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Volumn 1803, Issue 11, 2010, Pages 1287-1297

Posttranslational regulation of membrane type 1-matrix metalloproteinase (MT1-MMP) in mouse PTEN null prostate cancer cells: Enhanced surface expression and differential O-glycosylation of MT1-MMP

Author keywords

Glycosylation; Matrix metalloproteinases; Posttranslational modification; Prostate cancer; PTEN

Indexed keywords

COLLAGEN; MATRIX METALLOPROTEINASE 14; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PROTEIN KINASE B; RAPAMYCIN;

EID: 77956476631     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2010.06.011     Document Type: Article
Times cited : (26)

References (71)
  • 1
    • 0031656460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: structures, evolution, and diversification
    • Massova I., Kotra L.P., Fridman R., Mobashery S. Matrix metalloproteinases: structures, evolution, and diversification. FASEB J. 1998, 12:1075-1095.
    • (1998) FASEB J. , vol.12 , pp. 1075-1095
    • Massova, I.1    Kotra, L.P.2    Fridman, R.3    Mobashery, S.4
  • 3
    • 2642546699 scopus 로고    scopus 로고
    • Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MT1-MMP)
    • Osenkowski P., Toth M., Fridman R. Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MT1-MMP). J. Cell. Physiol. 2004, 200:2-10.
    • (2004) J. Cell. Physiol. , vol.200 , pp. 2-10
    • Osenkowski, P.1    Toth, M.2    Fridman, R.3
  • 4
    • 33749535260 scopus 로고    scopus 로고
    • MT1-MMP: a key regulator of cell migration in tissue
    • Itoh Y. MT1-MMP: a key regulator of cell migration in tissue. IUBMB Life 2006, 58:589-596.
    • (2006) IUBMB Life , vol.58 , pp. 589-596
    • Itoh, Y.1
  • 5
    • 33845396458 scopus 로고    scopus 로고
    • Cell surface collagenolysis requires homodimerization of the membrane-bound collagenase MT1-MMP
    • Itoh Y., Ito N., Nagase H., Evans R.D., Bird S.A., Seiki M. Cell surface collagenolysis requires homodimerization of the membrane-bound collagenase MT1-MMP. Mol. Biol. Cell 2006, 17:5390-5399.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 5390-5399
    • Itoh, Y.1    Ito, N.2    Nagase, H.3    Evans, R.D.4    Bird, S.A.5    Seiki, M.6
  • 6
    • 28444454893 scopus 로고    scopus 로고
    • MT1-MMP: a potent modifier of pericellular microenvironment
    • Itoh Y., Seiki M. MT1-MMP: a potent modifier of pericellular microenvironment. J. Cell. Physiol. 2006, 206:1-8.
    • (2006) J. Cell. Physiol. , vol.206 , pp. 1-8
    • Itoh, Y.1    Seiki, M.2
  • 9
    • 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
    • Nyalendo C., Michaud M., Beaulieu E., Roghi C., Murphy G., Gingras D., Beliveau R. Src-dependent phosphorylation of membrane type I matrix metalloproteinase on cytoplasmic tyrosine 573: role in endothelial and tumor cell migration. J. Biol. Chem. 2007, 282:15690-15699.
    • (2007) J. Biol. Chem. , vol.282 , pp. 15690-15699
    • Nyalendo, C.1    Michaud, M.2    Beaulieu, E.3    Roghi, C.4    Murphy, G.5    Gingras, D.6    Beliveau, R.7
  • 10
    • 23444460823 scopus 로고    scopus 로고
    • Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration
    • Anilkumar N., Uekita T., Couchman J.R., Nagase H., Seiki M., Itoh Y. Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration. FASEB J. 2005, 19:1326-1328.
    • (2005) FASEB J. , vol.19 , pp. 1326-1328
    • Anilkumar, N.1    Uekita, T.2    Couchman, J.R.3    Nagase, H.4    Seiki, M.5    Itoh, Y.6
  • 11
    • 58049218443 scopus 로고    scopus 로고
    • Identification and role of the homodimerization interface of the glycosylphosphatidylinositol-anchored membrane type 6 matrix metalloproteinase (MMP25)
    • Zhao H., Sohail A., Sun Q., Shi Q., Kim S., Mobashery S., Fridman R. Identification and role of the homodimerization interface of the glycosylphosphatidylinositol-anchored membrane type 6 matrix metalloproteinase (MMP25). J. Biol. Chem. 2008, 283:35023-35032.
    • (2008) J. Biol. Chem. , vol.283 , pp. 35023-35032
    • Zhao, H.1    Sohail, A.2    Sun, Q.3    Shi, Q.4    Kim, S.5    Mobashery, S.6    Fridman, R.7
  • 12
    • 33749350351 scopus 로고    scopus 로고
    • A cancer cell metalloprotease triad regulates the basement membrane transmigration program
    • Hotary K., Li X.Y., Allen E., Stevens S.L., Weiss S.J. A cancer cell metalloprotease triad regulates the basement membrane transmigration program. Genes Dev. 2006, 20:2673-2686.
    • (2006) Genes Dev. , vol.20 , pp. 2673-2686
    • Hotary, K.1    Li, X.Y.2    Allen, E.3    Stevens, S.L.4    Weiss, S.J.5
  • 13
    • 0038784546 scopus 로고    scopus 로고
    • Membrane type I matrix metalloproteinase usurps tumor growth control imposed by the three-dimensional extracellular matrix
    • Hotary K.B., Allen E.D., Brooks P.C., Datta N.S., Long M.W., Weiss S.J. Membrane type I matrix metalloproteinase usurps tumor growth control imposed by the three-dimensional extracellular matrix. Cell 2003, 114:33-45.
    • (2003) Cell , vol.114 , 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
  • 15
    • 33750450547 scopus 로고    scopus 로고
    • Prostate cancer progression into androgen independency is associated with alterations in cell adhesion and invasivity
    • Jennbacken K., Gustavsson H., Welen K., Vallbo C., Damber J.E. Prostate cancer progression into androgen independency is associated with alterations in cell adhesion and invasivity. Prostate 2006, 66:1631-1640.
    • (2006) Prostate , vol.66 , pp. 1631-1640
    • Jennbacken, K.1    Gustavsson, H.2    Welen, K.3    Vallbo, C.4    Damber, J.E.5
  • 16
    • 0038713422 scopus 로고    scopus 로고
    • Membrane type-1-matrix metalloproteinase expressed by prostate carcinoma cells cleaves human laminin-5 beta3 chain and induces cell migration
    • Udayakumar T.S., Chen M.L., Bair E.L., Von Bredow D.C., Cress A.E., Nagle R.B., Bowden G.T. Membrane type-1-matrix metalloproteinase expressed by prostate carcinoma cells cleaves human laminin-5 beta3 chain and induces cell migration. Cancer Res. 2003, 63:2292-2299.
    • (2003) Cancer Res. , vol.63 , pp. 2292-2299
    • Udayakumar, T.S.1    Chen, M.L.2    Bair, E.L.3    Von Bredow, D.C.4    Cress, A.E.5    Nagle, R.B.6    Bowden, G.T.7
  • 17
    • 16844383171 scopus 로고    scopus 로고
    • Membrane type 1-matrix metalloproteinase promotes human prostate cancer invasion and metastasis
    • Cao J., Chiarelli C., Kozarekar P., Adler H.L. Membrane type 1-matrix metalloproteinase promotes human prostate cancer invasion and metastasis. Thromb. Haemost. 2005, 93:770-778.
    • (2005) Thromb. Haemost. , vol.93 , pp. 770-778
    • Cao, J.1    Chiarelli, C.2    Kozarekar, P.3    Adler, H.L.4
  • 18
    • 65549140693 scopus 로고    scopus 로고
    • Increased aggressiveness of human prostate PC-3 tumor cells expressing cell surface localized membrane type-1 matrix metalloproteinase (MT1-MMP)
    • Wang X., Wilson M.J., Slaton J.W., Sinha A.A., Ewing S.L., Pei D. Increased aggressiveness of human prostate PC-3 tumor cells expressing cell surface localized membrane type-1 matrix metalloproteinase (MT1-MMP). J. Androl. 2009, 30:259-274.
    • (2009) J. Androl. , vol.30 , pp. 259-274
    • Wang, X.1    Wilson, M.J.2    Slaton, J.W.3    Sinha, A.A.4    Ewing, S.L.5    Pei, D.6
  • 19
    • 44449173164 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase induces epithelial-to-mesenchymal transition in prostate cancer
    • Cao J., Chiarelli C., Richman O., Zarrabi K., Kozarekar P., Zucker S. Membrane type 1 matrix metalloproteinase induces epithelial-to-mesenchymal transition in prostate cancer. J. Biol. Chem. 2008, 283:6232-6240.
    • (2008) J. Biol. Chem. , vol.283 , pp. 6232-6240
    • Cao, J.1    Chiarelli, C.2    Richman, O.3    Zarrabi, K.4    Kozarekar, P.5    Zucker, S.6
  • 20
    • 33645825874 scopus 로고    scopus 로고
    • Quantitative immunohistochemical and in situ hybridization analysis of metalloproteinases in prostate cancer
    • Cardillo M.R., Di Silverio F., Gentile V. Quantitative immunohistochemical and in situ hybridization analysis of metalloproteinases in prostate cancer. Anticancer Res. 2006, 26:973-982.
    • (2006) Anticancer Res. , vol.26 , pp. 973-982
    • Cardillo, M.R.1    Di Silverio, F.2    Gentile, V.3
  • 21
    • 42649083654 scopus 로고    scopus 로고
    • Membrane-type-1 matrix metalloproteinase, matrix metalloproteinase 2, and tissue inhibitor of matrix proteinase 2 in prostate cancer: identification of patients with poor prognosis by immunohistochemistry
    • Trudel D., Fradet Y., Meyer F., Harel F., Tetu B. Membrane-type-1 matrix metalloproteinase, matrix metalloproteinase 2, and tissue inhibitor of matrix proteinase 2 in prostate cancer: identification of patients with poor prognosis by immunohistochemistry. Hum. Pathol. 2008, 39:731-739.
    • (2008) Hum. Pathol. , vol.39 , pp. 731-739
    • Trudel, D.1    Fradet, Y.2    Meyer, F.3    Harel, F.4    Tetu, B.5
  • 22
    • 0033376888 scopus 로고    scopus 로고
    • Membrane type 1-matrix metalloproteinase (MT1-MMP) and MMP-2 immunolocalization in human prostate: change in cellular localization associated with high-grade prostatic intraepithelial neoplasia
    • Upadhyay J., Shekarriz B., Nemeth J.A., Dong Z., Cummings G.D., Fridman R., Sakr W., Grignon D.J., Cher M.L. Membrane type 1-matrix metalloproteinase (MT1-MMP) and MMP-2 immunolocalization in human prostate: change in cellular localization associated with high-grade prostatic intraepithelial neoplasia. Clin. Cancer Res. 1999, 5:4105-4110.
    • (1999) Clin. Cancer Res. , vol.5 , pp. 4105-4110
    • Upadhyay, J.1    Shekarriz, B.2    Nemeth, J.A.3    Dong, Z.4    Cummings, G.D.5    Fridman, R.6    Sakr, W.7    Grignon, D.J.8    Cher, M.L.9
  • 23
    • 0033856110 scopus 로고    scopus 로고
    • PTEN, a unique tumor suppressor gene
    • Dahia P.L. PTEN, a unique tumor suppressor gene. Endocr. Relat. Cancer 2000, 7:115-129.
    • (2000) Endocr. Relat. Cancer , vol.7 , pp. 115-129
    • Dahia, P.L.1
  • 25
    • 0031922369 scopus 로고    scopus 로고
    • Homozygous deletion of the PTEN tumor suppressor gene in a subset of prostate adenocarcinomas
    • Wang S.I., Parsons R., Ittmann M. Homozygous deletion of the PTEN tumor suppressor gene in a subset of prostate adenocarcinomas. Clin. Cancer Res. 1998, 4:811-815.
    • (1998) Clin. Cancer Res. , vol.4 , pp. 811-815
    • Wang, S.I.1    Parsons, R.2    Ittmann, M.3
  • 26
    • 53849146755 scopus 로고    scopus 로고
    • Is PTEN loss associated with clinical outcome measures in human prostate cancer?
    • McCall P., Witton C.J., Grimsley S., Nielsen K.V., Edwards J. Is PTEN loss associated with clinical outcome measures in human prostate cancer?. Br. J. Cancer 2008, 99:1296-1301.
    • (2008) Br. J. Cancer , vol.99 , pp. 1296-1301
    • McCall, P.1    Witton, C.J.2    Grimsley, S.3    Nielsen, K.V.4    Edwards, J.5
  • 28
    • 34548299547 scopus 로고    scopus 로고
    • FISH analysis of 107 prostate cancers shows that PTEN genomic deletion is associated with poor clinical outcome
    • Yoshimoto M., Cunha I.W., Coudry R.A., Fonseca F.P., Torres C.H., Soares F.A., Squire J.A. FISH analysis of 107 prostate cancers shows that PTEN genomic deletion is associated with poor clinical outcome. Br. J. Cancer 2007, 97:678-685.
    • (2007) Br. J. Cancer , vol.97 , pp. 678-685
    • Yoshimoto, M.1    Cunha, I.W.2    Coudry, R.A.3    Fonseca, F.P.4    Torres, C.H.5    Soares, F.A.6    Squire, J.A.7
  • 29
    • 0033200172 scopus 로고    scopus 로고
    • Loss of PTEN expression in paraffin-embedded primary prostate cancer correlates with high Gleason score and advanced stage
    • McMenamin M.E., Soung P., Perera S., Kaplan I., Loda M., Sellers W.R. Loss of PTEN expression in paraffin-embedded primary prostate cancer correlates with high Gleason score and advanced stage. Cancer Res. 1999, 59:4291-4296.
    • (1999) Cancer Res. , vol.59 , pp. 4291-4296
    • McMenamin, M.E.1    Soung, P.2    Perera, S.3    Kaplan, I.4    Loda, M.5    Sellers, W.R.6
  • 34
    • 10744221757 scopus 로고    scopus 로고
    • Differential inhibition of membrane type 3 (MT3)-matrix metalloproteinase (MMP) and MT1-MMP by tissue inhibitor of metalloproteinase (TIMP)-2 and TIMP-3 rgulates pro-MMP-2 activation
    • Zhao H., Bernardo M.M., Osenkowski P., Sohail A., Pei D., Nagase H., Kashiwagi M., Soloway P.D., DeClerck Y.A., Fridman R. Differential inhibition of membrane type 3 (MT3)-matrix metalloproteinase (MMP) and MT1-MMP by tissue inhibitor of metalloproteinase (TIMP)-2 and TIMP-3 rgulates pro-MMP-2 activation. J. Biol. Chem. 2004, 279:8592-8601.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8592-8601
    • Zhao, H.1    Bernardo, M.M.2    Osenkowski, P.3    Sohail, A.4    Pei, D.5    Nagase, H.6    Kashiwagi, M.7    Soloway, P.D.8    DeClerck, Y.A.9    Fridman, R.10
  • 35
    • 17644411110 scopus 로고    scopus 로고
    • Culture of mouse prostatic epithelial cells from genetically engineered mice
    • Barclay W.W., Cramer S.D. Culture of mouse prostatic epithelial cells from genetically engineered mice. Prostate 2005, 63:291-298.
    • (2005) Prostate , vol.63 , pp. 291-298
    • Barclay, W.W.1    Cramer, S.D.2
  • 36
    • 43049125543 scopus 로고    scopus 로고
    • Characterization of adult prostatic progenitor/stem cells exhibiting self-renewal and multilineage differentiation
    • Barclay W.W., Axanova L.S., Chen W., Romero L., Maund S.L., Soker S., Lees C.J., Cramer S.D. Characterization of adult prostatic progenitor/stem cells exhibiting self-renewal and multilineage differentiation. Stem Cells 2008, 26:600-610.
    • (2008) Stem Cells , vol.26 , pp. 600-610
    • Barclay, W.W.1    Axanova, L.S.2    Chen, W.3    Romero, L.4    Maund, S.L.5    Soker, S.6    Lees, C.J.7    Cramer, S.D.8
  • 37
    • 47749156773 scopus 로고    scopus 로고
    • The inactive 44-kDa processed form of membrane type 1 matrix metalloproteinase (MT1-MMP) enhances proteolytic activity via regulation of endocytosis of active MT1-MMP
    • Cho J.A., Osenkowski P., Zhao H., Kim S., Toth M., Cole K., Aboukameel A., Saliganan A., Schuger L., Bonfil R.D., Fridman R. The inactive 44-kDa processed form of membrane type 1 matrix metalloproteinase (MT1-MMP) enhances proteolytic activity via regulation of endocytosis of active MT1-MMP. J. Biol. Chem. 2008, 283:17391-17405.
    • (2008) J. Biol. Chem. , vol.283 , pp. 17391-17405
    • Cho, J.A.1    Osenkowski, P.2    Zhao, H.3    Kim, S.4    Toth, M.5    Cole, K.6    Aboukameel, A.7    Saliganan, A.8    Schuger, L.9    Bonfil, R.D.10    Fridman, R.11
  • 38
    • 0030755456 scopus 로고    scopus 로고
    • Phorbol ester-induced cell surface association of matrix metalloproteinase-9 in human MCF10A breast epithelial cells
    • Toth M., Gervasi D.C., Fridman R. Phorbol ester-induced cell surface association of matrix metalloproteinase-9 in human MCF10A breast epithelial cells. Cancer Res. 1997, 57:3159-3167.
    • (1997) Cancer Res. , vol.57 , pp. 3159-3167
    • Toth, M.1    Gervasi, D.C.2    Fridman, R.3
  • 39
    • 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
    • Hotary K., Allen E., Punturieri A., Yana I., Weiss S.J. 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.
    • (2000) J. Cell Biol. , vol.149 , pp. 1309-1323
    • Hotary, K.1    Allen, E.2    Punturieri, A.3    Yana, I.4    Weiss, S.J.5
  • 40
    • 58149093961 scopus 로고    scopus 로고
    • The cytoplasmic tail dileucine motif LL572 determines the glycosylation pattern of membrane-type 1 matrix metalloproteinase
    • Ludwig T., Theissen S.M., Morton M.J., Caplan M.J. The cytoplasmic tail dileucine motif LL572 determines the glycosylation pattern of membrane-type 1 matrix metalloproteinase. J. Biol. Chem. 2008, 283:35410-35418.
    • (2008) J. Biol. Chem. , vol.283 , pp. 35410-35418
    • Ludwig, T.1    Theissen, S.M.2    Morton, M.J.3    Caplan, M.J.4
  • 41
  • 43
    • 0030581638 scopus 로고    scopus 로고
    • Carbohydrate-mediated regulation of matrix metalloproteinase-2 activation in normal human fibroblasts and fibrosarcoma cells
    • Gervasi D.C., Raz A., Dehem M., Yang M., Kurkinen M., Fridman R. Carbohydrate-mediated regulation of matrix metalloproteinase-2 activation in normal human fibroblasts and fibrosarcoma cells. Biochem. Biophys. Res. Commun. 1996, 228:530-538.
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 530-538
    • Gervasi, D.C.1    Raz, A.2    Dehem, M.3    Yang, M.4    Kurkinen, M.5    Fridman, R.6
  • 44
    • 1242297705 scopus 로고    scopus 로고
    • Limited processing of pro-matrix metalloprotease-2 (gelatinase A) overexpressed by transfection in PC-3 human prostate tumor cells: association with restricted cell surface localization of membrane-type matrix metalloproteinase-1
    • Wilson M.J., Jiang A., Wiehr C., Wang X., Sinha A.A., Pei D. Limited processing of pro-matrix metalloprotease-2 (gelatinase A) overexpressed by transfection in PC-3 human prostate tumor cells: association with restricted cell surface localization of membrane-type matrix metalloproteinase-1. J. Androl. 2004, 25:274-285.
    • (2004) J. Androl. , vol.25 , pp. 274-285
    • Wilson, M.J.1    Jiang, A.2    Wiehr, C.3    Wang, X.4    Sinha, A.A.5    Pei, D.6
  • 45
    • 69249156451 scopus 로고    scopus 로고
    • Secreted versus membrane-anchored collagenases: relative roles in fibroblast-dependent collagenolysis and invasion
    • Sabeh F., Li X.Y., Saunders T.L., Rowe R.G., Weiss S.J. Secreted versus membrane-anchored collagenases: relative roles in fibroblast-dependent collagenolysis and invasion. J. Biol. Chem. 2009, 284:23001-23011.
    • (2009) J. Biol. Chem. , vol.284 , pp. 23001-23011
    • Sabeh, F.1    Li, X.Y.2    Saunders, T.L.3    Rowe, R.G.4    Weiss, S.J.5
  • 46
    • 35348820823 scopus 로고    scopus 로고
    • Targeting the mTOR signaling network in cancer
    • Chiang G.G., Abraham R.T. Targeting the mTOR signaling network in cancer. Trends Mol. Med. 2007, 13:433-442.
    • (2007) Trends Mol. Med. , vol.13 , pp. 433-442
    • Chiang, G.G.1    Abraham, R.T.2
  • 47
    • 27744569843 scopus 로고    scopus 로고
    • MTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events
    • Holz M.K., Ballif B.A., Gygi S.P., Blenis J. mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events. Cell 2005, 123:569-580.
    • (2005) Cell , vol.123 , pp. 569-580
    • Holz, M.K.1    Ballif, B.A.2    Gygi, S.P.3    Blenis, J.4
  • 48
    • 23844438209 scopus 로고    scopus 로고
    • Activation of Akt and eIF4E survival pathways by rapamycin-mediated mammalian target of rapamycin inhibition
    • Sun S.Y., Rosenberg L.M., Wang X., Zhou Z., Yue P., Fu H., Khuri F.R. Activation of Akt and eIF4E survival pathways by rapamycin-mediated mammalian target of rapamycin inhibition. Cancer Res. 2005, 65:7052-7058.
    • (2005) Cancer Res. , vol.65 , pp. 7052-7058
    • Sun, S.Y.1    Rosenberg, L.M.2    Wang, X.3    Zhou, Z.4    Yue, P.5    Fu, H.6    Khuri, F.R.7
  • 50
    • 40649121309 scopus 로고    scopus 로고
    • Temporally controlled ablation of PTEN in adult mouse prostate epithelium generates a model of invasive prostatic adenocarcinoma
    • Ratnacaram C.K., Teletin M., Jiang M., Meng X., Chambon P., Metzger D. Temporally controlled ablation of PTEN in adult mouse prostate epithelium generates a model of invasive prostatic adenocarcinoma. Proc. Natl. Acad. Sci. USA 2008, 105:2521-2526.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 2521-2526
    • Ratnacaram, C.K.1    Teletin, M.2    Jiang, M.3    Meng, X.4    Chambon, P.5    Metzger, D.6
  • 51
    • 22544471867 scopus 로고    scopus 로고
    • Mutational and structural analyses of the hinge region of membrane type 1-matrix metalloproteinase and enzyme processing
    • Osenkowski P., Meroueh S.O., Pavel D., Mobashery S., Fridman R. Mutational and structural analyses of the hinge region of membrane type 1-matrix metalloproteinase and enzyme processing. J. Biol. Chem. 2005, 280:26160-26168.
    • (2005) J. Biol. Chem. , vol.280 , pp. 26160-26168
    • Osenkowski, P.1    Meroueh, S.O.2    Pavel, D.3    Mobashery, S.4    Fridman, R.5
  • 52
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • Ohtsubo K., Marth J.D. Glycosylation in cellular mechanisms of health and disease. Cell 2006, 126:855-867.
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 53
    • 0042941848 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase regulates membrane Type 1-matrix metalloproteinase (MMP) and MMP-2 activity during melanoma cell vasculogenic mimicry
    • Hess A.R., Seftor E.A., Seftor R.E., Hendrix M.J. Phosphoinositide 3-kinase regulates membrane Type 1-matrix metalloproteinase (MMP) and MMP-2 activity during melanoma cell vasculogenic mimicry. Cancer Res. 2003, 63:4757-4762.
    • (2003) Cancer Res. , vol.63 , pp. 4757-4762
    • Hess, A.R.1    Seftor, E.A.2    Seftor, R.E.3    Hendrix, M.J.4
  • 54
    • 33749315900 scopus 로고    scopus 로고
    • JNK and PI3K differentially regulate MMP-2 and MT1-MMP mRNA and protein in response to actin cytoskeleton reorganization in endothelial cells
    • Ispanovic E., Haas T.L. JNK and PI3K differentially regulate MMP-2 and MT1-MMP mRNA and protein in response to actin cytoskeleton reorganization in endothelial cells. Am. J. Physiol. Cell Physiol. 2006, 291:C579-C588.
    • (2006) Am. J. Physiol. Cell Physiol. , vol.291
    • Ispanovic, E.1    Haas, T.L.2
  • 55
  • 56
    • 34249063875 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase is regulated by sp1 through the differential activation of AKT, JNK, and ERK pathways in human prostate tumor cells
    • Sroka I.C., Nagle R.B., Bowden G.T. Membrane-type 1 matrix metalloproteinase is regulated by sp1 through the differential activation of AKT, JNK, and ERK pathways in human prostate tumor cells. Neoplasia 2007, 9:406-417.
    • (2007) Neoplasia , vol.9 , pp. 406-417
    • Sroka, I.C.1    Nagle, R.B.2    Bowden, G.T.3
  • 57
    • 0037455716 scopus 로고    scopus 로고
    • Type 1 insulin-like growth factor regulates MT1-MMP synthesis and tumor invasion via PI 3-kinase/Akt signaling
    • Zhang D., Brodt P. Type 1 insulin-like growth factor regulates MT1-MMP synthesis and tumor invasion via PI 3-kinase/Akt signaling. Oncogene 2003, 22:974-982.
    • (2003) Oncogene , vol.22 , pp. 974-982
    • Zhang, D.1    Brodt, P.2
  • 61
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • Sarbassov D.D., Guertin D.A., Ali S.M., Sabatini D.M. Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 2005, 307:1098-1101.
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 62
    • 70350418625 scopus 로고    scopus 로고
    • MTOR signaling at a glance
    • Laplante M., Sabatini D.M. mTOR signaling at a glance. J. Cell Sci. 2009, 122:3589-3594.
    • (2009) J. Cell Sci. , vol.122 , pp. 3589-3594
    • Laplante, M.1    Sabatini, D.M.2
  • 63
    • 67349217986 scopus 로고    scopus 로고
    • Molecular mechanisms of mTOR-mediated translational control
    • Ma X.M., Blenis J. Molecular mechanisms of mTOR-mediated translational control. Nat. Rev. Mol. Cell. Biol. 2009, 10:307-318.
    • (2009) Nat. Rev. Mol. Cell. Biol. , vol.10 , pp. 307-318
    • Ma, X.M.1    Blenis, J.2
  • 65
    • 33947538050 scopus 로고    scopus 로고
    • Rapamycin induces feedback activation of Akt signaling through an IGF-1R-dependent mechanism
    • Wan X., Harkavy B., Shen N., Grohar P., Helman L.J. Rapamycin induces feedback activation of Akt signaling through an IGF-1R-dependent mechanism. Oncogene 2007, 26:1932-1940.
    • (2007) Oncogene , vol.26 , pp. 1932-1940
    • Wan, X.1    Harkavy, B.2    Shen, N.3    Grohar, P.4    Helman, L.J.5
  • 66
    • 54749095517 scopus 로고    scopus 로고
    • Enhancing mammalian target of rapamycin (mTOR)-targeted cancer therapy by preventing mTOR/raptor inhibition-initiated, mTOR/rictor-independent Akt activation
    • Wang X., Yue P., Kim Y.A., Fu H., Khuri F.R., Sun S.Y. Enhancing mammalian target of rapamycin (mTOR)-targeted cancer therapy by preventing mTOR/raptor inhibition-initiated, mTOR/rictor-independent Akt activation. Cancer Res. 2008, 68:7409-7418.
    • (2008) Cancer Res. , vol.68 , pp. 7409-7418
    • Wang, X.1    Yue, P.2    Kim, Y.A.3    Fu, H.4    Khuri, F.R.5    Sun, S.Y.6
  • 68
    • 27644534999 scopus 로고    scopus 로고
    • Mammalian target of rapamycin inhibitors activate the AKT kinase in multiple myeloma cells by up-regulating the insulin-like growth factor receptor/insulin receptor substrate-1/phosphatidylinositol 3-kinase cascade
    • Shi Y., Yan H., Frost P., Gera J., Lichtenstein A. Mammalian target of rapamycin inhibitors activate the AKT kinase in multiple myeloma cells by up-regulating the insulin-like growth factor receptor/insulin receptor substrate-1/phosphatidylinositol 3-kinase cascade. Mol. Cancer Ther. 2005, 4:1533-1540.
    • (2005) Mol. Cancer Ther. , vol.4 , pp. 1533-1540
    • Shi, Y.1    Yan, H.2    Frost, P.3    Gera, J.4    Lichtenstein, A.5
  • 69
    • 77950371095 scopus 로고    scopus 로고
    • Implication of RICTOR in the mTOR inhibitor-mediated induction of insulin-like growth factor-I receptor (IGF-IR) and human epidermal growth factor receptor-2 (Her2) expression in gastrointestinal cancer cells, Biochim Biophys Acta 1803 435-442
    • S.A. Lang, C. Hackl, C. Moser, S. Fichtner-Feigl, G.E. Koehl, H.J. Schlitt, E.K. Geissler, O. Stoeltzing, Implication of RICTOR in the mTOR inhibitor-mediated induction of insulin-like growth factor-I receptor (IGF-IR) and human epidermal growth factor receptor-2 (Her2) expression in gastrointestinal cancer cells, Biochim Biophys Acta 1803 (2010) 435-442.
    • (2010)
    • Lang, S.A.1    Hackl, C.2    Moser, C.3    Fichtner-Feigl, S.4    Koehl, G.E.5    Schlitt, H.J.6    Geissler, E.K.7    Stoeltzing, O.8
  • 70
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: navigating downstream
    • Manning B.D., Cantley L.C. AKT/PKB signaling: navigating downstream. Cell 2007, 129:1261-1274.
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 71
    • 51349098887 scopus 로고    scopus 로고
    • Cotargeting survival signaling pathways in cancer
    • Grant S. Cotargeting survival signaling pathways in cancer. J. Clin. Invest. 2008, 118:3003-3006.
    • (2008) J. Clin. Invest. , vol.118 , pp. 3003-3006
    • Grant, S.1


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