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Volumn 7, Issue 6, 2009, Pages 809-820

Epidermal growth factor receptor-mediated membrane type 1 matrix metalloproteinase endocytosis regulates the transition between invasive versus expansive growth of ovarian carcinoma cells in three-dimensional collagen

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; MATRIX METALLOPROTEINASE 14; TYROSINE;

EID: 66949151925     PISSN: 15417786     EISSN: None     Source Type: Journal    
DOI: 10.1158/1541-7786.MCR-08-0571     Document Type: Article
Times cited : (33)

References (107)
  • 4
    • 41949100690 scopus 로고    scopus 로고
    • Clinical implications of the ErbB/epidermal growth factor (EGF) receptor family and its ligands in ovarian cancer
    • Lafky JM, Wilken JA, Baron AT, Maihle NJ. Clinical implications of the ErbB/epidermal growth factor (EGF) receptor family and its ligands in ovarian cancer. Biochim Biophys Acta 2008;1785:232-265
    • (2008) Biochim Biophys Acta , vol.1785 , pp. 232-265
    • Lafky, J.M.1    Wilken, J.A.2    Baron, A.T.3    Maihle, N.J.4
  • 6
    • 0023675030 scopus 로고    scopus 로고
    • Augmented mitogenic responsiveness to Epidermal Growth Factor in murine fibroblasts that overexpress pp6Ocsrc
    • Luttrell DK, Luttrell LM, Parsons SJ. Augmented mitogenic responsiveness to Epidermal Growth Factor in murine fibroblasts that overexpress pp6Ocsrc. Mol Cell Biol 1998;8:497-501.
    • (1998) Mol Cell Biol , vol.8 , pp. 497-501
    • Luttrell, D.K.1    Luttrell, L.M.2    Parsons, S.J.3
  • 7
    • 0029121267 scopus 로고
    • Potentiation of epidermal growth factor receptor-mediated oncogenesis by c-Src: Implications for the etiology of multiple human cancers
    • Maa MC, Leu TH, McCarley DJ, Schatzman RC, Parsons SJ. Potentiation of epidermal growth factor receptor-mediated oncogenesis by c-Src: implications for the etiology of multiple human cancers. Proc Natl Acad Sci U S A 1995;92:6981-6985
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 6981-6985
    • Maa, M.C.1    Leu, T.H.2    McCarley, D.J.3    Schatzman, R.C.4    Parsons, S.J.5
  • 8
    • 0032230322 scopus 로고    scopus 로고
    • Shc phosphotyrosine-binding domain dominantly interacts with epidermal growth factor receptors and mediates ras activation in intact cells
    • Sakaguchi K, Okabayashi Y, Kido Y, et al. Shc phosphotyrosine-binding domain dominantly interacts with epidermal growth factor receptors and mediates Ras activation in intact cells. Mol Endocrinol 1998;12:536-543 (Pubitemid 30659084)
    • (1998) Molecular Endocrinology , vol.12 , Issue.4 , pp. 536-543
    • Sakaguchi, K.1    Okabayashi, Y.2    Kido, Y.3    Kimura, S.4    Matsumura, Y.5    Inushima, K.6    Kasuga, M.7
  • 10
    • 0029960791 scopus 로고    scopus 로고
    • STAT activation by epidermal growth factor (EGF) and amphiregulin. Requirement for the EFG receptor kinase but not for tyrosine phosphorylation sites or Jak1
    • DOI 10.1074/jbc.271.16.9185
    • David M, Wong L, Flavell R, et al. STAT activation by epidermal growth factor (EGF) and amphiregulin. Requirement for the EGF receptor kinase but not for tyrosine phosphorylation sites or JAK1. J Biol Chem 1996;271:9185-9188 (Pubitemid 26137315)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.16 , pp. 9185-9188
    • David, M.1    Wong, L.2    Flavell, R.3    Thompson, S.A.4    Wells, A.5    Larner, A.C.6    Johnson, G.R.7
  • 11
    • 0030447148 scopus 로고    scopus 로고
    • In vitro activation of Stat3 by epidermal growth factor receptor kinase
    • Park OK, Schaefer TS, Nathans D. In vitro activation of Stat3 by epidermal growth factor receptor kinase. Proc Natl Acad Sci U S A 1996;93:13704-13708
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 13704-13708
    • Park, O.K.1    Schaefer, T.S.2    Nathans, D.3
  • 12
    • 0032509206 scopus 로고    scopus 로고
    • PLD2 complexes with the EGF receptor and undergoes tyrosine phosphorylation at a single site upon agonist stimulation
    • DOI 10.1074/jbc.273.50.33722
    • Slaaby R, Jensen T, Hansen HS, Frohman MA, Seedorf K. PLD2 complexes with the EGF receptor and undergoes tyrosine phosphorylation at a single site upon agonist stimulation. J Biol Chem 1998;273:33722-33727 (Pubitemid 29005762)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.50 , pp. 33722-33727
    • Slaaby, R.1    Jensenll, T.2    Hansenh, H.S.3    Frohmanll, M.A.4    Seedorft, K.5
  • 15
    • 0025790916 scopus 로고
    • Genes for epidermal growth factor receptor, transforming growth factor α, and epidermal growth factor and their expression in human gliomas in vivo
    • Ekstrand AJ, James CD, Cavanee WK, Seliger B, Petterson RF, Collins VP. Genes for epidermal growth factor receptor, transforming growth factor α, and epidermal growth factor and their expression in human gliomas in vivo. Cancer Res 1991;51:2164-2172
    • (1991) Cancer Res , vol.51 , pp. 2164-2172
    • Ekstrand, A.J.1    James, C.D.2    Cavanee, W.K.3    Seliger, B.4    Petterson, R.F.5    Collins, V.P.6
  • 16
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signaling
    • Blume-Jensen P, Hunter T. Oncogenic kinase signaling. Nature 2001;411:355-365
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 17
    • 0028330743 scopus 로고    scopus 로고
    • The epidermal growth factor receptor as a prognostic marker: Results of 370 patients and review of 3009 patients
    • Fox SB, Smith K, Hollyer J, Greenall M, Hastrich D, Harris AL. The epidermal growth factor receptor as a prognostic marker: results of 370 patients and review of 3009 patients. Breast Cancer Res Treat 1999;29:41-49
    • (1999) Breast Cancer Res Treat , vol.29 , pp. 41-49
    • Fox, S.B.1    Smith, K.2    Hollyer, J.3    Greenall, M.4    Hastrich, D.5    Harris, A.L.6
  • 19
    • 0028955388 scopus 로고    scopus 로고
    • Epidermal growth factor-related peptides and their receptors in human malignancies
    • Salomon DS, Brandt R, Ciardiello F, Normanno N. Epidermal growth factor-related peptides and their receptors in human malignancies. Crit Rev Oncol Hematol 2005;3:183-232.
    • (2005) Crit Rev Oncol Hematol , vol.3 , pp. 183-232
    • Salomon, D.S.1    Brandt, R.2    Ciardiello, F.3    Normanno, N.4
  • 20
  • 21
    • 0026023499 scopus 로고
    • Epidermal growth factor receptor expression in normal ovarian epithelium and ovarian cancer. I. Correlation of receptor expression with prognostic factors in patients with ovarian cancer
    • Berchuck A, Rodriguez GC, Kamel A, et al. Epidermal growth factor receptor expression in normal ovarian epithelium and ovarian cancer. I. Correlation of receptor expression with prognostic factors in patients with ovarian cancer. Am J Obstet Gynecol 1991;2:669-674
    • (1991) Am J Obstet Gynecol , vol.2 , pp. 669-674
    • Berchuck, A.1    Rodriguez, G.C.2    Kamel, A.3
  • 22
    • 0026484997 scopus 로고
    • Immunohistochemical localization of c-erbB-2 protein and epidermal growth factor receptor in normal surface epithelium, surface inclusion cysts, and common epithelial tumours of the ovary
    • Wang DP, Konishi I, Koshiyama M, et al. Immunohistochemical localization of c-erbB-2 protein and epidermal growth factor receptor in normal surface epithelium, surface inclusion cysts, and common epithelial tumours of the ovary. Virchows Arch A Pathol Anat Histopathol 1992;421:393-400.
    • (1992) Virchows Arch A Pathol Anat Histopathol , vol.421 , pp. 393-400
    • Wang, D.P.1    Konishi, I.2    Koshiyama, M.3
  • 23
    • 0026508235 scopus 로고
    • Occurrence of epidermal growth factor receptors in benign and malignant ovarian tumors and normal ovarian tissues: An immunohistochemical study
    • Henzen-Logmans SC, van der Burg ME, Foekens JA, et al. Occurrence of epidermal growth factor receptors in benign and malignant ovarian tumors and normal ovarian tissues: an immunohistochemical study. J Cancer Res Clin Oncol 1994;118:303-307
    • (1994) J Cancer Res Clin Oncol , vol.118 , pp. 303-307
    • Henzen-Logmans, S.C.1    Van Der Burg, M.E.2    Foekens, J.A.3
  • 25
    • 4143076078 scopus 로고    scopus 로고
    • Targeting the epidermal growth factor receptor
    • DOI 10.1038/sj.bjc.6601921
    • El-Rayes BF, LoRusso PM. Targeting the epidermal growth factor receptor. Br J Cancer 2004;91:418-424 (Pubitemid 39093557)
    • (2004) British Journal of Cancer , vol.91 , Issue.3 , pp. 418-424
    • El-Rayes, B.F.1    Lorusso, P.M.2
  • 26
    • 2442701289 scopus 로고    scopus 로고
    • The ErbB/HER receptor protein-tyrosine kinases and cancer
    • Roskoski R, Jr. The ErbB/HER receptor protein-tyrosine kinases and cancer. Biochem Biophys Res Commun 2004;319:1-11.
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 1-11
    • Roskoski Jr., R.1
  • 27
    • 49649098028 scopus 로고    scopus 로고
    • Matrix metalloproteinase 9 is a mediator of epidermal growth factor-dependent e-cadherin loss in ovarian carcinoma cells
    • Cowden Dahl KD, Symowicz J, Ning Y, et al. Matrix metalloproteinase 9 is a mediator of epidermal growth factor-dependent e-cadherin loss in ovarian carcinoma cells. Cancer Res 2008;68:4606-4613
    • (2008) Cancer Res , vol.68 , pp. 4606-4613
    • Cowden Dahl, K.D.1    Symowicz, J.2    Ning, Y.3
  • 29
    • 5144220224 scopus 로고    scopus 로고
    • Prognostic factors in ovarian cancer: Current evidence and future prospects. The ECCO 12 Educational Book
    • Crijns APG, Boezen HM, Schouten JP, et al. Prognostic factors in ovarian cancer: current evidence and future prospects. The ECCO 12 Educational Book. Eur J Cancer 2003;1:127-145
    • (2003) Eur J Cancer , vol.1 , pp. 127-145
    • Crijns, A.P.G.1    Boezen, H.M.2    Schouten, J.P.3
  • 30
    • 0033761255 scopus 로고    scopus 로고
    • Anti-sense suppression of epidermal growth factor receptor expression alters cellular proliferation, cell-adhesion and tumorigenicity in ovarian cancer cells
    • DOI 10.1002/1097-0215(20001115)88:4<566::AID-IJC8>3.0.CO;2-D
    • Alper O, De Santis ML, Stromberg K, Hacker NF, Cho-Chung YS, Salomon DS. Anti-sense suppression of epidermal growth factor receptor expression alters cellular proliferation, cell-adhesion and tumorigenicity in ovarian cancer cells. Int J Cancer 2000;88:566-574 (Pubitemid 30805070)
    • (2000) International Journal of Cancer , vol.88 , Issue.4 , pp. 566-574
    • Alper, O.1    De Santis, M.L.2    Stromberg, K.3    Hacker, N.F.4    Cho-Chung, Y.S.5    Salomon, D.S.6
  • 31
    • 0031856726 scopus 로고    scopus 로고
    • Epidermal growth factor receptor (EGFR) antisense transfection reduces the expression of EGFR and suppresses the malignant phenotype of a human ovarian cancer cell line
    • Brader KR, Wolf JK, Chakrabarty S, Price JE. Epidermal growth factor receptor (EGFR) antisense transfection reduces the expression of EGFR and suppresses the malignant phenotype of a human ovarian cancer cell line. Oncol Rep 1998;5:1269-1274 (Pubitemid 28372601)
    • (1998) Oncology Reports , vol.5 , Issue.5 , pp. 1269-1274
    • Brader, K.R.1    Wolf, J.K.2    Chakrabarty, S.3    Price, J.E.4
  • 34
    • 33645676359 scopus 로고    scopus 로고
    • The clinical relevance of stromal matrix metalloproteinase expression in ovarian cancer
    • Kamat AA, Fletcher M, Gruman LM, et al. The clinical relevance of stromal matrix metalloproteinase expression in ovarian cancer. Clin Cancer Res 2006;12:1707-1714
    • (2006) Clin Cancer Res , vol.12 , pp. 1707-1714
    • Kamat, A.A.1    Fletcher, M.2    Gruman, L.M.3
  • 35
    • 67649616762 scopus 로고    scopus 로고
    • Development of an organotypic peritoneal three-dimensional culture to study peritoneal attachment of ovarian cancer cells
    • Kenny HA, Krausz T, Yamada SD, Lengyel E. Development of an organotypic peritoneal three-dimensional culture to study peritoneal attachment of ovarian cancer cells. Int J Cancer 2001;121:1463-1472
    • (2001) Int J Cancer , vol.121 , pp. 1463-1472
    • Kenny, H.A.1    Krausz, T.2    Yamada, S.D.3    Lengyel, E.4
  • 36
    • 41849105806 scopus 로고    scopus 로고
    • The initial steps of ovarian cancer cell metastasis are mediated by MMP-2 cleavage of vitronectin and fibronectin
    • Kenny HA, Kaur S, Coussens LM, Lengyel E. The initial steps of ovarian cancer cell metastasis are mediated by MMP-2 cleavage of vitronectin and fibronectin. J Clin Invest 2008;118:1367-1379
    • (2008) J Clin Invest , vol.118 , pp. 1367-1379
    • Kenny, H.A.1    Kaur, S.2    Coussens, L.M.3    Lengyel, E.4
  • 37
    • 58149483748 scopus 로고    scopus 로고
    • Expression of membrane type 1 matrix metalloproteinase (MMP-14) in epithelial ovarian cancer: High level expression in clear cell carcinoma
    • Adley BP, Gleason KJ, Yang X, Stack MS. Expression of membrane type 1 matrix metalloproteinase (MMP-14) in epithelial ovarian cancer: high level expression in clear cell carcinoma. Gynecol Oncol 2009;112:319-324
    • (2009) Gynecol Oncol , vol.112 , pp. 319-324
    • Adley, B.P.1    Gleason, K.J.2    Yang, X.3    Stack, M.S.4
  • 38
    • 0036364519 scopus 로고    scopus 로고
    • Ovarian cancer-associated proteinases
    • Ghosh S, Wu Y, Stack MS. Ovarian cancer-associated proteinases. Cancer Treat Res 2002;107:331-351
    • (2002) Cancer Treat Res , vol.107 , pp. 331-351
    • Ghosh, S.1    Wu, Y.2    Stack, M.S.3
  • 40
    • 0032578691 scopus 로고    scopus 로고
    • Proteinase requirements of epidermal growth factor-induced ovarian cancer cell invasion
    • DOI 10.1002/(SICI)1097-0215(19981029)78:3<331::AID-IJC13>3.0.CO;2-9
    • Ellerbroek SM, Hudson LG, Stack MS. Proteinase requirements of epidermal growth factor-induced ovarian cancer cell invasion. Int J Cancer 1998;78:331-337 (Pubitemid 28445371)
    • (1998) International Journal of Cancer , vol.78 , Issue.3 , pp. 331-337
    • Ellerbroek, S.M.1    Hudson, L.G.2    Stack, M.S.3
  • 41
    • 0035816605 scopus 로고    scopus 로고
    • Functional Interplay between Type I Collagen and Cell Surface Matrix Metalloproteinase Activity
    • DOI 10.1074/jbc.M005631200
    • Ellerbroek SM, Wu YI, Overall CM, Stack MS. Functional interplay between type I collagen and cell surface matrix metalloproteinase activity. J Biol Chem 2001;276:24833-24842 (Pubitemid 33659083)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.27 , pp. 24833-24842
    • Ellerbroek, S.M.1    Wu, Y.I.2    Overall, C.M.3    Sharon Stack, M.4
  • 42
    • 34250180482 scopus 로고    scopus 로고
    • PEA3 is necessary for optimal epidermal growth factor receptor-stimulated matrix metalloproteinase expression and invasion of ovarian tumor cells
    • DOI 10.1158/1541-7786.MCR-07-0019
    • Cowden Dahl KD, Zeineldin R, Hudson LG. PEA3 is necessary for optimal epidermal growth factor receptor-stimulated matrix metalloproteinase expression and invasion of ovarian tumor cells. Mol Cancer Res 2007;5:413-421 (Pubitemid 46903950)
    • (2007) Molecular Cancer Research , vol.5 , Issue.5 , pp. 413-421
    • Dahl, K.D.C.1    Zeineldin, R.2    Hudson, L.G.3
  • 43
    • 0031909775 scopus 로고    scopus 로고
    • MT1-MMP and MMP-2 mRNA expression in human ovarian tumors: Possible implications for the role of desmoplastic fibroblasts
    • DOI 10.1016/S0046-8177(98)90226-X
    • Afzal S, Lalani EN, Poulsom R, et al. MT1-MMP and MMP-2 mRNA expression in human ovarian tumors: possible implications for the role of desmoplastic fibroblasts. Hum Pathol 1998;29:155-165 (Pubitemid 28099511)
    • (1998) Human Pathology , vol.29 , Issue.2 , pp. 155-165
    • Afzal, S.1    Lalani, E.-N.2    Poulsom, R.3    Stubbs, A.4    Rowlinson, G.5    Sato, H.6    Seiki, M.7    Stamp, G.W.H.8
  • 46
    • 0036109679 scopus 로고    scopus 로고
    • MT-MMPs play pivotal roles in cancer dissemination
    • Yana I, Seiki M. MT-MMPs play pivotal roles in cancer dissemination. Clin Exp Metastasis 2003;19:209-215
    • (2003) Clin Exp Metastasis , vol.19 , pp. 209-215
    • Yana, I.1    Seiki, M.2
  • 47
    • 23044466812 scopus 로고    scopus 로고
    • Expression of membrane type 1 matrix metalloproteinase is associated with cervical carcinoma progression and invasion
    • DOI 10.1158/0008-5472.CAN-05-0231
    • Zhai Y, Hotary K, Nan B, et al. Expression of membrane type 1 matrix metalloproteinase is associated with cervical carcinoma progression and invasion. Cancer Res 2005;65:6543-6550 (Pubitemid 41060689)
    • (2005) Cancer Research , vol.65 , Issue.15 , pp. 6543-6550
    • Zhai, Y.1    Hotary, K.B.2    Nan, B.3    Bosch, F.X.4    Munoz, N.5    Weiss, S.J.6    Cho, K.R.7
  • 48
    • 28444454893 scopus 로고    scopus 로고
    • MT1-MMP: A potent modifier of pericellular microenvironment
    • DOI 10.1002/jcp.20431
    • Itoh Y, Seiki M. MT1-MMP: a potent modifier of pericellular microenvironment. J Cell Physiol 2006;206:1-8. (Pubitemid 41740711)
    • (2006) Journal of Cellular Physiology , vol.206 , Issue.1 , pp. 1-8
    • Itoh, Y.1    Seiki, M.2
  • 50
    • 0035955469 scopus 로고    scopus 로고
    • Activation of the extracellular signal-regulated protein kinase (ERK) cascade by membrane-type-1m atrix metalloproteinase (MT1-MMP)
    • Gingras D, Bousquet-Gagnon N, Langlois S, Lachambre M, Annabi B, Beliveau R. Activation of the extracellular signal-regulated protein kinase (ERK) cascade by membrane-type-1m atrix metalloproteinase (MT1-MMP). FEBS Lett 2001;507:231-236
    • (2001) FEBS Lett , vol.507 , pp. 231-236
    • Gingras, D.1    Bousquet-Gagnon, N.2    Langlois, S.3    Lachambre, M.4    Annabi, B.5    Beliveau, R.6
  • 51
    • 33947518899 scopus 로고    scopus 로고
    • Microenvironmental regulation of membrane type 1 matrix metalloproteinase activity in ovarian carcinoma cells via collagen-induced EGR1 expression
    • DOI 10.1074/jbc.M608428200
    • Barbolina MV, Adley BP, Ariztia EV, Liu Y, Stack MS. Microenvironmental regulation of membrane type 1ma trix metalloproteinase activity in ovarian carcinoma cells via collagen-induced EGR1expression. J Biol Chem 2007;282:4924-4931 (Pubitemid 47100955)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.7 , pp. 4924-4931
    • Barbolina, M.V.1    Adley, B.P.2    Ariztia, E.V.3    Liu, Y.4    Stack, M.S.5
  • 52
    • 0034641107 scopus 로고    scopus 로고
    • Regulation of cell invasion and morphogenesis in a three-dimensional type I collagen matrix by membrane-type matrix metalloproteinases 1, 2, and 3
    • DOI 10.1083/jcb.149.6.1309
    • Hotary K, Allen E, Punturieri A, Yana I, Weiss S. Regulation of cell invasion and morphogenesis in a three-dimensional type I collagen matrix by membrane-type matrix metalloproteinases 1, 2, and 3. J Cell Biol 2000;149:1309-1323 (Pubitemid 30399683)
    • (2000) Journal of Cell Biology , vol.149 , Issue.6 , pp. 1309-1323
    • Hotary, K.1    Allen, E.2    Punturieri, A.3    Yana, I.4    Weiss, S.J.5
  • 53
    • 0038784546 scopus 로고    scopus 로고
    • Membrane type I matrix metalloproteinase usurps tumor growth control imposed by the three-dimensional extracellular matrix
    • DOI 10.1016/S0092-8674(03)00513-0
    • Hotary K, Allen E, Brooks P, Datta N, Long M, Weiss SJ. Membrane type 1 matrix metalloproteinase usurps tumor growth control imposed by the three-dimensional extracellular matrix. Cell 2003;114:33-45. (Pubitemid 36859839)
    • (2003) Cell , vol.114 , Issue.1 , pp. 33-45
    • Hotary, K.B.1    Allen, E.D.2    Brooks, P.C.3    Datta, N.S.4    Long, M.W.5    Weiss, S.J.6
  • 54
    • 0033019758 scopus 로고    scopus 로고
    • Enhancement of membrane-type 1-matrix metalloproteinase (MT1-MMP) production and sequential activation of progelatinase a on human squamous carcinoma cells co-cultured with human dermal fibroblasts
    • DOI 10.1038/sj.bjc.6690477
    • Sato T, Iwai M, Sakai T, Sato H, et al. Enhancement of membrane-type 1-matrix metalloproteinase (MT1-MMP) production and sequential activation of progelatinase A on human squamous carcinoma cells co-cultured with human dermal fibroblasts. Br J Cancer 1999;80:1137-1143 (Pubitemid 29264071)
    • (1999) British Journal of Cancer , vol.80 , Issue.8 , pp. 1137-1143
    • Sato, T.1    Iwai, M.2    Sakai, T.3    Sato, H.4    Seiki, M.5    Mori, Y.6    Ito, A.7
  • 55
    • 4344594952 scopus 로고    scopus 로고
    • Induction of membrane-type-1 matrix metalloproteinase by epidermal growth factor-mediated signaling in gliomas
    • DOI 10.1215/S1152851703000486
    • Van Meter TE, Broaddus WC, Rooprai HK, Pilkington GJ, Fillmore HL. Induction of membrane-type-1ma trix metalloproteinase by epidermal growth factor-mediated signaling in gliomas. Neuro oncol 2004;6:188-199 (Pubitemid 39136502)
    • (2004) Neuro-Oncology , vol.6 , Issue.3 , pp. 188-199
    • Van Meter, T.E.1    Broaddus, W.C.2    Rooprai, H.K.3    Pilkington, G.J.4    Fillmore, H.L.5
  • 56
    • 0037084399 scopus 로고    scopus 로고
    • Signaling through the EGF receptor controls lung morphogenesis in part by regulating MT1-MMP-mediated activation of gelatinase A/MMP2
    • Kheradmand F, Rishi K, Werb Z. Signaling through the EGF receptor controls lung morphogenesis in part by regulating MT1-MMP-mediated activation of gelatinase A/MMP2. J Cell Sci 2002;115:839-848 (Pubitemid 34196343)
    • (2002) Journal of Cell Science , vol.115 , Issue.4 , pp. 839-848
    • Kheradmand, F.1    Rishi, K.2    Werb, Z.3
  • 59
    • 0033555946 scopus 로고    scopus 로고
    • 2-adrenergic receptor internalization and mitogen-activated protein kinase signaling
    • Ahn S, Maudsley S, Luttrell LM, Lefkowitz RJ, Daaka Y. Src-mediated tyrosine phosphorylation of dynamin is required for β2-adrenergic receptor internalization and mitogen-activated protein kinase signaling. J Biol Chem 1999;274:1185-1188 (Pubitemid 129507696)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.3 , pp. 1185-1188
    • Ahn, S.1    Maudsley, S.2    Luttrell, L.M.3    Lefkowitz, R.J.4    Daaka, Y.5
  • 60
    • 0035252979 scopus 로고    scopus 로고
    • Localization of membrane-type 1 matrix metalloproteinase in caveolae membrane domains
    • DOI 10.1042/0264-6021:3530547
    • Annabi B, Lachambre MP, Bousquet-Gagnon N, Page M, Gingras D, Beliveau R. Localization of membrane-type 1ma trix metalloproteinase in caveolae membrane domains. Biochem J 2001;353:547-553 (Pubitemid 32158323)
    • (2001) Biochemical Journal , vol.353 , Issue.3 , pp. 547-553
    • Annabi, B.1    Lachambre, M.2    Bousquet-Gagnon, N.-P.3    Page, M.4    Gingras, D.5    Beliveau, R.6
  • 62
    • 0142011033 scopus 로고    scopus 로고
    • Membrane type I-matrix metalloproteinase (MT1-MMP) is internalised by two different pathways and is recycled to the cell surface
    • DOI 10.1242/jcs.00710
    • Remacle A, Murphy G, Roghi C. Membrane type 1-matrix metalloproteinase (MT1-MMP) is internalized by two different pathways and is recycled to the cell surface. J Cell Sci 2003;116:3905-3916 (Pubitemid 37279306)
    • (2003) Journal of Cell Science , vol.116 , Issue.19 , pp. 3905-3916
    • Remacle, A.1    Murphy, G.2    Roghi, C.3
  • 63
    • 47749090496 scopus 로고    scopus 로고
    • Visualization of polarized membrane type 1 matrix metalloproteinase activity in live cells by fluorescence resonance energy transfer imaging
    • Ouyang M, Lu S, Li XY, et al. Visualization of polarized membrane type 1 matrix metalloproteinase activity in live cells by fluorescence resonance energy transfer imaging. J Biol Chem 2008;283:17740-17748
    • (2008) J Biol Chem , vol.283 , pp. 17740-17748
    • Ouyang, M.1    Lu, S.2    Li, X.Y.3
  • 64
    • 0028820041 scopus 로고
    • A detergent-free method for purifying caveolae membrane from tissue culture cells
    • Smart EJ, Ying YS, Mineo C, Anderson RG. A detergent-free method for purifying caveolae membrane from tissue culture cells. Proc Natl Acad Sci U S A 1995;92:10104-10108
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 10104-10108
    • Smart, E.J.1    Ying, Y.S.2    Mineo, C.3    Anderson, R.G.4
  • 65
    • 15844431258 scopus 로고    scopus 로고
    • Localization of epidermal growth factor-stimulated Ras/Raf-1 interaction to caveolae membrane
    • DOI 10.1074/jbc.271.20.11930
    • Mineo C, James GL, Smart EJ, Anderson RG. Localization of epidermal growth factor-stimulated Ras/Raf-1interac tion to caveolae membrane. J Biol Chem 1996;271:11930-11935 (Pubitemid 26157268)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.20 , pp. 11930-11935
    • Mineo, C.1    James, G.L.2    Smart, E.J.3    Anderson, R.G.W.4
  • 66
    • 0032696038 scopus 로고    scopus 로고
    • Regulated Migration of Epidermal Growth Factor Receptor from Caveolae
    • Mineo C, Gill GN, Anderson R. Regulated migration of epidermal growth factor receptor from caveolae. J Biol Chem 1999;30636-30643 (Pubitemid 129576804)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.43 , pp. 30636-30643
    • Mineo, C.1    Gill, G.N.2    Anderson, R.G.W.3
  • 67
    • 34250348787 scopus 로고    scopus 로고
    • Activated epidermal growth factor receptor induces integrin α2 internalization via caveolae/raft-dependent endocytic pathway
    • DOI 10.1074/jbc.M610915200
    • Ning Y, Buranda T, Hudson LG. Activated epidermal growth factor receptor induces integrin α2 internalization via caveolae/raft-dependent endocytic pathway. J Biol Chem 2007;282:6380-6387 (Pubitemid 47100824)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.9 , pp. 6380-6387
    • Ning, Y.1    Buranda, T.2    Hudson, L.G.3
  • 69
    • 0027620152 scopus 로고
    • Endocytosis of growth factor receptors
    • Sorkin A, Waters CM. Endocytosis of growth factor receptors. Bioessays 1993;15:375-382 (Pubitemid 23960864)
    • (1993) BioEssays , vol.15 , Issue.6 , pp. 375-382
    • Sorkin, A.1    Waters, C.M.2
  • 71
    • 0034158315 scopus 로고    scopus 로고
    • Caveolins and cellular cholesterol balance
    • Ikonen E, Parton RG. Caveolins and cellular cholesterol balance. Traffic 2000;1:212-217
    • (2000) Traffic , vol.1 , pp. 212-217
    • Ikonen, E.1    Parton, R.G.2
  • 72
    • 0032575524 scopus 로고    scopus 로고
    • Cholesterol depletion delocalizes phosphatidylinositol bisphosphate and inhibits hormone-stimulated phosphatidylinositol turnover
    • DOI 10.1074/jbc.273.35.22298
    • Pike LJ, Miller JM. Cholesterol depletion delocalizes phosphatidylinositol biphosphate and inhibits hormone-stimulated phosphatidylinositol turnover. J Biol Chem 1998;273:22298-22304 (Pubitemid 28399788)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.35 , pp. 22298-22304
    • Pike, L.J.1    Miller, J.M.2
  • 73
    • 38649103149 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate induces the association of membrane-type 1 matrix metalloproteinase with p130Cas in endothelial cells
    • Gingras D, Michaud M, Tomasso G, Béliveau E, Nyalendo C, Béliveau R. Sphingosine-1-phosphate induces the association of membrane-type 1 matrix metalloproteinase with p130Cas in endothelial cells. FEBS Lett 2008;582:399-404.
    • (2008) FEBS Lett , vol.582 , pp. 399-404
    • Gingras, D.1    Michaud, M.2    Tomasso, G.3    Béliveau, E.4    Nyalendo, C.5    Béliveau, R.6
  • 74
    • 49649112970 scopus 로고    scopus 로고
    • Impaired tyrosine phosphorylation of membrane-type 1matrix metalloproteinase reduces tumor cell proliferation in three-dimensional matrices and abrogates tumor growth in mice
    • Nyalendo C, Beaulieu E, Sartelet H, et al. Impaired tyrosine phosphorylation of membrane-type 1matrix metalloproteinase reduces tumor cell proliferation in three-dimensional matrices and abrogates tumor growth in mice. Carcinogenesis 2008;29:1655-1664
    • (2008) Carcinogenesis , vol.29 , pp. 1655-1664
    • Nyalendo, C.1    Beaulieu, E.2    Sartelet, H.3
  • 75
    • 47549085187 scopus 로고    scopus 로고
    • Phenotypic plasticity of neoplastic ovarian epithelium: Unique cadherin profiles in tumor progression
    • Hudson LG, Zeineldin R, Stack MS. Phenotypic plasticity of neoplastic ovarian epithelium: unique cadherin profiles in tumor progression. Clin Exp Metastasis 2008;25:643-655
    • (2008) Clin Exp Metastasis , vol.25 , pp. 643-655
    • Hudson, L.G.1    Zeineldin, R.2    Stack, M.S.3
  • 76
    • 0029741632 scopus 로고    scopus 로고
    • Evidence for preferential adhesion of ovarian epithelial carcinoma cells to type I collagen mediated by the α2β1 integrin
    • DOI 10.1002/(SICI)1097-0215(19960904)67:5<695::AID-IJC18>3.0.CO;2-4
    • Moser TL, Pizzo SV, Bafetti LM, Fishman DA, Stack MS. Evidence for preferential adhesion of ovarian epithelial carcinoma cells to type I collagen mediated by the α2β1 integrin. Int J Cancer 1996;67:695-701. (Pubitemid 26300989)
    • (1996) International Journal of Cancer , vol.67 , Issue.5 , pp. 695-701
    • Moser, T.L.1    Pizzo, S.V.2    Bafetti, L.M.3    Fishman, D.A.4    Stack, M.S.5
  • 77
    • 0029753004 scopus 로고    scopus 로고
    • Expression of membrane-type matrix metalloproteinase 1 (MT1-MMP) in tumor cells enhances pulmonary metastasis in an experimental metastasis assay
    • Tsunezuka Y, Kino H, Takino T, et al. Expression of membrane-type matrix metalloproteinase I (MT1-MMP) in tumor cells enhances pulmonary metastasis in an experimental metastasis. Cancer Res 1996;56:5678-5683 (Pubitemid 26422172)
    • (1996) Cancer Research , vol.56 , Issue.24 , pp. 5678-5683
    • Tsunezuka, Y.1    Kinoh, H.2    Takino, T.3    Watanabe, Y.4    Okada, Y.5    Shinagawa, A.6    Sato, H.7    Seiki, M.8
  • 78
    • 0028285191 scopus 로고
    • Caveolae, caveolin and caveolin-rich membrane domains: A signalling hypothesis
    • DOI 10.1016/0962-8924(94)90114-7
    • Lisanti MP, Scherer P, Tang ZL, Sargiacomo M. Caveolae, caveolin and caveolin-rich membrane domains: a signaling hypothesis. Trends Cell Biol 1994;4:231-235 (Pubitemid 24190653)
    • (1994) Trends in Cell Biology , vol.4 , Issue.7 , pp. 231-235
    • Lisanti, M.P.1    Scherer, P.E.2    Tang, Z.3    Sargiacomo, M.4
  • 79
    • 0037306525 scopus 로고    scopus 로고
    • Caveolae: Anchored, multifunctional platforms in the lipid ocean
    • DOI 10.1016/S0962-8924(02)00039-9, PII S0962892402000399
    • van Deurs B, Roepstorff K, Hommelgaard AM, Sandvig K. Caveolae: anchored, multifunctional platforms in the lipid ocean. Trends Cell Biol 2003;13:92-100. (Pubitemid 36135891)
    • (2003) Trends in Cell Biology , vol.13 , Issue.2 , pp. 92-100
    • Van Deurs, B.1    Roepstorff, K.2    Hommelgaard, A.M.3    Sandvig, K.4
  • 81
    • 0031692336 scopus 로고    scopus 로고
    • The caveolae membrane system
    • DOI 10.1146/annurev.biochem.67.1.199
    • Anderson RGW. The caveolae membrane system. Annu Rev Biochem 1998;67:199-225. (Pubitemid 28411129)
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 199-225
    • Anderson, R.G.W.1
  • 82
    • 0036830114 scopus 로고    scopus 로고
    • Multiple functions of caveolin-1
    • DOI 10.1074/jbc.R200020200
    • Liu P, Rudick M, Anderson RG. Multiple functions of caveolin-1. J Biol Chem 2002;277:41295-41298 (Pubitemid 35257426)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.44 , pp. 41295-41298
    • Rudick, M.1    Anderson, R.G.W.2
  • 84
    • 0037237791 scopus 로고    scopus 로고
    • Src-mediated tyrosine phosphorylation of caveolin-1induces its association with membrane type 1matrix metalloproteinase
    • Labrecque L, Royal I, Surprenant DS, Patterson C, Gingras D, Beliveau R. Src-mediated tyrosine phosphorylation of caveolin-1induces its association with membrane type 1matrix metalloproteinase. Mol Biol Cell 2003;14:334-347
    • (2003) Mol Biol Cell , vol.14 , pp. 334-347
    • Labrecque, L.1    Royal, I.2    Surprenant, D.S.3    Patterson, C.4    Gingras, D.5    Beliveau, R.6
  • 85
    • 0029912981 scopus 로고    scopus 로고
    • Co-purification and direct interaction of ras with caveolin, an integral membrane protein of caveolae microdomains
    • Song KS, Shengwen L, Okamoto T, Quilliam LA, Sargiacomo M, Lisanti MP. Co-purification and direct interaction of ras with caveolin, an integral membrane protein of caveolae microdomains. J Biol Chem 1996;271:9690-9697
    • (1996) J Biol Chem , vol.271 , pp. 9690-9697
    • Song, K.S.1    Shengwen, L.2    Okamoto, T.3    Quilliam, L.A.4    Sargiacomo, M.5    Lisanti, M.P.6
  • 86
    • 0032516835 scopus 로고    scopus 로고
    • Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase (ERK)
    • DOI 10.1074/jbc.273.33.21099
    • Furuchi T, Anderson RGW. Cholesterol depletion of caveolae causes hyperactivation of extracellular signal related kinase (ERK). J Biol Chem 1998;273:21099-21104 (Pubitemid 28385396)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.33 , pp. 21099-21104
    • Furuchi, T.1    Anderson, R.G.W.2
  • 88
    • 0033555946 scopus 로고    scopus 로고
    • 2-adrenergic receptor internalization and mitogen-activated protein kinase signaling
    • Ahn S, Maudsley S, Luttrell LM, Lefkowitz RJ, Daaka Y. Src-mediated tyrosine phosphorylation of dynamin is required for β2-adrenergic receptor internalization and mitogen-activated protein kinase signaling. J Biol Chem 1999;274:1185-1188 (Pubitemid 129507696)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.3 , pp. 1185-1188
    • Ahn, S.1    Maudsley, S.2    Luttrell, L.M.3    Lefkowitz, R.J.4    Daaka, Y.5
  • 89
    • 0035945354 scopus 로고    scopus 로고
    • Cytoplasmic tail-dependent internalization of membrane-type 1 matrix metalloproteinase is important for its invasion-promoting activity
    • DOI 10.1083/jcb.200108112
    • Uekita T, Itoh Y, Yana I, Ohno H, Seiki M. Cytoplasmic tail-dependent internalization of membrane type 1 matrix metalloproteinase is important for its invasion-promoting activity. J Cell Biol 2001;155:1345-1356 (Pubitemid 34286282)
    • (2001) Journal of Cell Biology , vol.155 , Issue.7 , pp. 1345-1356
    • Uekita, T.1    Itoh, Y.2    Yana, I.3    Ohno, H.4    Seiki, M.5
  • 90
    • 0036479204 scopus 로고    scopus 로고
    • Caveolin-1 is a negative regulator of caveolae-mediated endocytosis to the endoplasmic reticulum
    • DOI 10.1074/jbc.M111240200
    • Le P, Guay G, Altschuler Y, Nabi IR. Caveolin-1is a negative regulator of caveolae mediated endocytosis to the endoplasmic reticulum. J Biol Chem 2002;277:3371-3379 (Pubitemid 34953205)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.5 , pp. 3371-3379
    • Le, P.U.1    Guay, G.2    Altschuler, Y.3    Nabi, I.R.4
  • 91
    • 0034605039 scopus 로고    scopus 로고
    • Endothelial cell surface gp60 activates vesicle formation and trafficking via G (i)-coupled Src kinase signaling pathway
    • Minshall RD, Tiruppathi C, Vogel SM, et al. Endothelial cell surface gp60 activates vesicle formation and trafficking via G (i)-coupled Src kinase signaling pathway. J Cell Biol 2000;150:1057-1070
    • (2000) J Cell Biol , vol.150 , pp. 1057-1070
    • Minshall, R.D.1    Tiruppathi, C.2    Vogel, S.M.3
  • 92
    • 0036151510 scopus 로고    scopus 로고
    • Caveolae are highly immobile plasma membrane microdomains, which are not involved in constitutive endocytic trafficking
    • DOI 10.1091/mbc.01-06-0317
    • Thomsen P, Roepstorff K, Stahlhut M, Van Deurs B. Caveolae are highly immobile plasma membrane microdomains, which are not involved in constitutive endocytic trafficking. Mol Biol Cell 2002;13:238-250 (Pubitemid 34106072)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.1 , pp. 238-250
    • Thomsen, P.1    Roepstorff, K.2    Stahlhut, M.3    Van Deurs, B.4
  • 93
    • 0242268532 scopus 로고    scopus 로고
    • Lipid rafts and caveolae as portals for endocytosis: New insights and common mechanisms
    • DOI 10.1034/j.1600-0854.2003.00128.x
    • Parton RG, Richards AA. Lipid rafts and caveolae as portals for endocytosis: new insights and common mechanisms. Traffic 2003;4:724-738 (Pubitemid 37361854)
    • (2003) Traffic , vol.4 , Issue.11 , pp. 724-738
    • Parton, R.G.1    Richards, A.A.2
  • 94
    • 0034677942 scopus 로고    scopus 로고
    • Epidermal growth factor-stimulated tyrosine phosphorylation of caveolin- 1. Enhanced caveolin-1 tyrosine phosphorylation following aberrant epidermal growth factor receptor status
    • DOI 10.1074/jbc.275.11.7481
    • Kim YN, Wiepz GJ, Guadarrama AG, Bertics PJ. Epidermal growth factor-stimulated tyrosine phosphorylation of caveolin-1. Enhanced caveolin-1 tyrosine phosphorylation following aberrant epidermal growth factor receptor status. J Biol Chem 2000;275:7481-7491 (Pubitemid 30159643)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.11 , pp. 7481-7491
    • Kim, Y.-N.1    Wiepz, G.J.2    Guadarrama, A.G.3    Bertics, P.J.4
  • 95
    • 34447522132 scopus 로고    scopus 로고
    • Src-dependent phosphorylation of membrane type I matrix metalloproteinase on cytoplasmic tyrosine 573: Role in endothelial and tumor cell migration
    • DOI 10.1074/jbc.M608045200
    • Nyalendo C, Michaud M, Beaulieu E, et al. Src dependent phosphorylation of membrane-type I matrix metallopoteinase on cytoplasmic tyrosine 573: role in endothelial and tumor cell migration. J Biol Chem 2007;282:15690-15699 (Pubitemid 47093303)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.21 , pp. 15690-15699
    • Nyalendo, C.1    Michaud, M.2    Beaulieu, E.3    Roghi, C.4    Murphy, G.5    Gingras, D.6    Beliveau, R.7
  • 97
    • 0032854578 scopus 로고    scopus 로고
    • Specialized surface protrusions of invasive cells, invadopodia and lamellipodia, have differential MT1-MMP, MMP-2, and TIMP-2 localization
    • DOI 10.1111/j.1749-6632.1999.tb07695.x
    • Chen WT, Wang JY. Specialized surface protrusions of invasive cells, invadopodia and lamellipodia, have differential MT1-MMP, MMP-2, and TIMP-2 localization. Ann N Y Acad Sci 1990;878:361-371 (Pubitemid 29353581)
    • (1999) Annals of the New York Academy of Sciences , vol.878 , pp. 361-371
    • Chen, W.-T.1    Wang, J.-Y.2
  • 98
    • 0034685778 scopus 로고    scopus 로고
    • Regulation of membrane-type-1 matrix metalloproteinase activity by its cytoplasmic domain
    • DOI 10.1074/jbc.M910220199
    • Lehti K, Valtanen H, Wickström SA, Lohi J, Keski-Oja J. Regulation of membrane-type-1 matrix metalloproteinase activity by its cytoplasmic domain. J Biol Chem 2000;275:15006-15013 (Pubitemid 30337219)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.20 , pp. 15006-15013
    • Lehti, K.1    Valtanen, H.2    Wickstrom, S.3    Lohi, J.4    Keski-Oja, J.5
  • 99
    • 33645507413 scopus 로고    scopus 로고
    • Dynamic interactions of cortactin and membrane type 1matrix metalloproteinase at invadopodia: Defining the stages of invadopodia formation and function
    • Artym VV, Zhang Y, Seillier-Moiseiwitsch F, Yamada KM, Mueller SC. Dynamic interactions of cortactin and membrane type 1matrix metalloproteinase at invadopodia: defining the stages of invadopodia formation and function. Cancer Res 2006;66:3034-3043
    • (2006) Cancer Res , vol.66 , pp. 3034-3043
    • Artym, V.V.1    Zhang, Y.2    Seillier-Moiseiwitsch, F.3    Yamada, K.M.4    Mueller, S.C.5
  • 100
    • 34547569807 scopus 로고    scopus 로고
    • Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion
    • DOI 10.1038/ncb1616, PII NCB1616
    • Wolf K, Wu YI, Liu Y, et al. Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion. Nat Cell Biol 2007;9:893-904. (Pubitemid 47190444)
    • (2007) Nature Cell Biology , vol.9 , Issue.8 , pp. 893-904
    • Wolf, K.1    Wu, Y.I.2    Liu, Y.3    Geiger, J.4    Tam, E.5    Overall, C.6    Stack, M.S.7    Friedl, P.8
  • 102
    • 33750495804 scopus 로고    scopus 로고
    • A critical role for the membrane-type 1 matrix metalloproteinase in collagen phagocytosis
    • DOI 10.1091/mbc.E06-06-0486
    • Lee H, Overall CM, McCulloch CA, Sodek J. A critical role for the membrane-type 1 matrix metalloproteinase in collagen phagocytosis. Mol Biol Cell 2006;17:4812-4826 (Pubitemid 44665750)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.11 , pp. 4812-4826
    • Lee, H.1    Overall, C.M.2    McCulloch, C.A.3    Sodek, J.4
  • 103
    • 0037064041 scopus 로고    scopus 로고
    • Collagen binding properties of the membrane type-1 matrix metalloproteinase (MT1-MMP) hemopexin C domain: The ectodomain of the 44-kDa autocatalytic product of MT1-MMP inhibits cell invasion by disrupting native type I collagen cleavage
    • DOI 10.1074/jbc.M206874200
    • Tam EM, Wu YI, Butler GS, Stack MS, Overall CM. Collagen binding properties of the membrane type-1 matrix metalloproteinase (MT1-MMP) hemopexin C domain. The ectodomain of the 44-kDa autocatalytic product of MT1-MMP inhibits cell invasion by disrupting native type I collagen cleavage. J Biol Chem 2002;277:39005-39014 (Pubitemid 35154767)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.41 , pp. 39005-39014
    • Tam, E.M.1    Wu, Y.I.2    Butler, G.S.3    Sharon Stack, M.4    Overall, C.M.5
  • 104
    • 0035801473 scopus 로고    scopus 로고
    • Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion
    • DOI 10.1093/emboj/20.17.4782
    • Itoh Y, Takamura A, Ito N, et al. Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion. EMBO J 2001;20:4782-4793 (Pubitemid 32848631)
    • (2001) EMBO Journal , vol.20 , Issue.17 , pp. 4782-4793
    • Itoh, Y.1    Takamura, A.2    Ito, N.3    Maru, Y.4    Sato, H.5    Suenaga, N.6    Aoki, T.7    Seiki, M.8


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