human breast cancer cells
    • Matters GL, Manni A, Bond JS (2005) Inhibitors of polyamine biosynthesis decrease the expression of the metalloproteases meprin alpha and MMP-7 in hormone-independent human breast cancer cells. Clin Exp Metastasis 22: 331-339.
    • (2005) Clin Exp Metastasis , vol.22 , pp. 331-339
    • Matters, G.L.1    Manni, A.2    Bond, J.S.3
  • 18
    • 0033026426 scopus 로고    scopus 로고
    • Expression and regulation of the meprin beta gene in human cancer cells
    • Matters GL, Bond JS (1999) Expression and regulation of the meprin beta gene in human cancer cells. Mol Carcinog 25: 169-178.
    • (1999) Mol Carcinog , vol.25 , pp. 169-178
    • Matters, G.L.1    Bond, J.S.2
  • 19
    • 0030056968 scopus 로고    scopus 로고
    • Cell adhesion: The molecular basis of tissue architecture and morphogenesis
    • Gumbiner BM (1996) Cell adhesion: the molecular basis of tissue architecture and morphogenesis. Cell 84: 345-357.
    • (1996) Cell , vol.84 , pp. 345-357
    • Gumbiner, B.M.1
  • 20
    • 0032510494 scopus 로고    scopus 로고
    • A causal role for E-cadherin in the transition from adenoma to carcinoma
    • Perl AK, Wilgenbus P, Dahl U, Semb H, Christofori G (1998) A causal role for E-cadherin in the transition from adenoma to carcinoma. Nature 392: 190-193.
    • (1998) Nature , vol.392 , pp. 190-193
    • Perl, A.K.1    Wilgenbus, P.2    Dahl, U.3    Semb, H.4    Christofori, G.5
  • 21
    • 0028245813 scopus 로고
    • Cadherin expression in carcinomas: Role in the formation of cell junctions and the prevention of invasiveness
    • Birchmeier W, Behrens J (1994) Cadherin expression in carcinomas: role in the formation of cell junctions and the prevention of invasiveness. Biochim Biophys Acta 1198: 11-26.
    • (1994) Biochim Biophys Acta , vol.1198 , pp. 11-26
    • Birchmeier, W.1    Behrens, J.2
  • 22
    • 33645748171 scopus 로고    scopus 로고
    • Regulation of E-cadherin expression by VHL and hypoxia-inducible factor
    • Esteban MA, Tran MG, Harten SK, Hill P, Castellanos MC, et al. (2006) Regulation of E-cadherin expression by VHL and hypoxia-inducible factor. Cancer Res 66: 3567-3575.
    • (2006) Cancer Res , vol.66 , pp. 3567-3575
    • Esteban, M.A.1    Tran, M.G.2    Harten, S.K.3    Hill, P.4    Castellanos, M.C.5
  • 23
    • 34347360836 scopus 로고    scopus 로고
    • Role of APAF-1, Ecadherin and peritumoral lymphocytic infiltration in tumour budding in colorectal cancer
    • Zlobec I, Lugli A, Baker K, Roth S, Minoo P, et al. (2007) Role of APAF-1, Ecadherin and peritumoral lymphocytic infiltration in tumour budding in colorectal cancer. J Pathol 212: 260-268.
    • (2007) J Pathol , vol.212 , pp. 260-268
    • Zlobec, I.1    Lugli, A.2    Baker, K.3    Roth, S.4    Minoo, P.5
  • 24
    • 0030811614 scopus 로고    scopus 로고
    • Aberrant E-cadherin and alpha-catenin expression in prostate cancer: Correlation with patient survival
    • Richmond PJ, Karayiannakis AJ, Nagafuchi A, Kaisary AV, Pignatelli M (1997) Aberrant E-cadherin and alpha-catenin expression in prostate cancer: correlation with patient survival. Cancer Res 57: 3189-3193.
    • (1997) Cancer Res , vol.57 , pp. 3189-3193
    • Richmond, P.J.1    Karayiannakis, A.J.2    Nagafuchi, A.3    Kaisary, A.V.4    Pignatelli, M.5
  • 25
    • 0026795845 scopus 로고
    • Expression of the cellular adhesion molecule E-cadherin is reduced or absent in high-grade prostate cancer
    • Umbas R, Schalken JA, Aalders TW, Carter BS, Karthaus HF, et al. (1992) Expression of the cellular adhesion molecule E-cadherin is reduced or absent in high-grade prostate cancer. Cancer Res 52: 5104-5109.
    • (1992) Cancer Res , vol.52 , pp. 5104-5109
    • Umbas, R.1    Schalken, J.A.2    Aalders, T.W.3    Carter, B.S.4    Karthaus, H.F.5
  • 26
    • 0033789680 scopus 로고    scopus 로고
    • The transcription factor snail is a repressor of E-cadherin gene expression in epithelial tumour cells
    • Batlle E, Sancho E, Franci C, Dominguez D, Monfar M, et al. (2000) The transcription factor snail is a repressor of E-cadherin gene expression in epithelial tumour cells. Nat Cell Biol 2: 84-89.
    • (2000) Nat Cell Biol , vol.2 , pp. 84-89
    • Batlle, E.1    Sancho, E.2    Franci, C.3    Dominguez, D.4    Monfar, M.5
  • 27
    • 0034964418 scopus 로고    scopus 로고
    • The two-handed E box binding zinc finger protein SIP1 downregulates Ecadherin and induces invasion
    • Comijn J, Berx G, Vermassen P, Verschueren K, van Grunsven L, et al. (2001) The two-handed E box binding zinc finger protein SIP1 downregulates Ecadherin and induces invasion. Mol Cell 7: 1267-1278.
    • (2001) Mol Cell , vol.7 , pp. 1267-1278
    • Comijn, J.1    Berx, G.2    Vermassen, P.3    Verschueren, K.4    van Grunsven, L.5
  • 28
    • 0028849277 scopus 로고
    • E-cadherin expression is silenced by DNA hypermethylation in human breast and prostate carcinomas
    • Graff JR, Herman JG, Lapidus RG, Chopra H, Xu R, et al. (1995) E-cadherin expression is silenced by DNA hypermethylation in human breast and prostate carcinomas. Cancer Res 55: 5195-5199.
    • (1995) Cancer Res , vol.55 , pp. 5195-5199
    • Graff, J.R.1    Herman, J.G.2    Lapidus, R.G.3    Chopra, H.4    Xu, R.5
  • 29
    • 0035147313 scopus 로고    scopus 로고
    • Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1
    • Noe V, Fingleton B, Jacobs K, Crawford HC, Vermeulen S, et al. (2001) Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1. J Cell Sci 114: 111-118.
    • (2001) J Cell Sci , vol.114 , pp. 111-118
    • Noe, V.1    Fingleton, B.2    Jacobs, K.3    Crawford, H.C.4    Vermeulen, S.5
  • 30
    • 21544467772 scopus 로고    scopus 로고
    • ADAM10 mediates E-cadherin shedding and regulates epithelial cell-cell adhesion, migration, and beta-catenin translocation
    • Maretzky T, Reiss K, Ludwig A, Buchholz J, Scholz F, et al. (2005) ADAM10 mediates E-cadherin shedding and regulates epithelial cell-cell adhesion, migration, and beta-catenin translocation. Proc Natl Acad Sci U S A 102: 9182-9187.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 9182-9187
    • Maretzky, T.1    Reiss, K.2    Ludwig, A.3    Buchholz, J.4    Scholz, F.5
  • 31
    • 0001082248 scopus 로고    scopus 로고
    • Secretion of human meprin from intestinal epithelial cells depends on differential expression of the alpha and beta subunits
    • Lottaz D, Hahn D, Muller S, Muller C, Sterchi EE (1999) Secretion of human meprin from intestinal epithelial cells depends on differential expression of the alpha and beta subunits. Eur J Biochem 259: 496-504.
    • (1999) Eur J Biochem , vol.259 , pp. 496-504
    • Lottaz, D.1    Hahn, D.2    Muller, S.3    Muller, C.4    Sterchi, E.E.5
  • 32
    • 0037532953 scopus 로고    scopus 로고
    • Differences in the activation mechanism between the alpha and beta subunits of human meprin
    • Becker C, Kruse MN, Slotty KA, Köhler D, Harris JR, et al. (2003) Differences in the activation mechanism between the alpha and beta subunits of human meprin. Biol Chem 384: 825-831.
    • (2003) Biol Chem , vol.384 , pp. 825-831
    • Becker, C.1    Kruse, M.N.2    Slotty, K.A.3    Köhler, D.4    Harris, J.R.5
  • 33
    • 0024095524 scopus 로고
    • The role of the cell adhesion molecule uvomorulin in the formation and maintenance of the epithelial junctional complex
    • Gumbiner B, Stevenson B, Grimaldi A (1988) The role of the cell adhesion molecule uvomorulin in the formation and maintenance of the epithelial junctional complex. J Cell Biol 107: 1575-1587.
    • (1988) J Cell Biol , vol.107 , pp. 1575-1587
    • Gumbiner, B.1    Stevenson, B.2    Grimaldi, A.3
  • 34
    • 0032526941 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and src family kinases control keratinocyte cell-cell adhesion
    • Calautti E, Cabodi S, Stein PL, Hatzfeld M, Kedersha N, et al. (1998) Tyrosine phosphorylation and src family kinases control keratinocyte cell-cell adhesion. J Cell Biol 141: 1449-1465.
    • (1998) J Cell Biol , vol.141 , pp. 1449-1465
    • Calautti, E.1    Cabodi, S.2    Stein, P.L.3    Hatzfeld, M.4    Kedersha, N.5
  • 35
    • 0030867219 scopus 로고    scopus 로고
    • Cadherins promote skeletal muscle differentiation in three-dimensional cultures
    • Redfield A, Nieman MT, Knudsen KA (1997) Cadherins promote skeletal muscle differentiation in three-dimensional cultures. J Cell Biol 138: 1323-1331.
    • (1997) J Cell Biol , vol.138 , pp. 1323-1331
    • Redfield, A.1    Nieman, M.T.2    Knudsen, K.A.3
  • 36
    • 0038352085 scopus 로고    scopus 로고
    • Biochemical processing of E-cadherin under cellular stress
    • Keller SH, Nigam SK (2003) Biochemical processing of E-cadherin under cellular stress. Biochem Biophys Res Commun 307: 215-223.
    • (2003) Biochem Biophys Res Commun , vol.307 , pp. 215-223
    • Keller, S.H.1    Nigam, S.K.2
  • 37
    • 0034787354 scopus 로고    scopus 로고
    • Matrilysin mediates extracellular cleavage of E-cadherin from prostate cancer cells: A key mechanism in hepatocyte growth factor/scatter factor-induced cell-cell dissociation and in vitro invasion
    • Davies G, Jiang WG, Mason MD (2001) Matrilysin mediates extracellular cleavage of E-cadherin from prostate cancer cells: a key mechanism in hepatocyte growth factor/scatter factor-induced cell-cell dissociation and in vitro invasion. Clin Cancer Res 7: 3289-3297.
    • (2001) Clin Cancer Res , vol.7 , pp. 3289-3297
    • Davies, G.1    Jiang, W.G.2    Mason, M.D.3
  • 38
    • 33845380864 scopus 로고    scopus 로고
    • Re-solving the cadherin-catenin-actin conundrum
    • Weis WI, Nelson WJ (2006) Re-solving the cadherin-catenin-actin conundrum. J Biol Chem 281: 35593-35597.
    • (2006) J Biol Chem , vol.281 , pp. 35593-35597
    • Weis, W.I.1    Nelson, W.J.2
  • 39
    • 1842390685 scopus 로고
    • Cell binding function of E-cadherin is regulated by the cytoplasmic domain
    • Nagafuchi A, Takeichi M (1988) Cell binding function of E-cadherin is regulated by the cytoplasmic domain. Embo J 7: 3679-3684.
    • (1988) Embo J , vol.7 , pp. 3679-3684
    • Nagafuchi, A.1    Takeichi, M.2
  • 40
    • 0024451982 scopus 로고
    • The cytoplasmic domain of the cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species
    • Ozawa M, Baribault H, Kemler R (1989) The cytoplasmic domain of the cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species. Embo J 8: 1711-1717.
    • (1989) Embo J , vol.8 , pp. 1711-1717
    • Ozawa, M.1    Baribault, H.2    Kemler, R.3
  • 41
    • 20444376552 scopus 로고    scopus 로고
    • Meprin metalloprotease expression and regulation in kidney, intestine, urinary tract infections and cancer
    • Bond JS, Matters GL, Banerjee S, Dusheck RE (2005) Meprin metalloprotease expression and regulation in kidney, intestine, urinary tract infections and cancer. FEBS Lett 579: 3317-3322.
    • (2005) FEBS Lett , vol.579 , pp. 3317-3322
    • Bond, J.S.1    Matters, G.L.2    Banerjee, S.3    Dusheck, R.E.4
  • 42
    • 0037428430 scopus 로고    scopus 로고
    • The role of calpain in the proteolytic cleavage of E-cadherin in prostate and mammary epithelial cells
    • Rios-Doria J, Day KC, Kuefer R, Rashid MG, Chinnaiyan AM, et al. (2003) The role of calpain in the proteolytic cleavage of E-cadherin in prostate and mammary epithelial cells. J Biol Chem 278: 1372-1379.
    • (2003) J Biol Chem , vol.278 , pp. 1372-1379
    • Rios-Doria, J.1    Day, K.C.2    Kuefer, R.3    Rashid, M.G.4    Chinnaiyan, A.M.5
  • 43
    • 0035895927 scopus 로고    scopus 로고
    • Cleavage and shedding of E-cadherin after induction of apoptosis
    • Steinhusen U, Weiske J, Badock V, Tauber R, Bommert K, et al. (2001) Cleavage and shedding of E-cadherin after induction of apoptosis. J Biol Chem 276: 4972-4980.
    • (2001) J Biol Chem , vol.276 , pp. 4972-4980
    • Steinhusen, U.1    Weiske, J.2    Badock, V.3    Tauber, R.4    Bommert, K.5
  • 44
    • 18344380083 scopus 로고    scopus 로고
    • A presenilin-1/gamma-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions
    • Marambaud P, Shioi J, Serban G, Georgakopoulos A, Sarner S, et al. (2002) A presenilin-1/gamma-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions. Embo J 21: 1948-1956.
    • (2002) Embo J , vol.21 , pp. 1948-1956
    • Marambaud, P.1    Shioi, J.2    Serban, G.3    Georgakopoulos, A.4    Sarner, S.5
  • 45
    • 17144368746 scopus 로고    scopus 로고
    • Intersubunit and domain interactions of the meprin B metalloproteinase. Disulfide bonds and protein-protein interactions in the MAM and TRAF domains
    • Ishmael FT, Shier VK, Ishmael SS, Bond JS (2005) Intersubunit and domain interactions of the meprin B metalloproteinase. Disulfide bonds and protein-protein interactions in the MAM and TRAF domains. J Biol Chem 280: 13895-13901.
    • (2005) J Biol Chem , vol.280 , pp. 13895-13901
    • Ishmael, F.T.1    Shier, V.K.2    Ishmael, S.S.3    Bond, J.S.4
  • 46
    • 33747736649 scopus 로고    scopus 로고
    • A basolateral sorting signal directs ADAM10 to adherens junctions and is required for its function in cell migration
    • Wild-Bode C, Fellerer K, Kugler J, Haass C, Capell A (2006) A basolateral sorting signal directs ADAM10 to adherens junctions and is required for its function in cell migration. J Biol Chem 281: 23824-23829.
    • (2006) J Biol Chem , vol.281 , pp. 23824-23829
    • Wild-Bode, C.1    Fellerer, K.2    Kugler, J.3    Haass, C.4    Capell, A.5
  • 47
    • 25444466556 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase signaling to Akt promotes keratinocyte differentiation versus death
    • Calautti E, Li J, Saoncella S, Brissette JL, Goetinck PF (2005) Phosphoinositide 3-kinase signaling to Akt promotes keratinocyte differentiation versus death. J Biol Chem 280: 32856-32865.
    • (2005) J Biol Chem , vol.280 , pp. 32856-32865
    • Calautti, E.1    Li, J.2    Saoncella, S.3    Brissette, J.L.4    Goetinck, P.F.5
  • 48
    • 34250361104 scopus 로고    scopus 로고
    • E-cadherin homophilic ligation inhibits cell growth and epidermal growth factor receptor signaling independently of other cell interactions
    • Perrais M, Chen X, Perez-Moreno M, Gumbiner BM (2007) E-cadherin homophilic ligation inhibits cell growth and epidermal growth factor receptor signaling independently of other cell interactions. Mol Biol Cell 18: 2013-2025.
    • (2007) Mol Biol Cell , vol.18 , pp. 2013-2025
    • Perrais, M.1    Chen, X.2    Perez-Moreno, M.3    Gumbiner, B.M.4
  • 49
    • 34247869640 scopus 로고    scopus 로고
    • The recruitment of phosphatidylinositol 3-kinase to the E-cadherin-catenin complex at the plasma membrane is required for calcium-induced phospholipase C-gamma1 activation and human keratinocyte differentiation
    • Xie Z, Bikle DD (2007) The recruitment of phosphatidylinositol 3-kinase to the E-cadherin-catenin complex at the plasma membrane is required for calcium-induced phospholipase C-gamma1 activation and human keratinocyte differentiation. J Biol Chem 282: 8695-8703.
    • (2007) J Biol Chem , vol.282 , pp. 8695-8703
    • Xie, Z.1    Bikle, D.D.2
  • 50
    • 33644811128 scopus 로고    scopus 로고
    • E-cadherin and its downstream catenins are proteolytically cleaved in human HaCaT keratinocytes exposed to UVB
    • Hung CF, Chiang HS, Lo HM, Jian JS, Wu WB (2006) E-cadherin and its downstream catenins are proteolytically cleaved in human HaCaT keratinocytes exposed to UVB. Exp Dermatol 15: 315-321.
    • (2006) Exp Dermatol , vol.15 , pp. 315-321
    • Hung, C.F.1    Chiang, H.S.2    Lo, H.M.3    Jian, J.S.4    Wu, W.B.5
  • 51
    • 5644271513 scopus 로고    scopus 로고
    • Cleavage of beta-catenin by calpain in prostate and mammary tumor cells
    • Rios-Doria J, Kuefer R, Ethier SP, Day ML (2004) Cleavage of beta-catenin by calpain in prostate and mammary tumor cells. Cancer Res 64: 7237-7240.
    • (2004) Cancer Res , vol.64 , pp. 7237-7240
    • Rios-Doria, J.1    Kuefer, R.2    Ethier, S.P.3    Day, M.L.4
  • 52
    • 0025374899 scopus 로고
    • Uvomorulin-catenin complex formation is regulated by a specific domain in the cytoplasmic region of the cell adhesion molecule
    • Ozawa M, Ringwald M, Kemler R (1990) Uvomorulin-catenin complex formation is regulated by a specific domain in the cytoplasmic region of the cell adhesion molecule. Proc Natl Acad Sci U S A 87: 4246-4250.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 4246-4250
    • Ozawa, M.1    Ringwald, M.2    Kemler, R.3
  • 53
    • 0026551855 scopus 로고
    • Remodeling the cell surface distribution of membrane proteins during the development of epithelial cell polarity
    • Wollner DA, Krzeminski KA, Nelson WJ (1992) Remodeling the cell surface distribution of membrane proteins during the development of epithelial cell polarity. J Cell Biol 116: 889-899.
    • (1992) J Cell Biol , vol.116 , pp. 889-899
    • Wollner, D.A.1    Krzeminski, K.A.2    Nelson, W.J.3
  • 54
    • 23144442645 scopus 로고    scopus 로고
    • Regulation of cadherin-mediated adhesion in morphogenesis
    • Gumbiner BM (2005) Regulation of cadherin-mediated adhesion in morphogenesis. Nat Rev Mol Cell Biol 6: 622-634.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 622-634
    • Gumbiner, B.M.1
  • 55
    • 0025740054 scopus 로고
    • Expression of immunoreactive E-cadherin adhesion molecules in human cancers
    • Shiozaki H, Tahara H, Oka H, Miyata M, Kobayashi K, et al. (1991) Expression of immunoreactive E-cadherin adhesion molecules in human cancers. Am J Pathol 139: 17-23.
    • (1991) Am J Pathol , vol.139 , pp. 17-23
    • Shiozaki, H.1    Tahara, H.2    Oka, H.3    Miyata, M.4    Kobayashi, K.5
  • 56
    • 0030032714 scopus 로고    scopus 로고
    • A novel meprin beta' mRNA in mouse embryonal and human colon carcinoma cells
    • Dietrich JM, Jiang W, Bond JS (1996) A novel meprin beta' mRNA in mouse embryonal and human colon carcinoma cells. J Biol Chem 271: 2271-2278.
    • (1996) J Biol Chem , vol.271 , pp. 2271-2278
    • Dietrich, J.M.1    Jiang, W.2    Bond, J.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.