메뉴 건너뛰기




Volumn 54, Issue 1, 2003, Pages 371-389

Emmprin (CD147), a cell surface regulator of matrix metalloproteinase production and function

Author keywords

[No Author keywords available]

Indexed keywords

BSG PROTEIN, HUMAN; CD147 ANTIGEN; LEUKOCYTE ANTIGEN; MATRIX METALLOPROTEINASE; MEMBRANE PROTEIN; TUMOR ANTIGEN;

EID: 0642277903     PISSN: 00702153     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0070-2153(03)54015-7     Document Type: Review
Times cited : (163)

References (100)
  • 1
    • 0029896682 scopus 로고    scopus 로고
    • Expression and function of matrix metalloproteinases and their inhibitors at the maternal-embryonic boundary during mouse embryo implantation
    • Alexander, C. M., Hansell, E. J., Behrendtsen, O., Flannery, M. L., Kishnani, N. S., Hawkes, S. P., and Werb, Z. (1996). Expression and function of matrix metalloproteinases and their inhibitors at the maternal-embryonic boundary during mouse embryo implantation. Development 122, 1723-1736.
    • (1996) Development , vol.122 , pp. 1723-1736
    • Alexander, C.M.1    Hansell, E.J.2    Behrendtsen, O.3    Flannery, M.L.4    Kishnani, N.S.5    Hawkes, S.P.6    Werb, Z.7
  • 2
    • 0024825053 scopus 로고
    • Cloning of cDNA for a novel mouse membrane glycoprotein (gp42): shared identity to histocompatibility antigens, immunoglobulins and neural-cell adhesion molecules
    • Altruda, F., Cervella, P., Gaeta, M. L., Daniele, A., Giancotti, F., Tarone, G., Stefanuto, G., and Silengo, L. (1989). Cloning of cDNA for a novel mouse membrane glycoprotein (gp42): shared identity to histocompatibility antigens, immunoglobulins and neural-cell adhesion molecules. Gene 85, 445-451.
    • (1989) Gene , vol.85 , pp. 445-451
    • Altruda, F.1    Cervella, P.2    Gaeta, M.L.3    Daniele, A.4    Giancotti, F.5    Tarone, G.6    Stefanuto, G.7    Silengo, L.8
  • 3
    • 0030663733 scopus 로고    scopus 로고
    • Generation of monoclonal antibodies to integrin-associated proteins. Evidence that alpha3beta1 complexes with EMMPRIN/basigin/OX47/M6
    • Berditchevski, F., Chang, S., Bodorova, J., and Hemler, M. E. (1997). Generation of monoclonal antibodies to integrin-associated proteins. Evidence that alpha3beta1 complexes with EMMPRIN/basigin/OX47/M6. J. Biol. Chem 272, 29174-29180.
    • (1997) J. Biol. Chem , vol.272 , pp. 29174-29180
    • Berditchevski, F.1    Chang, S.2    Bodorova, J.3    Hemler, M.E.4
  • 4
    • 0020395961 scopus 로고
    • Tumor cell stimulation of collagenase production by fibroblasts
    • Biswas, C. (1982). Tumor cell stimulation of collagenase production by fibroblasts. Biochem. Biophys. Res. Commun 109, 1026-1034.
    • (1982) Biochem. Biophys. Res. Commun , vol.109 , pp. 1026-1034
    • Biswas, C.1
  • 5
    • 0021127113 scopus 로고
    • Collagenase stimulation in cocultures of human fibroblasts and human tumor cells
    • Biswas, C. (1984). Collagenase stimulation in cocultures of human fibroblasts and human tumor cells. Cancer Lett 24, 201-207.
    • (1984) Cancer Lett , vol.24 , pp. 201-207
    • Biswas, C.1
  • 6
    • 0023444008 scopus 로고
    • Membrane association of collagenase stimulatory factor(s) from B-16 melanoma cells
    • Biswas, C., and Nugent, M. A. (1987). Membrane association of collagenase stimulatory factor(s) from B-16 melanoma cells. J. Cell. Biochem 35, 247-258.
    • (1987) J. Cell. Biochem , vol.35 , pp. 247-258
    • Biswas, C.1    Nugent, M.A.2
  • 7
    • 0028795147 scopus 로고
    • The human tumor cell-derived collagenase stimulatory factor (renamed EMMPRIN) is a member of the immunoglobulin superfamily
    • Biswas, C., Zhang, Y., DeCastro, R., Guo, H., Nakamura, T., Kataoka, H., and Nabeshima, K. (1995). The human tumor cell-derived collagenase stimulatory factor (renamed EMMPRIN) is a member of the immunoglobulin superfamily. Cancer Res 55, 434-439.
    • (1995) Cancer Res , vol.55 , pp. 434-439
    • Biswas, C.1    Zhang, Y.2    DeCastro, R.3    Guo, H.4    Nakamura, T.5    Kataoka, H.6    Nabeshima, K.7
  • 9
    • 0028291794 scopus 로고
    • Localization of the 92 kd gelatinase mRNA in squamous cell and adenocarcinomas of the lung using in situ hybridization
    • Canete-Soler, R., Litzky, L., Lubensky, I., and Muschel, R. J. (1994). Localization of the 92 kd gelatinase mRNA in squamous cell and adenocarcinomas of the lung using in situ hybridization. Am. J. Pathol 144, 518-527.
    • (1994) Am. J. Pathol , vol.144 , pp. 518-527
    • Canete-Soler, R.1    Litzky, L.2    Lubensky, I.3    Muschel, R.J.4
  • 11
    • 0032714763 scopus 로고    scopus 로고
    • Expression of the extracellular matrix metalloproteinase inducer (EMMPRIN) and the matrix metalloproteinase-2 in bronchopulmonary and breast lesions
    • Caudroy, S., Polette, M., Tournier, J. M., Burlet, H., Toole, B., Zucker, S., and Birembaut, P. (1999). Expression of the extracellular matrix metalloproteinase inducer (EMMPRIN) and the matrix metalloproteinase-2 in bronchopulmonary and breast lesions. J. Histochem. Cytochem 47, 1575-1580.
    • (1999) J. Histochem. Cytochem , vol.47 , pp. 1575-1580
    • Caudroy, S.1    Polette, M.2    Tournier, J.M.3    Burlet, H.4    Toole, B.5    Zucker, S.6    Birembaut, P.7
  • 12
    • 0035880225 scopus 로고    scopus 로고
    • The functional interactions between CD98, beta1-integrins, and CD147 in the induction of U937 homotypic aggregation
    • Cho, J. Y., Fox, D. A., Horejsi, V., Sagawa, K., Skubitz, K. M., Katz, D. R., and Chain, B. (2001). The functional interactions between CD98, beta1-integrins, and CD147 in the induction of U937 homotypic aggregation. Blood 98, 374-382.
    • (2001) Blood , vol.98 , pp. 374-382
    • Cho, J.Y.1    Fox, D.A.2    Horejsi, V.3    Sagawa, K.4    Skubitz, K.M.5    Katz, D.R.6    Chain, B.7
  • 15
    • 0033998456 scopus 로고    scopus 로고
    • Gelatinase A, membrane type 1 matrix metalloproteinase, and extracellular matrix metalloproteinase inducer mRNA expression: correlation with invasive growth of breast cancer
    • Dalberg, K., Eriksson, E., Enberg, U., Kjellman, M., and Backdahl, M. (2000). Gelatinase A, membrane type 1 matrix metalloproteinase, and extracellular matrix metalloproteinase inducer mRNA expression: correlation with invasive growth of breast cancer. World J. Surg 24, 334-340.
    • (2000) World J. Surg , vol.24 , pp. 334-340
    • Dalberg, K.1    Eriksson, E.2    Enberg, U.3    Kjellman, M.4    Backdahl, M.5
  • 16
    • 0029888651 scopus 로고    scopus 로고
    • Human keratinocytes express EMMPRIN, an extracellular matrix metalloproteinase inducer
    • DeCastro, R., Zhang, Y., Guo, H., Kataoka, H., Gordon, M. K., Toole, B., and Biswas, G. (1996). Human keratinocytes express EMMPRIN, an extracellular matrix metalloproteinase inducer. J. Invest. Dermatol 106, 1260-1265.
    • (1996) J. Invest. Dermatol , vol.106 , pp. 1260-1265
    • DeCastro, R.1    Zhang, Y.2    Guo, H.3    Kataoka, H.4    Gordon, M.K.5    Toole, B.6    Biswas, G.7
  • 17
    • 0034123653 scopus 로고    scopus 로고
    • Interactions between tumour cells and stromal cells and proteolytic modification of the extracellular matrix by metalloproteinases in cancer
    • DeClerck, Y. A. (2000). Interactions between tumour cells and stromal cells and proteolytic modification of the extracellular matrix by metalloproteinases in cancer. Eur. J. Cancer 36, 1258-1268.
    • (2000) Eur. J. Cancer , vol.36 , pp. 1258-1268
    • DeClerck, Y.A.1
  • 19
    • 0024386474 scopus 로고
    • Monoclonal antibody preparation and purification of a tumor cell collagenase-stimulatory factor
    • Ellis, S. M., Nabeshima, K., and Biswas, C. (1989). Monoclonal antibody preparation and purification of a tumor cell collagenase-stimulatory factor. Cancer Res 49, 3385-3391.
    • (1989) Cancer Res , vol.49 , pp. 3385-3391
    • Ellis, S.M.1    Nabeshima, K.2    Biswas, C.3
  • 20
    • 0027199009 scopus 로고
    • 5A11 antigen is a cell recognition molecule which is involved in neuronal-glial interactions in avian neural retina
    • Fadool, J. M., and Linser, P. J. (1993). 5A11 antigen is a cell recognition molecule which is involved in neuronal-glial interactions in avian neural retina. Dev. Dynam 196, 252-262.
    • (1993) Dev. Dynam , vol.196 , pp. 252-262
    • Fadool, J.M.1    Linser, P.J.2
  • 21
    • 0030569545 scopus 로고    scopus 로고
    • Evidence for the formation of multimeric forms of the 5A11/HT7 antigen
    • Fadool, J. M., and Linser, P. J. (1996). Evidence for the formation of multimeric forms of the 5A11/HT7 antigen. Biochem. Biophys. Res. Commun 229, 280-286.
    • (1996) Biochem. Biophys. Res. Commun , vol.229 , pp. 280-286
    • Fadool, J.M.1    Linser, P.J.2
  • 22
    • 0035198816 scopus 로고    scopus 로고
    • Ventilator-induced lung injury upregulates and activates gelatinases and EMMPRIN: attenuation by the synthetic matrix metalloproteinase inhibitor, Prinomastat (AG3340)
    • Foda, H. D., Rollo, E. E., Drews, M., Conner, C., Appelt, K., Shalinsky, D. R., and Zucker, S. (2001). Ventilator-induced lung injury upregulates and activates gelatinases and EMMPRIN: attenuation by the synthetic matrix metalloproteinase inhibitor, Prinomastat (AG3340). Am. J. Respir. Cell. Mol. Biol 25, 717-724.
    • (2001) Am. J. Respir. Cell. Mol. Biol , vol.25 , pp. 717-724
    • Foda, H.D.1    Rollo, E.E.2    Drews, M.3    Conner, C.4    Appelt, K.5    Shalinsky, D.R.6    Zucker, S.7
  • 23
    • 0025971638 scopus 로고
    • The MRC OX-47 antigen is a member of the immunoglobulin superfamily with an unusual transmembrane sequence
    • Fossum, S., Mallett, S., and Barclay, A. N. (1991). The MRC OX-47 antigen is a member of the immunoglobulin superfamily with an unusual transmembrane sequence. Eur. J. Immunol 21, 671-679.
    • (1991) Eur. J. Immunol , vol.21 , pp. 671-679
    • Fossum, S.1    Mallett, S.2    Barclay, A.N.3
  • 24
    • 0034652586 scopus 로고    scopus 로고
    • EMMPRIN (CD147), an inducer of matrix metalloproteinase synthesis, also binds interstitial collagenase to the tumor cell surface
    • Guo, H., Li, R., Zucker, S., and Toole, B. P. (2000). EMMPRIN (CD147), an inducer of matrix metalloproteinase synthesis, also binds interstitial collagenase to the tumor cell surface. Cancer Res 60, 888-891.
    • (2000) Cancer Res , vol.60 , pp. 888-891
    • Guo, H.1    Li, R.2    Zucker, S.3    Toole, B.P.4
  • 25
    • 0032487394 scopus 로고    scopus 로고
    • Characterization of the gene for human EMMPRIN, a tumor cell surface inducer of matrix metalloproteinases
    • Guo, H., Majmudar, G., Jensen, T. C., Biswas, C., Toole, B. P., and Gordon, M. K. (1998). Characterization of the gene for human EMMPRIN, a tumor cell surface inducer of matrix metalloproteinases. Gene 220, 99-108.
    • (1998) Gene , vol.220 , pp. 99-108
    • Guo, H.1    Majmudar, G.2    Jensen, T.C.3    Biswas, C.4    Toole, B.P.5    Gordon, M.K.6
  • 26
    • 0031036521 scopus 로고    scopus 로고
    • Stimulation of matrix metalloproteinase production by recombinant extracellular matrix metalloproteinase inducer from transfected Chinese hamster ovary cells
    • Guo, H., Zucker, S., Gordon, M. K., Toole, B. P., and Biswas, C. (1997). Stimulation of matrix metalloproteinase production by recombinant extracellular matrix metalloproteinase inducer from transfected Chinese hamster ovary cells. J. Biol. Chem 272, 24-27.
    • (1997) J. Biol. Chem , vol.272 , pp. 24-27
    • Guo, H.1    Zucker, S.2    Gordon, M.K.3    Toole, B.P.4    Biswas, C.5
  • 27
    • 0034050009 scopus 로고    scopus 로고
    • Annexin II and regulation of cell surface fibrinolysis
    • Hajjar, K. A., and Acharya, S. S. (2000). Annexin II and regulation of cell surface fibrinolysis. Ann. NY Acad. Sci 902, 265-271.
    • (2000) Ann. NY Acad. Sci , vol.902 , pp. 265-271
    • Hajjar, K.A.1    Acharya, S.S.2
  • 28
    • 0029788890 scopus 로고    scopus 로고
    • Interaction of the fibrinolytic receptor, annexin II, with the endothelial cell surface. Essential role of endonexin repeat 2
    • Hajjar, K. A., Guevara, C. A., Lev, E., Dowling, K., and Chacko, J. (1996). Interaction of the fibrinolytic receptor, annexin II, with the endothelial cell surface. Essential role of endonexin repeat 2. J. Biol. Chem 271, 21652-21659.
    • (1996) J. Biol. Chem , vol.271 , pp. 21652-21659
    • Hajjar, K.A.1    Guevara, C.A.2    Lev, E.3    Dowling, K.4    Chacko, J.5
  • 29
    • 84940173052 scopus 로고    scopus 로고
    • Mechanical stretch induces MMP-2 release and activation in lung endothelium: role of emmprin
    • in press
    • Haseneen, N. A., Vaday, G. G., Zucker, S., and Foda, H. D. (2002). Mechanical stretch induces MMP-2 release and activation in lung endothelium: role of emmprin. Am. J. Physiol., in press.
    • (2002) Am. J. Physiol.
    • Haseneen, N.A.1    Vaday, G.G.2    Zucker, S.3    Foda, H.D.4
  • 30
    • 0029946569 scopus 로고    scopus 로고
    • Expression of most matrix metalloproteinase family members in breast cancer represents a tumor-induced host response
    • Heppner, K. J., Matrisian, L. M., Jensen, R. A., and Rodgers, W. H. (1996). Expression of most matrix metalloproteinase family members in breast cancer represents a tumor-induced host response. Am. J. Pathol 149, 273-282.
    • (1996) Am. J. Pathol , vol.149 , pp. 273-282
    • Heppner, K.J.1    Matrisian, L.M.2    Jensen, R.A.3    Rodgers, W.H.4
  • 31
    • 0030056669 scopus 로고    scopus 로고
    • Induction of matrix metalloproteinase 9 expression in breast carcinoma cells by a soluble factor from fibroblasts
    • Himelstein, B. P., and Muschel, R. J. (1996). Induction of matrix metalloproteinase 9 expression in breast carcinoma cells by a soluble factor from fibroblasts. Clin. Exp. Metastasis 14, 197-208.
    • (1996) Clin. Exp. Metastasis , vol.14 , pp. 197-208
    • Himelstein, B.P.1    Muschel, R.J.2
  • 32
    • 0028326346 scopus 로고
    • Induction of fibroblast 92 kDa gelatinase/type IV collagenase expression by direct contact with metastatic tumor cells
    • Himelstein, B. P., Canete-Soler, R., Bernhard, E. J., and Muschel, R. J. (1994). Induction of fibroblast 92 kDa gelatinase/type IV collagenase expression by direct contact with metastatic tumor cells. J. Cell Sci 107, 477-486.
    • (1994) J. Cell Sci , vol.107 , pp. 477-486
    • Himelstein, B.P.1    Canete-Soler, R.2    Bernhard, E.J.3    Muschel, R.J.4
  • 34
    • 0028263584 scopus 로고
    • Autocrine factor enhancing the secretion of M(r) 95,000 gelatinase (matrix metalloproteinase 9) in serum-free medium conditioned with murine metastatic colon carcinoma cells
    • Hyuga, S., Nishikawa, Y., Sakata, K., Tanaka, H., Yamagata, S., Sugita, K., Saga, S., Matsuyama, M., and Shimizu, S. (1994). Autocrine factor enhancing the secretion of M(r) 95,000 gelatinase (matrix metalloproteinase 9) in serum-free medium conditioned with murine metastatic colon carcinoma cells. Cancer Res 54, 3611-3616.
    • (1994) Cancer Res , vol.54 , pp. 3611-3616
    • Hyuga, S.1    Nishikawa, Y.2    Sakata, K.3    Tanaka, H.4    Yamagata, S.5    Sugita, K.6    Saga, S.7    Matsuyama, M.8    Shimizu, S.9
  • 35
    • 0036525468 scopus 로고    scopus 로고
    • Gene-expression profile of collagen-induced arthritis
    • Ibrahim, S. M., Koczan, D., and Thiesen, H. J. (2002). Gene-expression profile of collagen-induced arthritis. J. Autoimmun 18, 159-167.
    • (2002) J. Autoimmun , vol.18 , pp. 159-167
    • Ibrahim, S.M.1    Koczan, D.2    Thiesen, H.J.3
  • 38
    • 0032031861 scopus 로고    scopus 로고
    • Reduced angiogenesis and tumor progression in gelatinase A-deficient mice
    • Itoh, T., Tanioka, M., Yoshida, H., Yoshioka, T., Nishimoto, H., and Itohara, S. (1998). Reduced angiogenesis and tumor progression in gelatinase A-deficient mice. Cancer Res 58, 1048-1051.
    • (1998) Cancer Res , vol.58 , pp. 1048-1051
    • Itoh, T.1    Tanioka, M.2    Yoshida, H.3    Yoshioka, T.4    Nishimoto, H.5    Itohara, S.6
  • 39
    • 0035966011 scopus 로고    scopus 로고
    • Neuritogenesis and the nerve growth factor-induced differentiation of PC-12 cells requires annexin II-mediated plasmin generation
    • Jacovina, A. T., Zhong, F., Khazanova, E., Lev, E., Deora, A. B., and Hajjar, K. A. (2001). Neuritogenesis and the nerve growth factor-induced differentiation of PC-12 cells requires annexin II-mediated plasmin generation. J. Biol. Chem 276, 49350-49358.
    • (2001) J. Biol. Chem , vol.276 , pp. 49350-49358
    • Jacovina, A.T.1    Zhong, F.2    Khazanova, E.3    Lev, E.4    Deora, A.B.5    Hajjar, K.A.6
  • 40
    • 0035861597 scopus 로고    scopus 로고
    • The involvement of HAb18G/CD147 in regulation of store-operated calcium entry and metastasis of human hepatoma cells
    • Jiang, J. L., Zhou, Q., Yu, M. K., Ho, L. S., Chen, Z. N., and Chan, H. C. (2001). The involvement of HAb18G/CD147 in regulation of store-operated calcium entry and metastasis of human hepatoma cells. J. Biol. Chem 276, 46870-46877.
    • (2001) J. Biol. Chem , vol.276 , pp. 46870-46877
    • Jiang, J.L.1    Zhou, Q.2    Yu, M.K.3    Ho, L.S.4    Chen, Z.N.5    Chan, H.C.6
  • 41
    • 0031719897 scopus 로고    scopus 로고
    • Cancer invasion and tissue remodeling: common themes in proteolytic matrix degradation
    • Johnsen, M., Lund, L. R., Romer, J., Almholt, K., and Dano, K. (1998). Cancer invasion and tissue remodeling: common themes in proteolytic matrix degradation. Curr. Opin. Cell Biol 10, 667-671.
    • (1998) Curr. Opin. Cell Biol , vol.10 , pp. 667-671
    • Johnsen, M.1    Lund, L.R.2    Romer, J.3    Almholt, K.4    Dano, K.5
  • 42
    • 0036605095 scopus 로고    scopus 로고
    • Basigin (CD147) is expressed on melanoma cells and induces tumor cell invasion by stimulating production of matrix metalloproteinases by fibroblasts
    • Kanekura, T., Chen, X., and Kanzaki, T. (2002). Basigin (CD147) is expressed on melanoma cells and induces tumor cell invasion by stimulating production of matrix metalloproteinases by fibroblasts. Int. J. Cancer 99, 520-528.
    • (2002) Int. J. Cancer , vol.99 , pp. 520-528
    • Kanekura, T.1    Chen, X.2    Kanzaki, T.3
  • 43
    • 0026659128 scopus 로고
    • Human leukocyte activation antigen M6, a member of the Ig superfamily, is the species homologue of rat OX-47, mouse basigin, and chicken HT7 molecule
    • Kasinrerk, W., Fiebiger, E., Stefanova, I., Baumruker, T., Knapp, W., and Stockinger, H. (1992). Human leukocyte activation antigen M6, a member of the Ig superfamily, is the species homologue of rat OX-47, mouse basigin, and chicken HT7 molecule. J. Immunol 149, 847-854.
    • (1992) J. Immunol , vol.149 , pp. 847-854
    • Kasinrerk, W.1    Fiebiger, E.2    Stefanova, I.3    Baumruker, T.4    Knapp, W.5    Stockinger, H.6
  • 44
    • 0032956758 scopus 로고    scopus 로고
    • CD147 monoclonal antibodies induce homotypic cell aggregation of monocytic cell line U937 via LFA-1/ICAM-1 pathway
    • Kasinrerk, W., Tokrasinwit, N., and Phunpae, P. (1999). CD147 monoclonal antibodies induce homotypic cell aggregation of monocytic cell line U937 via LFA-1/ICAM-1 pathway. Immunology 96, 184-192.
    • (1999) Immunology , vol.96 , pp. 184-192
    • Kasinrerk, W.1    Tokrasinwit, N.2    Phunpae, P.3
  • 45
    • 0027328322 scopus 로고
    • Tumor cell-derived collagenase-stimulatory factor increases expression of interstitial collagenase, stromelysin, and 72-kDa gelatinase
    • Kataoka, H., DeCastro, R., Zucker, S., and Biswas, C. (1993). Tumor cell-derived collagenase-stimulatory factor increases expression of interstitial collagenase, stromelysin, and 72-kDa gelatinase. Cancer Res 53, 3154-3158.
    • (1993) Cancer Res , vol.53 , pp. 3154-3158
    • Kataoka, H.1    DeCastro, R.2    Zucker, S.3    Biswas, C.4
  • 46
    • 0034254638 scopus 로고    scopus 로고
    • CD147 is tightly associated with lactate transporters MCT1 and MCT4 and facilitates their cell surface expression
    • Kirk, P., Wilson, M. C., Heddle, C., Brown, M. H., Barclay, A. N., and Halestrap, A. P. (2000). CD147 is tightly associated with lactate transporters MCT1 and MCT4 and facilitates their cell surface expression. EMBO J 19, 3896-3904.
    • (2000) EMBO J , vol.19 , pp. 3896-3904
    • Kirk, P.1    Wilson, M.C.2    Heddle, C.3    Brown, M.H.4    Barclay, A.N.5    Halestrap, A.P.6
  • 48
    • 0034351580 scopus 로고    scopus 로고
    • Fibroblast biology. Signals targeting the synovial fibroblast in arthritis
    • Konttinen, Y. T., Li, T. F., Hukkanen, M., Ma, J., Xu, J. W., and Virtanen, I. (2000a). Fibroblast biology. Signals targeting the synovial fibroblast in arthritis. Arthritis Res 2, 348-355.
    • (2000) Arthritis Res , vol.2 , pp. 348-355
    • Konttinen, Y.T.1    Li, T.F.2    Hukkanen, M.3    Ma, J.4    Xu, J.W.5    Virtanen, I.6
  • 50
    • 0031012891 scopus 로고    scopus 로고
    • Synaptic membrane glycoproteins gp65 and gp55 are new members of the immunoglobulin superfamily
    • Langnaese, K., Beesley, P. W., and Gundelfinger, E. D. (1997). Synaptic membrane glycoproteins gp65 and gp55 are new members of the immunoglobulin superfamily. J. Biol. Chem 272, 821-827.
    • (1997) J. Biol. Chem , vol.272 , pp. 821-827
    • Langnaese, K.1    Beesley, P.W.2    Gundelfinger, E.D.3
  • 51
    • 0028980084 scopus 로고
    • Induction of Mr 92,000 type IV collagenase expression in a squamous cell carcinoma cell line by fibroblasts
    • Lengyel, E., Gum, R., Juarez, J., Clayman, G., Seiki, M., Sato, H., and Boyd, D. (1995). Induction of Mr 92,000 type IV collagenase expression in a squamous cell carcinoma cell line by fibroblasts. Cancer Res 55, 963-967.
    • (1995) Cancer Res , vol.55 , pp. 963-967
    • Lengyel, E.1    Gum, R.2    Juarez, J.3    Clayman, G.4    Seiki, M.5    Sato, H.6    Boyd, D.7
  • 52
    • 0035124589 scopus 로고    scopus 로고
    • Basigin (murine EMMPRIN) stimulates matrix metalloproteinase production by fibroblasts
    • Li, R., Huang, L., Guo, H., and Toole, B. P. (2001). Basigin (murine EMMPRIN) stimulates matrix metalloproteinase production by fibroblasts. J. Cell Physiol 186, 371-379.
    • (2001) J. Cell Physiol , vol.186 , pp. 371-379
    • Li, R.1    Huang, L.2    Guo, H.3    Toole, B.P.4
  • 53
    • 0034115114 scopus 로고    scopus 로고
    • Interplay of matrix metalloproteinases, tissue inhibitors of metalloproteinases and their regulators in cardiac matrix remodeling
    • Li, Y. Y., McTiernan, C. F., and Feldman, A. M. (2000). Interplay of matrix metalloproteinases, tissue inhibitors of metalloproteinases and their regulators in cardiac matrix remodeling. Cardiovasc. Res 46, 214-224.
    • (2000) Cardiovasc. Res , vol.46 , pp. 214-224
    • Li, Y.Y.1    McTiernan, C.F.2    Feldman, A.M.3
  • 54
    • 0037045423 scopus 로고    scopus 로고
    • Characterization of the promoter of human extracellular matrix metalloproteinase inducer (EMMPRIN)
    • Liang, L., Major, T., and Bocan, T. (2002). Characterization of the promoter of human extracellular matrix metalloproteinase inducer (EMMPRIN). Gene 282, 75-86.
    • (2002) Gene , vol.282 , pp. 75-86
    • Liang, L.1    Major, T.2    Bocan, T.3
  • 55
    • 0032443309 scopus 로고    scopus 로고
    • Tumor-derived EMMPRIN (extracellular matrix metalloproteinase inducer) stimulates collagenase transcription through MAPK p38
    • Lim, M., Martinez, T., Jablons, D., Cameron, R., Guo, H., Toole, B., Li, J. D., and Basbaum, C. (1998). Tumor-derived EMMPRIN (extracellular matrix metalloproteinase inducer) stimulates collagenase transcription through MAPK p38. FEBS Lett 441, 88-92.
    • (1998) FEBS Lett , vol.441 , pp. 88-92
    • Lim, M.1    Martinez, T.2    Jablons, D.3    Cameron, R.4    Guo, H.5    Toole, B.6    Li, J.D.7    Basbaum, C.8
  • 56
    • 0034725119 scopus 로고    scopus 로고
    • Human procathepsin B interacts with the annexin II tetramer on the surface of tumor cells
    • Mai, J., Finley, R. L. Jr., Waisman, D. M., and Sloane, B. F. (2000). Human procathepsin B interacts with the annexin II tetramer on the surface of tumor cells. J. Biol. Chem 275, 12806-12812.
    • (2000) J. Biol. Chem , vol.275 , pp. 12806-12812
    • Mai, J.1    Finley, R.L.Jr.2    Waisman, D.M.3    Sloane, B.F.4
  • 57
    • 0031877495 scopus 로고    scopus 로고
    • Apical polarity of N-CAM and EMMPRIN in retinal pigment epithelium resulting from suppression of basolateral signal recognition
    • Marmorstein, A. D., Gan, Y. C., Bonilha, V. L., Finnemann, S. C., Csaky, K. G., and Rodriguez-Boulan, E. (1998). Apical polarity of N-CAM and EMMPRIN in retinal pigment epithelium resulting from suppression of basolateral signal recognition. J. Cell. Biol 142, 697-710.
    • (1998) J. Cell. Biol , vol.142 , pp. 697-710
    • Marmorstein, A.D.1    Gan, Y.C.2    Bonilha, V.L.3    Finnemann, S.C.4    Csaky, K.G.5    Rodriguez-Boulan, E.6
  • 59
    • 0028874356 scopus 로고
    • Structure of the mouse basigin gene, a unique member of the immunoglobulin superfamily
    • Tokyo
    • Miyauchi, T., Jimma, F., Igakura, T., Yu, S., Ozawa, M., and Muramatsu, T. (1995). Structure of the mouse basigin gene, a unique member of the immunoglobulin superfamily. J. Biochem. (Tokyo) 118, 717-724.
    • (1995) J. Biochem , vol.118 , pp. 717-724
    • Miyauchi, T.1    Jimma, F.2    Igakura, T.3    Yu, S.4    Ozawa, M.5    Muramatsu, T.6
  • 60
    • 0025129356 scopus 로고
    • Basigin, a new, broadly distributed member of the immunoglobulin superfamily, has strong homology with both the immunoglobulin V domain and the beta-chain of major histocompatibility complex class II antigen
    • Tokyo
    • Miyauchi, T., Kanekura, T., Yamaoka, A., Ozawa, M., Miyazawa, S., and Muramatsu, T. (1990). Basigin, a new, broadly distributed member of the immunoglobulin superfamily, has strong homology with both the immunoglobulin V domain and the beta-chain of major histocompatibility complex class II antigen. J. Biochem (Tokyo) 107, 316-323.
    • (1990) J. Biochem , vol.107 , pp. 316-323
    • Miyauchi, T.1    Kanekura, T.2    Yamaoka, A.3    Ozawa, M.4    Miyazawa, S.5    Muramatsu, T.6
  • 61
    • 0025718981 scopus 로고
    • The basigin group of the immunoglobulin superfamily: complete conservation of a segment in and around transmembrane domains of human and mouse basigin and chicken HT7 antigen
    • Tokyo
    • Miyauchi, T., Masuzawa, Y., and Muramatsu, T. (1991). The basigin group of the immunoglobulin superfamily: complete conservation of a segment in and around transmembrane domains of human and mouse basigin and chicken HT7 antigen. J. Biochem (Tokyo) 110, 770-774.
    • (1991) J. Biochem , vol.110 , pp. 770-774
    • Miyauchi, T.1    Masuzawa, Y.2    Muramatsu, T.3
  • 62
    • 0027328798 scopus 로고
    • Enhanced expression of a tumor-cell-derived collagenase-stimulatory factor in urothelial carcinoma: its usefulness as a tumor marker for bladder cancers
    • Muraoka, K., Nabeshima, K., Murayama, T., Biswas, C., and Koono, M. (1993). Enhanced expression of a tumor-cell-derived collagenase-stimulatory factor in urothelial carcinoma: its usefulness as a tumor marker for bladder cancers. Int. J. Cancer 55, 19-26.
    • (1993) Int. J. Cancer , vol.55 , pp. 19-26
    • Muraoka, K.1    Nabeshima, K.2    Murayama, T.3    Biswas, C.4    Koono, M.5
  • 63
    • 0002423901 scopus 로고    scopus 로고
    • Activation and induction of collagenases
    • W. Hoeffler, Ed, R. G. Landes, Austin, TX
    • Nabeshima, K., Kataoka, H., Toole, B. P., and Koono, M. (1999). Activation and induction of collagenases. In "Collagenases" (W. Hoeffler, Ed.), pp. 91-113. R. G. Landes, Austin, TX.
    • (1999) Collagenases , pp. 91-113
    • Nabeshima, K.1    Kataoka, H.2    Toole, B.P.3    Koono, M.4
  • 64
    • 0026081069 scopus 로고
    • Partial sequencing and characterization of the tumor cell-derived collagenase stimulatory factor
    • Nabeshima, K., Lane, W. S., and Biswas, C. (1991). Partial sequencing and characterization of the tumor cell-derived collagenase stimulatory factor. Arch. Biochem. Biophys 285, 90-96.
    • (1991) Arch. Biochem. Biophys , vol.285 , pp. 90-96
    • Nabeshima, K.1    Lane, W.S.2    Biswas, C.3
  • 67
    • 0027389493 scopus 로고
    • Breaching the diffusion barrier that compartmentalizes the transmembrane glycoprotein CE9 to the posterior-tail plasma membrane domain of the rat spermatozoon
    • Nehme, C. L., Cesario, M. M., Myles, D. G., Koppel, D. E., and Bartles, J. R. (1993). Breaching the diffusion barrier that compartmentalizes the transmembrane glycoprotein CE9 to the posterior-tail plasma membrane domain of the rat spermatozoon. J. Cell Biol 120, 687-694.
    • (1993) J. Cell Biol , vol.120 , pp. 687-694
    • Nehme, C.L.1    Cesario, M.M.2    Myles, D.G.3    Koppel, D.E.4    Bartles, J.R.5
  • 68
    • 0029079786 scopus 로고
    • Distribution of the integral plasma membrane glycoprotein CE9 (MRC OX-47) among rat tissues and its induction by diverse stimuli of metabolic activation
    • Nehme, C. L., Fayos, B. E., and Bartles, J. R. (1995). Distribution of the integral plasma membrane glycoprotein CE9 (MRC OX-47) among rat tissues and its induction by diverse stimuli of metabolic activation. Biochem J 310, 693-698.
    • (1995) Biochem J , vol.310 , pp. 693-698
    • Nehme, C.L.1    Fayos, B.E.2    Bartles, J.R.3
  • 69
    • 0034770988 scopus 로고    scopus 로고
    • Retinal degeneration following failed photoreceptor maturation in 5A11/basigin null mice
    • Ochrietor, J. D., Moroz, T. M., Kadomatsu, K., Muramatsu, T., and Linser, P. J. (2001). Retinal degeneration following failed photoreceptor maturation in 5A11/basigin null mice. Exp. Eye Res. 72, 467-477.
    • (2001) Exp. Eye Res. , vol.72 , pp. 467-477
    • Ochrietor, J.D.1    Moroz, T.M.2    Kadomatsu, K.3    Muramatsu, T.4    Linser, P.J.5
  • 70
  • 72
    • 0024441086 scopus 로고
    • Coordinate increase in collagenase mRNA and enzyme levels in human fibroblasts treated with the tumor cell factor, TCSF
    • Prescott, J., Troccoli, N., and Biswas, C. (1989). Coordinate increase in collagenase mRNA and enzyme levels in human fibroblasts treated with the tumor cell factor, TCSF. Biochem. Int 19, 257-266.
    • (1989) Biochem. Int , vol.19 , pp. 257-266
    • Prescott, J.1    Troccoli, N.2    Biswas, C.3
  • 74
    • 0033851302 scopus 로고    scopus 로고
    • Expression of emmprin (CD147), a cell surface inducer of matrix metalloproteinases, in normal human brain and gliomas
    • Sameshima, T., Nabeshima, K., Toole, B. P., Yokogami, K., Okada, Y., Goya, T., Koono, M., and Wakisaka, S. (2000a). Expression of emmprin (CD147), a cell surface inducer of matrix metalloproteinases, in normal human brain and gliomas. Int. J. Cancer 88, 21-27.
    • (2000) Int. J. Cancer , vol.88 , pp. 21-27
    • Sameshima, T.1    Nabeshima, K.2    Toole, B.P.3    Yokogami, K.4    Okada, Y.5    Goya, T.6    Koono, M.7    Wakisaka, S.8
  • 75
    • 0034285090 scopus 로고    scopus 로고
    • Glioma cell extracellular matrix metalloproteinase inducer (EMMPRIN) (CD147) stimulates production of membrane-type matrix metalloproteinases and activated gelatinase A in co-cultures with brain-derived fibroblasts
    • Sameshima, T., Nabeshima, K., Toole, B. P., Yokogami, K., Okada, Y., Goya, T., Koono, M., and Wakisaka, S. (2000b). Glioma cell extracellular matrix metalloproteinase inducer (EMMPRIN) (CD147) stimulates production of membrane-type matrix metalloproteinases and activated gelatinase A in co-cultures with brain-derived fibroblasts. Cancer Lett 157, 177-184.
    • (2000) Cancer Lett , vol.157 , pp. 177-184
    • Sameshima, T.1    Nabeshima, K.2    Toole, B.P.3    Yokogami, K.4    Okada, Y.5    Goya, T.6    Koono, M.7    Wakisaka, S.8
  • 76
    • 0036119370 scopus 로고    scopus 로고
    • Behaviour of a sperm surface transmembrane glycoprotein basigin during epididymal maturation and its role in fertilization in mice
    • Saxena, D. K., Oh-Oka, T., Kadomatsu, K., Muramatsu, T., and Toshimori, K. (2002). Behaviour of a sperm surface transmembrane glycoprotein basigin during epididymal maturation and its role in fertilization in mice. Reproduction 123, 435-444.
    • (2002) Reproduction , vol.123 , pp. 435-444
    • Saxena, D.K.1    Oh-Oka, T.2    Kadomatsu, K.3    Muramatsu, T.4    Toshimori, K.5
  • 77
    • 0027604576 scopus 로고
    • The blood-brain barrier: morphology, molecules, and neurothelin
    • Schlosshauer, B. (1993). The blood-brain barrier: morphology, molecules, and neurothelin. Bioessays 15, 341-346.
    • (1993) Bioessays , vol.15 , pp. 341-346
    • Schlosshauer, B.1
  • 78
    • 0028818328 scopus 로고
    • Neurothelin: amino acid sequence, cell surface dynamics and actin colocalization
    • Schlosshauer, B., Bauch, H., and Frank, R. (1995). Neurothelin: amino acid sequence, cell surface dynamics and actin colocalization. Eur. J. Cell Biol 68, 159-166.
    • (1995) Eur. J. Cell Biol , vol.68 , pp. 159-166
    • Schlosshauer, B.1    Bauch, H.2    Frank, R.3
  • 79
    • 0030464272 scopus 로고    scopus 로고
    • Induction of fibroblast gelatinase B expression by direct contact with cell lines derived from primary tumor but not from metastases
    • Segain, J. P., Harb, J., Gregoire, M., Meflah, K., and Menanteau, J. (1996). Induction of fibroblast gelatinase B expression by direct contact with cell lines derived from primary tumor but not from metastases. Cancer Res 56, 5506-5512.
    • (1996) Cancer Res , vol.56 , pp. 5506-5512
    • Segain, J.P.1    Harb, J.2    Gregoire, M.3    Meflah, K.4    Menanteau, J.5
  • 80
    • 0031930324 scopus 로고    scopus 로고
    • Requirement for matrix metalloproteinase-9 (gelatinase B) expression in metastasis by murine prostate carcinoma
    • Sehgal, G., Hua, J., Bernhard, E. J., Sehgal, I., Thompson, T. C., and Muschel, R. J. (1998). Requirement for matrix metalloproteinase-9 (gelatinase B) expression in metastasis by murine prostate carcinoma. Am. J. Pathol 152, 591-596.
    • (1998) Am. J. Pathol , vol.152 , pp. 591-596
    • Sehgal, G.1    Hua, J.2    Bernhard, E.J.3    Sehgal, I.4    Thompson, T.C.5    Muschel, R.J.6
  • 81
    • 0026653792 scopus 로고
    • HT7, Neurothelin, Basigin, gp42 and OX-47-many names for one developmentally regulated immuno-globulin-like surface glycoprotein on blood-brain barrier endothelium, epithelial tissue barriers and neurons
    • Seulberger, H., Unger, C. M., and Risau, W. (1992). HT7, Neurothelin, Basigin, gp42 and OX-47-many names for one developmentally regulated immuno-globulin-like surface glycoprotein on blood-brain barrier endothelium, epithelial tissue barriers and neurons. Neurosci. Lett 140, 93-97.
    • (1992) Neurosci. Lett , vol.140 , pp. 93-97
    • Seulberger, H.1    Unger, C.M.2    Risau, W.3
  • 82
    • 0034685789 scopus 로고    scopus 로고
    • Dissection of protein linkage between keratins and pinin, a protein with dual location at desmosome-intermediate filament complex and in the nucleus
    • Shi, J., and Sugrue, S. P. (2000). Dissection of protein linkage between keratins and pinin, a protein with dual location at desmosome-intermediate filament complex and in the nucleus. J. Biol. Chem 275, 14910-14915.
    • (2000) J. Biol. Chem , vol.275 , pp. 14910-14915
    • Shi, J.1    Sugrue, S.P.2
  • 83
    • 0034642508 scopus 로고    scopus 로고
    • Characterization of the gene encoding pinin/DRS/memA and evidence for its potential tumor suppressor function
    • Shi, Y., Ouyang, P., and Sugrue, S. P. (2000). Characterization of the gene encoding pinin/DRS/memA and evidence for its potential tumor suppressor function. Oncogene 19, 289-297.
    • (2000) Oncogene , vol.19 , pp. 289-297
    • Shi, Y.1    Ouyang, P.2    Sugrue, S.P.3
  • 84
    • 0035811592 scopus 로고    scopus 로고
    • Change in gene expression subsequent to induction of Pnn/DRS/memA: increase in p21(cip1/waf1)
    • Shi, Y., Simmons, M. N., Seki, T., Oh, S. P., and Sugrue, S. P. (2001). Change in gene expression subsequent to induction of Pnn/DRS/memA: increase in p21(cip1/waf1). Oncogene 20, 4007-4018.
    • (2001) Oncogene , vol.20 , pp. 4007-4018
    • Shi, Y.1    Simmons, M.N.2    Seki, T.3    Oh, S.P.4    Sugrue, S.P.5
  • 86
    • 0028306295 scopus 로고
    • 72 KD and 92 KD type IV collagenase, type IV collagen, and laminin mRNAs in breast cancer: a study by in situ hybridization
    • Soini, Y., Hurskainen, T., Hoyhtya, M., Oikarinen, A., and Autio-Harmainen, H. (1994). 72 KD and 92 KD type IV collagenase, type IV collagen, and laminin mRNAs in breast cancer: a study by in situ hybridization. J. Histochem. Cytochem 42, 945-951.
    • (1994) J. Histochem. Cytochem , vol.42 , pp. 945-951
    • Soini, Y.1    Hurskainen, T.2    Hoyhtya, M.3    Oikarinen, A.4    Autio-Harmainen, H.5
  • 87
    • 0034680366 scopus 로고    scopus 로고
    • A matrix metalloproteinase induction/activation system exists in the human left ventricular myocardium and is upregulated in heart failure
    • Spinale, F. G., Coker, M. L., Heung, L. J., Bond, B. R., Gunasinghe, H. R., Etoh, T., Goldberg, A. T., Zellner, J. L., and Crumbley, A. J. (2000). A matrix metalloproteinase induction/activation system exists in the human left ventricular myocardium and is upregulated in heart failure. Circulation 102, 1944-1949.
    • (2000) Circulation , vol.102 , pp. 1944-1949
    • Spinale, F.G.1    Coker, M.L.2    Heung, L.J.3    Bond, B.R.4    Gunasinghe, H.R.5    Etoh, T.6    Goldberg, A.T.7    Zellner, J.L.8    Crumbley, A.J.9
  • 88
    • 0030611739 scopus 로고    scopus 로고
    • The Oka blood group antigen is a marker for the M6 leukocyte activation antigen, the human homolog of OX-47 antigen, basigin and neurothelin, an immunoglobulin superfamily molecule that is widely expressed in human cells and tissues
    • Spring, F. A., Holmes, C. H., Simpson, K. L., Mawby, W. J., Mattes, M. J., Okubo, Y., and Parsons, S. F. (1997). The Oka blood group antigen is a marker for the M6 leukocyte activation antigen, the human homolog of OX-47 antigen, basigin and neurothelin, an immunoglobulin superfamily molecule that is widely expressed in human cells and tissues. Eur. J. Immunol 27, 891-897.
    • (1997) Eur. J. Immunol , vol.27 , pp. 891-897
    • Spring, F.A.1    Holmes, C.H.2    Simpson, K.L.3    Mawby, W.J.4    Mattes, M.J.5    Okubo, Y.6    Parsons, S.F.7
  • 90
    • 0035266353 scopus 로고    scopus 로고
    • Regulation of MMP-1 and MMP-2 production through CD147/extracellular matrix metalloproteinase inducer interactions
    • Sun, J., and Hemler, M. E. (2001). Regulation of MMP-1 and MMP-2 production through CD147/extracellular matrix metalloproteinase inducer interactions. Cancer Res 61, 2276-2281.
    • (2001) Cancer Res , vol.61 , pp. 2276-2281
    • Sun, J.1    Hemler, M.E.2
  • 91
    • 0036166371 scopus 로고    scopus 로고
    • Expression of extracellular matrix metalloproteinase inducer and enhancement of the production of matrix metalloproteinases in rheumatoid arthritis
    • Tomita, T., Nakase, T., Kaneko, M., Shi, K., Takahi, K., Ochi, T., and Yoshikawa, H. (2002). Expression of extracellular matrix metalloproteinase inducer and enhancement of the production of matrix metalloproteinases in rheumatoid arthritis. Arthritis Rheum 46, 373-378.
    • (2002) Arthritis Rheum , vol.46 , pp. 373-378
    • Tomita, T.1    Nakase, T.2    Kaneko, M.3    Shi, K.4    Takahi, K.5    Ochi, T.6    Yoshikawa, H.7
  • 92
    • 0027436971 scopus 로고
    • Extracellular annexin II is associated with divalent cation-dependent tumor cell-endothelial cell adhesion of metastatic RAW117 large-cell lymphoma cells
    • Tressler, R. J., Updyke, T. V., Yeatman, T., and Nicolson, G. L. (1993). Extracellular annexin II is associated with divalent cation-dependent tumor cell-endothelial cell adhesion of metastatic RAW117 large-cell lymphoma cells. J. Cell. Biochem 53, 265-276.
    • (1993) J. Cell. Biochem , vol.53 , pp. 265-276
    • Tressler, R.J.1    Updyke, T.V.2    Yeatman, T.3    Nicolson, G.L.4
  • 93
    • 0030884405 scopus 로고    scopus 로고
    • Expression of gelatinase B and the extracellular matrix metalloproteinase inducer EMMPRIN in benign and malignant pigment cell lesions of the skin
    • van den Oord, J. J., Paemen, L., Opdenakker, G., and de Wolf-Peeters, C. (1997). Expression of gelatinase B and the extracellular matrix metalloproteinase inducer EMMPRIN in benign and malignant pigment cell lesions of the skin. Am. J. Pathol 151, 665-670.
    • (1997) Am. J. Pathol , vol.151 , pp. 665-670
    • Van Den Oord, J.J.1    Paemen, L.2    Opdenakker, G.3    de Wolf-Peeters, C.4
  • 94
    • 0033848986 scopus 로고    scopus 로고
    • Matrix metalloproteinases: effectors of development and normal physiology
    • Vu, T. H., and Werb, Z. (2000). Matrix metalloproteinases: effectors of development and normal physiology. Genes Dev 14, 2123-2133.
    • (2000) Genes Dev , vol.14 , pp. 2123-2133
    • Vu, T.H.1    Werb, Z.2
  • 95
    • 0030715322 scopus 로고    scopus 로고
    • ECM and cell surface proteolysis: regulating cellular ecology
    • Werb, Z. (1997). ECM and cell surface proteolysis: regulating cellular ecology. Cell 91, 439-442.
    • (1997) Cell , vol.91 , pp. 439-442
    • Werb, Z.1
  • 96
    • 0036479231 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer studies on the interaction between the lactate transporter MCT1 and CD147 provide information on the topology and stoichiometry of the complex in situ
    • Wilson, M. C., Meredith, D., and Halestrap, A. P. (2002). Fluorescence resonance energy transfer studies on the interaction between the lactate transporter MCT1 and CD147 provide information on the topology and stoichiometry of the complex in situ. J. Biol. Chem 277, 3666-3672.
    • (2002) J. Biol. Chem , vol.277 , pp. 3666-3672
    • Wilson, M.C.1    Meredith, D.2    Halestrap, A.P.3
  • 97
    • 0027998859 scopus 로고
    • A switch from stromal to tumor cell expression of stromelysin-1 mRNA associated with the conversion of squamous to spindle carcinomas during mouse skin tumor progression
    • Wright, J. H., McDonnell, S., Portella, G., Bowden, G. T., Balmain, A., and Matrisian, L. M. (1994). A switch from stromal to tumor cell expression of stromelysin-1 mRNA associated with the conversion of squamous to spindle carcinomas during mouse skin tumor progression. Mol. Carcinog 10, 207-215.
    • (1994) Mol. Carcinog , vol.10 , pp. 207-215
    • Wright, J.H.1    McDonnell, S.2    Portella, G.3    Bowden, G.T.4    Balmain, A.5    Matrisian, L.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.