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Volumn 295, Issue 2, 2010, Pages 198-204

Inhibition of Na+/H+ exchanger 1 by 5-(N-ethyl-N-isopropyl) amiloride reduces hypoxia-induced hepatocellular carcinoma invasion and motility

Author keywords

Hepatocellular carcinoma; Invasion; Migration; Na+ H+ exchanger 1; Tumor microenvironment

Indexed keywords

5 (N ETHYL N ISOPROPYL)AMILORIDE; GELATINASE A; GELATINASE B; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; SODIUM PROTON EXCHANGE PROTEIN 1; VASCULOTROPIN;

EID: 77954034986     PISSN: 03043835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.canlet.2010.03.001     Document Type: Article
Times cited : (68)

References (47)
  • 1
    • 7044264264 scopus 로고    scopus 로고
    • Hepatitis C infection and the increasing incidence of hepatocellular carcinoma: a population-based study
    • Davila J.A., Morgan R.O., Shaib Y., McGlynn K.A., El-Serag H.B. Hepatitis C infection and the increasing incidence of hepatocellular carcinoma: a population-based study. Gastroenterology 2004, 127:1372-1380.
    • (2004) Gastroenterology , vol.127 , pp. 1372-1380
    • Davila, J.A.1    Morgan, R.O.2    Shaib, Y.3    McGlynn, K.A.4    El-Serag, H.B.5
  • 2
    • 0033545541 scopus 로고    scopus 로고
    • Rising incidence of hepatocellular carcinoma in the United States
    • El-Serag H.B., Mason A.C. Rising incidence of hepatocellular carcinoma in the United States. New Engl. J. Med. 1999, 340:745-750.
    • (1999) New Engl. J. Med. , vol.340 , pp. 745-750
    • El-Serag, H.B.1    Mason, A.C.2
  • 3
    • 19644381818 scopus 로고    scopus 로고
    • Hepatocellular carcinoma: the need for progress
    • Thomas M.B., Zhu A.X. Hepatocellular carcinoma: the need for progress. J. Clin. Oncol. 2005, 23:2892-2899.
    • (2005) J. Clin. Oncol. , vol.23 , pp. 2892-2899
    • Thomas, M.B.1    Zhu, A.X.2
  • 4
    • 0033947630 scopus 로고    scopus 로고
    • Risk factors, prevention, and management of postoperative recurrence after resection of hepatocellular carcinoma
    • Poon R.T., Fan S.T., Wong J. Risk factors, prevention, and management of postoperative recurrence after resection of hepatocellular carcinoma. Ann. Surg. 2000, 232:10-24.
    • (2000) Ann. Surg. , vol.232 , pp. 10-24
    • Poon, R.T.1    Fan, S.T.2    Wong, J.3
  • 6
    • 36649014657 scopus 로고    scopus 로고
    • PH dependence of melanoma cell migration: protons extruded by NHE1 dominate protons of the bulk solution
    • Stuwe L., Muller M., Fabian A., Waning J., Mally S., Noel J., Schwab A., Stock C. PH dependence of melanoma cell migration: protons extruded by NHE1 dominate protons of the bulk solution. J. Physiol. 2007, 585:351-360.
    • (2007) J. Physiol. , vol.585 , pp. 351-360
    • Stuwe, L.1    Muller, M.2    Fabian, A.3    Waning, J.4    Mally, S.5    Noel, J.6    Schwab, A.7    Stock, C.8
  • 8
    • 33646576169 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tumor metastasis
    • Deryugina E.I., Quigley J.P. Matrix metalloproteinases and tumor metastasis. Cancer Metast. Rev. 2006, 25:9-34.
    • (2006) Cancer Metast. Rev. , vol.25 , pp. 9-34
    • Deryugina, E.I.1    Quigley, J.P.2
  • 9
    • 0036118399 scopus 로고    scopus 로고
    • Matrix metalloproteinases and matrix metalloproteinase inhibitors in lung cancer
    • Bonomi P. Matrix metalloproteinases and matrix metalloproteinase inhibitors in lung cancer. Semin. Oncol. 2002, 291:78-86.
    • (2002) Semin. Oncol. , vol.291 , pp. 78-86
    • Bonomi, P.1
  • 10
    • 31344458952 scopus 로고    scopus 로고
    • Structure and function of matrix metalloproteinases and TIMPs
    • Nagase H., Visse R., Murphy G. Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc. Res. 2006, 69:562-573.
    • (2006) Cardiovasc. Res. , vol.69 , pp. 562-573
    • Nagase, H.1    Visse, R.2    Murphy, G.3
  • 12
    • 0030229413 scopus 로고    scopus 로고
    • Vascular endothelial growth factor, a multifunctional polypeptide
    • Stephan C.C., Brock T.A. Vascular endothelial growth factor, a multifunctional polypeptide. Puerto Rico Health Sci. J. 1996, 15:169-178.
    • (1996) Puerto Rico Health Sci. J. , vol.15 , pp. 169-178
    • Stephan, C.C.1    Brock, T.A.2
  • 17
    • 0024408986 scopus 로고
    • Blood flow, oxygen and nutrient supply, and metabolic microenvironment of human tumors: a review
    • Vaupel P., Kallinowski F., Okunieff P. Blood flow, oxygen and nutrient supply, and metabolic microenvironment of human tumors: a review. Cancer Res. 1989, 49:6449-6465.
    • (1989) Cancer Res. , vol.49 , pp. 6449-6465
    • Vaupel, P.1    Kallinowski, F.2    Okunieff, P.3
  • 18
    • 0037144460 scopus 로고    scopus 로고
    • Oxygen-mediated regulation of tumor cell invasiveness: involvement of a nitric oxide signaling pathway
    • Postovit L.M., Adams M.A., Lash G.E., Heaton J.P., Graham C.H. Oxygen-mediated regulation of tumor cell invasiveness: involvement of a nitric oxide signaling pathway. J. Biol. Chem. 2002, 277:35730-35737.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35730-35737
    • Postovit, L.M.1    Adams, M.A.2    Lash, G.E.3    Heaton, J.P.4    Graham, C.H.5
  • 20
    • 0034037286 scopus 로고    scopus 로고
    • Microenvironment-induced cancer metastasis
    • Rofstad E.K. Microenvironment-induced cancer metastasis. Int. J. Radiat. Biol. 2000, 76:589-605.
    • (2000) Int. J. Radiat. Biol. , vol.76 , pp. 589-605
    • Rofstad, E.K.1
  • 21
    • 33751117499 scopus 로고    scopus 로고
    • HIF-1 regulates hypoxic induction of NHE1 expression and alkalinization of intracellular pH in pulmonary arterial myocytes
    • Shimoda L.A., Fallon M., Pisarcik S., Wang J., Semenza G.L. HIF-1 regulates hypoxic induction of NHE1 expression and alkalinization of intracellular pH in pulmonary arterial myocytes. Am. J. Physiol. Lung Cell. Mol. Physiol. 2006, 291:941-949.
    • (2006) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.291 , pp. 941-949
    • Shimoda, L.A.1    Fallon, M.2    Pisarcik, S.3    Wang, J.4    Semenza, G.L.5
  • 22
    • 0029751950 scopus 로고    scopus 로고
    • A reaction-diffusion model of cancer invasion
    • Gatenby R.A., Gawlinski E.T. A reaction-diffusion model of cancer invasion. Cancer Res. 1996, 56:5745-5753.
    • (1996) Cancer Res. , vol.56 , pp. 5745-5753
    • Gatenby, R.A.1    Gawlinski, E.T.2
  • 24
    • 0029970607 scopus 로고    scopus 로고
    • Implications of acidic tumour microenvironment for neoplastic growth and cancer treatment: a computer analysis
    • Kraus M., Wolf B. Implications of acidic tumour microenvironment for neoplastic growth and cancer treatment: a computer analysis. Tumor Biol. 1996, 17:133-154.
    • (1996) Tumor Biol. , vol.17 , pp. 133-154
    • Kraus, M.1    Wolf, B.2
  • 26
    • 0345643514 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase expression in tumor invasion
    • Westermarck J., Kahari V.M. Regulation of matrix metalloproteinase expression in tumor invasion. FASEB J. 1999, 13:781-792.
    • (1999) FASEB J. , vol.13 , pp. 781-792
    • Westermarck, J.1    Kahari, V.M.2
  • 27
    • 0032904304 scopus 로고    scopus 로고
    • Loss of basement membrane type IV collagen is associated with increased expression of metalloproteinases 2 and 9 (MMP-2 and MMP-9) during human colorectal tumorigenesis
    • Zeng Z.S., Cohen A.M., Guillem J.G. Loss of basement membrane type IV collagen is associated with increased expression of metalloproteinases 2 and 9 (MMP-2 and MMP-9) during human colorectal tumorigenesis. Carcinogenesis 1999, 20:749-755.
    • (1999) Carcinogenesis , vol.20 , pp. 749-755
    • Zeng, Z.S.1    Cohen, A.M.2    Guillem, J.G.3
  • 28
    • 13244291565 scopus 로고    scopus 로고
    • Expression and quantitative analysis of matrix metalloproteinase-2 and -9 in human gliomas
    • Komatsu K., Nakanishi Y., Nemoto N., Hori T., Sawada T., Kobayashi M. Expression and quantitative analysis of matrix metalloproteinase-2 and -9 in human gliomas. Brain Tumor Pathol. 2004, 21:105-112.
    • (2004) Brain Tumor Pathol. , vol.21 , pp. 105-112
    • Komatsu, K.1    Nakanishi, Y.2    Nemoto, N.3    Hori, T.4    Sawada, T.5    Kobayashi, M.6
  • 30
    • 20144378365 scopus 로고    scopus 로고
    • Acidic extracellular pH induces matrix metalloproteinase-9 expression in mouse metastatic melanoma cells through the phospholipase d-mitogen-activated protein kinase signaling
    • Kato Y., Lambert C.A., Colige A.C., Mineur P., Noël A., Frankenne F., Foidart J.-M., Baba M., Hata R.-I., Miyazaki K., Tsukuda M. Acidic extracellular pH induces matrix metalloproteinase-9 expression in mouse metastatic melanoma cells through the phospholipase d-mitogen-activated protein kinase signaling. J. Biol. Chem. 2005, 280:10938-10944.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10938-10944
    • Kato, Y.1    Lambert, C.A.2    Colige, A.C.3    Mineur, P.4    Noël, A.5    Frankenne, F.6    Foidart, J.-M.7    Baba, M.8    Hata, R.-I.9    Miyazaki, K.10    Tsukuda, M.11
  • 31
    • 9144231428 scopus 로고    scopus 로고
    • Expression profile of genes regulated by activity of the Na-H exchanger NHE1
    • Putney L.K., Barber D.L. Expression profile of genes regulated by activity of the Na-H exchanger NHE1. BMC Genom. 2004, 5:46-59.
    • (2004) BMC Genom. , vol.5 , pp. 46-59
    • Putney, L.K.1    Barber, D.L.2
  • 33
    • 84970070220 scopus 로고
    • Expression of vascular endothelial growth factor and its receptor, KDR, correlates with vascularity, metastasis, and proliferation of human colon cancer
    • Takahashi Y., Kitadai Y., Bucana C.D., Cleary K.R., EllisS L.M. Expression of vascular endothelial growth factor and its receptor, KDR, correlates with vascularity, metastasis, and proliferation of human colon cancer. Cancer Res. 1995, 55:3964-3968.
    • (1995) Cancer Res. , vol.55 , pp. 3964-3968
    • Takahashi, Y.1    Kitadai, Y.2    Bucana, C.D.3    Cleary, K.R.4    EllisS, L.M.5
  • 34
  • 35
    • 0032535721 scopus 로고    scopus 로고
    • Human mitogen-activated protein kinase kinase kinase mediates the stress-induced activation of mitogen-activated protein kinase cascades
    • Chan-Hui P.Y., Weaver R. Human mitogen-activated protein kinase kinase kinase mediates the stress-induced activation of mitogen-activated protein kinase cascades. Biochem. J. 1998, 336:599-609.
    • (1998) Biochem. J. , vol.336 , pp. 599-609
    • Chan-Hui, P.Y.1    Weaver, R.2
  • 36
    • 0036551486 scopus 로고    scopus 로고
    • Scatter-factor and semaphorin receptors: cell signalling for invasive growth
    • Trusolino L., Comoglio P.M. Scatter-factor and semaphorin receptors: cell signalling for invasive growth. Nat. Rev. Cancer 2002, 2:289-300.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 289-300
    • Trusolino, L.1    Comoglio, P.M.2
  • 37
    • 26044455880 scopus 로고    scopus 로고
    • Silibinin inhibits cell invasion through inactivation of both PI3K-Akt and MAPK signaling pathways
    • Chen P.N., Hsieh Y.S., Chiou H.L., Chu S.C. Silibinin inhibits cell invasion through inactivation of both PI3K-Akt and MAPK signaling pathways. Chem. Biol. Interact. 2005, 156:141-150.
    • (2005) Chem. Biol. Interact. , vol.156 , pp. 141-150
    • Chen, P.N.1    Hsieh, Y.S.2    Chiou, H.L.3    Chu, S.C.4
  • 38
    • 0041363324 scopus 로고    scopus 로고
    • Essential role for ERK mitogen-activated protein kinase in matrix metalloproteinase-9 regulation in rat cortical astrocytes
    • Arai K., Lee S.R., Lo E.H. Essential role for ERK mitogen-activated protein kinase in matrix metalloproteinase-9 regulation in rat cortical astrocytes. Glia 2003, 43:254-264.
    • (2003) Glia , vol.43 , pp. 254-264
    • Arai, K.1    Lee, S.R.2    Lo, E.H.3
  • 39
    • 0032990608 scopus 로고    scopus 로고
    • Role of ERK and JNK pathways in regulating cell motility and matrix metalloproteinase 9 production in growth factor-stimulated human epidermal keratinocytes
    • Zeigler M.E., Chi Y., Schmidt T., Varani J. Role of ERK and JNK pathways in regulating cell motility and matrix metalloproteinase 9 production in growth factor-stimulated human epidermal keratinocytes. J. Cell. Physiol. 1999, 180:271-284.
    • (1999) J. Cell. Physiol. , vol.180 , pp. 271-284
    • Zeigler, M.E.1    Chi, Y.2    Schmidt, T.3    Varani, J.4
  • 40
    • 1542398801 scopus 로고    scopus 로고
    • Downmodulation of ERK protein kinase activity inhibits VEGF secretion by human myeloma cells and myeloma-induced angiogenesis
    • Giuliani N., Lunghi P., Morandi F., Colla S., Bonomini S., Hojden M., Rizzoli V., Bonati A. Downmodulation of ERK protein kinase activity inhibits VEGF secretion by human myeloma cells and myeloma-induced angiogenesis. Leukemia 2004, 18:628-635.
    • (2004) Leukemia , vol.18 , pp. 628-635
    • Giuliani, N.1    Lunghi, P.2    Morandi, F.3    Colla, S.4    Bonomini, S.5    Hojden, M.6    Rizzoli, V.7    Bonati, A.8
  • 41
    • 0034595061 scopus 로고    scopus 로고
    • Different regulation of vascular endothelial growth factor expression by the ERK and p38 kinase pathways in V-ras, v-raf, and v-myc transformed cells
    • Okajima E., Thorgeirsson U.P. Different regulation of vascular endothelial growth factor expression by the ERK and p38 kinase pathways in V-ras, v-raf, and v-myc transformed cells. Biochem. Biophys. Res. Commun. 2000, 270:108-111.
    • (2000) Biochem. Biophys. Res. Commun. , vol.270 , pp. 108-111
    • Okajima, E.1    Thorgeirsson, U.P.2
  • 42
    • 0032498850 scopus 로고    scopus 로고
    • Role of ion channels and exchangers in mechanical stretch-induced cardiomyocyte hypertrophy
    • Yamazaki T., Komuro I., Kudoh S., Zou Y., Nagai R., Aikawa R., Uozumi H., Yazaki Y. Role of ion channels and exchangers in mechanical stretch-induced cardiomyocyte hypertrophy. Circ. Res. 1998, 82:430-437.
    • (1998) Circ. Res. , vol.82 , pp. 430-437
    • Yamazaki, T.1    Komuro, I.2    Kudoh, S.3    Zou, Y.4    Nagai, R.5    Aikawa, R.6    Uozumi, H.7    Yazaki, Y.8
  • 43
    • 0345826111 scopus 로고    scopus 로고
    • ERK is regulated by sodium-proton exchanger in rat aortic vascular smooth muscle cells
    • Mukhin Y.V., Garnovskaya M.N., Ullian M.E., Raymond J.R. ERK is regulated by sodium-proton exchanger in rat aortic vascular smooth muscle cells. J. Biol. Chem. 2004, 279:1845-1852.
    • (2004) J. Biol. Chem. , vol.279 , pp. 1845-1852
    • Mukhin, Y.V.1    Garnovskaya, M.N.2    Ullian, M.E.3    Raymond, J.R.4
  • 47
    • 0032824458 scopus 로고    scopus 로고
    • MAPKinase and regulation of the sodium proton exchanger in human red blood cell
    • Sartori M., Ceolotto G., Semplicini A. MAPKinase and regulation of the sodium proton exchanger in human red blood cell. Biochim. Biophys. Acta 1999, 1421:140-148.
    • (1999) Biochim. Biophys. Acta , vol.1421 , pp. 140-148
    • Sartori, M.1    Ceolotto, G.2    Semplicini, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.