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Volumn 39, Issue 11, 2007, Pages 2049-2062

Retraction notice: Retraction notice to “Growth factors and beta cell replication” (International Journal of Biochemistry and Cell Biology (2007) 39(11) (2049–2062), (S1357272507001768), (10.1016/j.biocel.2007.05.023));siRNA targeted against matrix metalloproteinase 11 inhibits the metastatic capability of murine hepatocarcinoma cell Hca-F to lymph nodes

Author keywords

Hepatocarcinoma; Lymphatic metastasis; MMP 11; RNAi

Indexed keywords

PROTEINASE; SMALL INTERFERING RNA; STROMELYSIN 3; UNCLASSIFIED DRUG; ZINC ENDOPEPTIDASE;

EID: 34548444272     PISSN: 13572725     EISSN: 18785875     Source Type: Journal    
DOI: 10.1016/j.biocel.2021.106075     Document Type: Erratum
Times cited : (33)

References (39)
  • 1
    • 0141731300 scopus 로고    scopus 로고
    • Dual stromelysin-3 function during natural mouse mammary tumor virus-ras tumor progression
    • Andarawewa K.L., Boulay A., Masson R., Mathelin C., Stoll I., Tomasetto C., et al. Dual stromelysin-3 function during natural mouse mammary tumor virus-ras tumor progression. Cancer Res. 15 (2003) 5844-5849
    • (2003) Cancer Res. , vol.15 , pp. 5844-5849
    • Andarawewa, K.L.1    Boulay, A.2    Masson, R.3    Mathelin, C.4    Stoll, I.5    Tomasetto, C.6
  • 2
    • 28244496184 scopus 로고    scopus 로고
    • Stromelysin-3 is a potent negative regulator of adipogenesis participating to cancer cell-adipocyte interaction/crosstalk at the tumor invasive front
    • Andarawewa K.L., Motrescu E.R., Chenard M.P., Gansmuller A., Stoll I., Tomasetto C., et al. Stromelysin-3 is a potent negative regulator of adipogenesis participating to cancer cell-adipocyte interaction/crosstalk at the tumor invasive front. Cancer Res. 1 (2005) 10862-10871
    • (2005) Cancer Res. , vol.1 , pp. 10862-10871
    • Andarawewa, K.L.1    Motrescu, E.R.2    Chenard, M.P.3    Gansmuller, A.4    Stoll, I.5    Tomasetto, C.6
  • 3
    • 0029022983 scopus 로고
    • Structure and promoter characterization of the human stromelysin-3 gene
    • Anglard P., Melot T., Guerin E., Thomas G., and Basset P. Structure and promoter characterization of the human stromelysin-3 gene. J. Biol. Chem. 270 (1995) 20337-20344
    • (1995) J. Biol. Chem. , vol.270 , pp. 20337-20344
    • Anglard, P.1    Melot, T.2    Guerin, E.3    Thomas, G.4    Basset, P.5
  • 4
    • 0025641098 scopus 로고
    • A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas
    • Basset P., Bellocq J.P., Wolf C., Stoll I., Hutin P., Limacher J.M., et al. A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas. Nature 348 (1990) 699-704
    • (1990) Nature , vol.348 , pp. 699-704
    • Basset, P.1    Bellocq, J.P.2    Wolf, C.3    Stoll, I.4    Hutin, P.5    Limacher, J.M.6
  • 5
    • 0035266386 scopus 로고    scopus 로고
    • High cancer cell death in syngeneic tumors developed in host mice deficient for the stromelysin-3 matrix metalloproteinase
    • Boulay A., Masson R., Chenard M.P., Fahime M., Cassard L., Bellocq J.P., et al. High cancer cell death in syngeneic tumors developed in host mice deficient for the stromelysin-3 matrix metalloproteinase. Cancer Res. 61 (2001) 2189-2193
    • (2001) Cancer Res. , vol.61 , pp. 2189-2193
    • Boulay, A.1    Masson, R.2    Chenard, M.P.3    Fahime, M.4    Cassard, L.5    Bellocq, J.P.6
  • 6
    • 4644293454 scopus 로고    scopus 로고
    • Conditionally replicating adenoviruses expressing short hairpin RNAs silence the expression of a target gene in cancer cells
    • Carette J.E., Overmeer R.M., Schagen F.H., Alemany R., Barski O.A., Gerritsen W.R., et al. Conditionally replicating adenoviruses expressing short hairpin RNAs silence the expression of a target gene in cancer cells. Cancer Res. 64 (2004) 2663-2667
    • (2004) Cancer Res. , vol.64 , pp. 2663-2667
    • Carette, J.E.1    Overmeer, R.M.2    Schagen, F.H.3    Alemany, R.4    Barski, O.A.5    Gerritsen, W.R.6
  • 7
    • 29144530303 scopus 로고    scopus 로고
    • Suppression of tumor formation in lymph nodes by l-selectin-mediated natural killer cell recruitment
    • Chen S., Kawashima H., Lowe J.B., Lanier L.L., and Fukuda M. Suppression of tumor formation in lymph nodes by l-selectin-mediated natural killer cell recruitment. J. Exp. Med. 202 (2005) 1679-1689
    • (2005) J. Exp. Med. , vol.202 , pp. 1679-1689
    • Chen, S.1    Kawashima, H.2    Lowe, J.B.3    Lanier, L.L.4    Fukuda, M.5
  • 8
    • 26944476981 scopus 로고    scopus 로고
    • Expression of stromelysin-3 (matrix metalloproteinase-11) in macrophages of murine thymus following thymocyte apoptosis
    • Chikako O., and Shinji I. Expression of stromelysin-3 (matrix metalloproteinase-11) in macrophages of murine thymus following thymocyte apoptosis. Cell. Immunol. 235 (2005) 21-28
    • (2005) Cell. Immunol. , vol.235 , pp. 21-28
    • Chikako, O.1    Shinji, I.2
  • 9
    • 33749832089 scopus 로고    scopus 로고
    • Functional expression of CXC chemokine recepter-4 mediates the secretion of matrix metalloproteinases from mouse hepatocarcinoma cell lines with different lymphatic metastasis ability
    • Chu H., Zhou H., Liu Y., Hu Y., and Zhang J. Functional expression of CXC chemokine recepter-4 mediates the secretion of matrix metalloproteinases from mouse hepatocarcinoma cell lines with different lymphatic metastasis ability. IJBCB 39 (2007) 197-205
    • (2007) IJBCB , vol.39 , pp. 197-205
    • Chu, H.1    Zhou, H.2    Liu, Y.3    Hu, Y.4    Zhang, J.5
  • 10
    • 0034114776 scopus 로고    scopus 로고
    • Overexpression level of stromelysin 3 is related to the lymph node involvement in nonsmall cell lung cancer
    • Delebecq T.J., Porte H., Zerimech F., Copin M.C., Gouyer V., Dacquembronne E., et al. Overexpression level of stromelysin 3 is related to the lymph node involvement in nonsmall cell lung cancer. Clin. Cancer Res. 6 (2000) 1086-1092
    • (2000) Clin. Cancer Res. , vol.6 , pp. 1086-1092
    • Delebecq, T.J.1    Porte, H.2    Zerimech, F.3    Copin, M.C.4    Gouyer, V.5    Dacquembronne, E.6
  • 11
    • 10044248211 scopus 로고    scopus 로고
    • Matrix metalloproteinase 11 depletion inhibits cell proliferation in gastric cancer cells
    • Deng H., Guo R.F., Li W.M., Zhao M., and Lu Y.Y. Matrix metalloproteinase 11 depletion inhibits cell proliferation in gastric cancer cells. BBRC 14 (2005) 274-281
    • (2005) BBRC , vol.14 , pp. 274-281
    • Deng, H.1    Guo, R.F.2    Li, W.M.3    Zhao, M.4    Lu, Y.Y.5
  • 12
    • 0037829219 scopus 로고    scopus 로고
    • Active stromelysin-3 (MMP-11) increases MCF-7 survival in three-dimensional Matrigel culture via activation of p42/p44 MAP-kinase
    • Fromigue O., Louis K., Wu E., Loubat A., Shipp M., Auberger P., et al. Active stromelysin-3 (MMP-11) increases MCF-7 survival in three-dimensional Matrigel culture via activation of p42/p44 MAP-kinase. Int. J. Cancer 106 (2003) 355-363
    • (2003) Int. J. Cancer , vol.106 , pp. 355-363
    • Fromigue, O.1    Louis, K.2    Wu, E.3    Loubat, A.4    Shipp, M.5    Auberger, P.6
  • 14
    • 0034892712 scopus 로고    scopus 로고
    • Molecular mechanism about lymphogenous metastasis of hepatocarcinoma cells in mice
    • Hou L., Li Y., Jia Y.H., Wang B., Xin Y., Ling M.Y., et al. Molecular mechanism about lymphogenous metastasis of hepatocarcinoma cells in mice. World J. Gastroenterol. 7 (2001) 532-536
    • (2001) World J. Gastroenterol. , vol.7 , pp. 532-536
    • Hou, L.1    Li, Y.2    Jia, Y.H.3    Wang, B.4    Xin, Y.5    Ling, M.Y.6
  • 15
    • 33744797077 scopus 로고    scopus 로고
    • MMP-9 is differentially expressed in primary human colorectal adenocarcinomas and their metastases
    • Illemann M., Bird N., Majeed A., Sehested M., Laerum O.D., Lund L.R., et al. MMP-9 is differentially expressed in primary human colorectal adenocarcinomas and their metastases. Mol. Cancer Res. 4 (2006) 293-302
    • (2006) Mol. Cancer Res. , vol.4 , pp. 293-302
    • Illemann, M.1    Bird, N.2    Majeed, A.3    Sehested, M.4    Laerum, O.D.5    Lund, L.R.6
  • 16
    • 33646556449 scopus 로고    scopus 로고
    • Caveolin-1 upregulates CD147 glycosylation and the invasive capability of murine hepatocarcinoma cell lines
    • Jia L., Wang S., Zhou H., Cao J., Hu Y., and Zhang J. Caveolin-1 upregulates CD147 glycosylation and the invasive capability of murine hepatocarcinoma cell lines. IJBCB 38 (2006) 1584-1593
    • (2006) IJBCB , vol.38 , pp. 1584-1593
    • Jia, L.1    Wang, S.2    Zhou, H.3    Cao, J.4    Hu, Y.5    Zhang, J.6
  • 17
    • 33745115646 scopus 로고    scopus 로고
    • Deglycosylation of CD147 down-regulates Matrix Metalloproteinase-11 expression and the adhesive capability of murine Hepatocarcinoma cell HcaF in vitro
    • Jia L., Zhou H., Wang S., Cao J., Wei W., and Zhang J. Deglycosylation of CD147 down-regulates Matrix Metalloproteinase-11 expression and the adhesive capability of murine Hepatocarcinoma cell HcaF in vitro. IUBMB Life 58 (2006) 209-216
    • (2006) IUBMB Life , vol.58 , pp. 209-216
    • Jia, L.1    Zhou, H.2    Wang, S.3    Cao, J.4    Wei, W.5    Zhang, J.6
  • 18
    • 33645698574 scopus 로고    scopus 로고
    • Transforming growth factor-B1 induces tissue inhibitor of metalloproteinase-1 expression via activation of extracellular signal-regulated kinase and Sp1 in human fibrosarcoma cells
    • Kwak H.J., Park M.J., Cho H., Park C.M., Moon S.I., Lee H.C., et al. Transforming growth factor-B1 induces tissue inhibitor of metalloproteinase-1 expression via activation of extracellular signal-regulated kinase and Sp1 in human fibrosarcoma cells. Mol. Cancer Res. 4 (2006) 209-220
    • (2006) Mol. Cancer Res. , vol.4 , pp. 209-220
    • Kwak, H.J.1    Park, M.J.2    Cho, H.3    Park, C.M.4    Moon, S.I.5    Lee, H.C.6
  • 19
    • 0035650675 scopus 로고    scopus 로고
    • MMP9 production by human monocytederived macrophages is decreased on polymerized type I collagen
    • Lepidi S., Kenagy R.D., Raines E.W., Chiu E.S., Chait A., Ross R., et al. MMP9 production by human monocytederived macrophages is decreased on polymerized type I collagen. J. Vasc. Surg. 34 (2001) 1111-1118
    • (2001) J. Vasc. Surg. , vol.34 , pp. 1111-1118
    • Lepidi, S.1    Kenagy, R.D.2    Raines, E.W.3    Chiu, E.S.4    Chait, A.5    Ross, R.6
  • 20
    • 0032526634 scopus 로고    scopus 로고
    • Unique organization and involvement of GAGA factors in the transcriptional regulation of the Xenopus stromelysin-3 gene
    • Li J., Liang V.C.T., Sedgwick T., Wong J., and Shi Y.B. Unique organization and involvement of GAGA factors in the transcriptional regulation of the Xenopus stromelysin-3 gene. Nucl. Acids Res. 26 (1998) 3018-3025
    • (1998) Nucl. Acids Res. , vol.26 , pp. 3018-3025
    • Li, J.1    Liang, V.C.T.2    Sedgwick, T.3    Wong, J.4    Shi, Y.B.5
  • 21
    • 0035283892 scopus 로고    scopus 로고
    • Expression and activity of matrix metalloproteases in human malignant mesothelioma cell lines
    • Liu Z., Ivanoff A., and Klominek J. Expression and activity of matrix metalloproteases in human malignant mesothelioma cell lines. Int. J. Cancer 91 (2001) 638-643
    • (2001) Int. J. Cancer , vol.91 , pp. 638-643
    • Liu, Z.1    Ivanoff, A.2    Klominek, J.3
  • 22
    • 0034704133 scopus 로고    scopus 로고
    • Multiple regulator elements in the murine stromelysin-3 promoter: Evidence for direct control by CCAAT/enhancer-binding protein beta and thyroid and retinoid receptors
    • Ludwig M.G., Basset P., and Anglard P. Multiple regulator elements in the murine stromelysin-3 promoter: Evidence for direct control by CCAAT/enhancer-binding protein beta and thyroid and retinoid receptors. J. Biol. Chem. 275 (2000) 39981-39990
    • (2000) J. Biol. Chem. , vol.275 , pp. 39981-39990
    • Ludwig, M.G.1    Basset, P.2    Anglard, P.3
  • 23
    • 0040776938 scopus 로고    scopus 로고
    • Identification of insulin-like growth factor-binding protein-1 as a potential physiological substrate for human stromelysin-3
    • Manes S., Mira E., Barbacid M.M., Cipres A., FernandezResa P., Buesa J.M., et al. Identification of insulin-like growth factor-binding protein-1 as a potential physiological substrate for human stromelysin-3. J. Biol. Chem. 272 (1997) 25706-25712
    • (1997) J. Biol. Chem. , vol.272 , pp. 25706-25712
    • Manes, S.1    Mira, E.2    Barbacid, M.M.3    Cipres, A.4    FernandezResa, P.5    Buesa, J.M.6
  • 24
    • 0032559821 scopus 로고    scopus 로고
    • In vivo evidence that the stromelysin-3 metalloproteinase contributes in a paracrine manner to epithelial cell malignancy
    • Masson R., Lefebvre O., Noel A., Fahime M.E., Chenard M.P., Wendling C., et al. In vivo evidence that the stromelysin-3 metalloproteinase contributes in a paracrine manner to epithelial cell malignancy. J. Cell Biol. 140 (1998) 1535-1541
    • (1998) J. Cell Biol. , vol.140 , pp. 1535-1541
    • Masson, R.1    Lefebvre, O.2    Noel, A.3    Fahime, M.E.4    Chenard, M.P.5    Wendling, C.6
  • 25
    • 0033999308 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Biologic activity and clinical implications
    • Nelson A.R., Fingleton B., Rothenberg M.L., and Matrisian L.M. Matrix metalloproteinases: Biologic activity and clinical implications. J. Clin. Oncol. 18 (2000) 1135-1149
    • (2000) J. Clin. Oncol. , vol.18 , pp. 1135-1149
    • Nelson, A.R.1    Fingleton, B.2    Rothenberg, M.L.3    Matrisian, L.M.4
  • 27
    • 0034673675 scopus 로고    scopus 로고
    • Demonstration in vivo that stromelysin-3 functions through its proteolytic activity
    • Noel A., Boulay A., Kebers F., Kannan R., Hajitou A., and CalbergBacq C.M. Demonstration in vivo that stromelysin-3 functions through its proteolytic activity. Oncogene 19 (2000) 1605-1612
    • (2000) Oncogene , vol.19 , pp. 1605-1612
    • Noel, A.1    Boulay, A.2    Kebers, F.3    Kannan, R.4    Hajitou, A.5    CalbergBacq, C.M.6
  • 28
    • 0028116127 scopus 로고
    • Hydrolytic inactivation of a breast carcinoma cell-derived serpin by human stromelysin-3
    • Pei D., Majmudar G., and Weiss S.J. Hydrolytic inactivation of a breast carcinoma cell-derived serpin by human stromelysin-3. J. Biol. Chem. 269 (1994) 25849-25855
    • (1994) J. Biol. Chem. , vol.269 , pp. 25849-25855
    • Pei, D.1    Majmudar, G.2    Weiss, S.J.3
  • 29
    • 0029014101 scopus 로고
    • Furin-dependent intracellular activation of the human stromelysin-3 zymogen
    • Pei D., and WeissF S.J. Furin-dependent intracellular activation of the human stromelysin-3 zymogen. Nature 375 (1995) 244-247
    • (1995) Nature , vol.375 , pp. 244-247
    • Pei, D.1    WeissF, S.J.2
  • 31
    • 15244340583 scopus 로고    scopus 로고
    • From a unique cell to metastasis is a long way to go: Clues to stromelysin-3 participation
    • Rio M.C. From a unique cell to metastasis is a long way to go: Clues to stromelysin-3 participation. Biochimie 87 (2005) 299-306
    • (2005) Biochimie , vol.87 , pp. 299-306
    • Rio, M.C.1
  • 33
    • 0345306117 scopus 로고    scopus 로고
    • Transposon silencing in the Caenorhabditis elegans germ line by natural RNAi
    • Sijen T., and Plasterk R.H. Transposon silencing in the Caenorhabditis elegans germ line by natural RNAi. Nature 426 (2003) 310-314
    • (2003) Nature , vol.426 , pp. 310-314
    • Sijen, T.1    Plasterk, R.H.2
  • 34
    • 0031797110 scopus 로고    scopus 로고
    • Stromelysin 3 is overexpressed in human pancreatic carcinoma and regulated by retinoic acid in pancreatic carcinoma cell lines
    • Von-Marschall Z., Riecken E.O., and Rosewicz S. Stromelysin 3 is overexpressed in human pancreatic carcinoma and regulated by retinoic acid in pancreatic carcinoma cell lines. Gut 43 (1998) 692-698
    • (1998) Gut , vol.43 , pp. 692-698
    • Von-Marschall, Z.1    Riecken, E.O.2    Rosewicz, S.3
  • 35
    • 0027534904 scopus 로고
    • Stromelysin 3 belongs to a subgroup of proteinases expressed in breast carcinoma fibroblastic cells and possibly implicated in tumor progression
    • Wolf C., Rouyer N., Lutz Y., Adida C., Loriot M., Bellocq J.P., et al. Stromelysin 3 belongs to a subgroup of proteinases expressed in breast carcinoma fibroblastic cells and possibly implicated in tumor progression. Proc Natl Acad Sci USA 90 (1993) 1843-1847
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1843-1847
    • Wolf, C.1    Rouyer, N.2    Lutz, Y.3    Adida, C.4    Loriot, M.5    Bellocq, J.P.6
  • 37
    • 85047174774 scopus 로고    scopus 로고
    • Extracellular matrix metalloproteinase inducer stimulates tumor angiogenesis by elevating vascular endothelial cell growth factor and matrix metalloproteinases
    • Yi T., Marian T., Nakada K., Prabakaran K., Francis M.C., Hillary M., et al. Extracellular matrix metalloproteinase inducer stimulates tumor angiogenesis by elevating vascular endothelial cell growth factor and matrix metalloproteinases. Cancer Res. 65 (2005) 3139-3199
    • (2005) Cancer Res. , vol.65 , pp. 3139-3199
    • Yi, T.1    Marian, T.2    Nakada, K.3    Prabakaran, K.4    Francis, M.C.5    Hillary, M.6
  • 38
    • 12244274394 scopus 로고    scopus 로고
    • Reliability of tissue microarrays in detecting protein expression and gene amplification in breast cancer
    • Zhang D., Salto-Tellez M., Putti T.C., Do E., and Koay E.S. Reliability of tissue microarrays in detecting protein expression and gene amplification in breast cancer. Mod. Pathol. 16 (2003) 79-84
    • (2003) Mod. Pathol. , vol.16 , pp. 79-84
    • Zhang, D.1    Salto-Tellez, M.2    Putti, T.C.3    Do, E.4    Koay, E.S.5
  • 39
    • 33646415976 scopus 로고    scopus 로고
    • Divergent expression and roles for caveolin-1 in mouse hepatocarcinoma cell lines with varying invasive ability
    • Zhou H., Jia L., Wang S., Wang H., Chou H., Hu Y., et al. Divergent expression and roles for caveolin-1 in mouse hepatocarcinoma cell lines with varying invasive ability. BBRC 345 (2006) 486-494
    • (2006) BBRC , vol.345 , pp. 486-494
    • Zhou, H.1    Jia, L.2    Wang, S.3    Wang, H.4    Chou, H.5    Hu, Y.6


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