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Volumn 30, Issue 4, 2010, Pages 1169-1181

Gamma-glutamyltransferase of cancer cells at the crossroads of tumor progression, drug resistance and drug targeting

Author keywords

Drug resistance; Gamma glutamyltransferase; Human neoplasia; Redox regulation; Review; Tumor progression

Indexed keywords

4 [N (GLUTATHIONYLACETYL)AMINO]PHENYLARSONOUS ACID; 6 DIAZO 5 OXONORLEUCINE; ACIVICIN; ARSENIC ACID DERIVATIVE; AZASERINE; CISPLATIN; CYSTEINE; DOXORUBICIN; FLUOROURACIL; GAMMA GLUTAMYLTRANSFERASE; HYDROGEN PEROXIDE; UNCLASSIFIED DRUG;

EID: 77953783691     PISSN: 02507005     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (211)

References (159)
  • 1
    • 0034837235 scopus 로고    scopus 로고
    • Gamma-glutamyltransferase
    • Whitfield JB: Gamma-glutamyltransferase. Crit Rev Clin Lab Sci 38: 263-355, 2001.
    • (2001) Crit Rev Clin Lab Sci , vol.38 , pp. 263-355
    • Whitfield, J.B.1
  • 2
    • 0025164256 scopus 로고
    • Leukotrienes and other products of the 5-lipoxygenase pathway. Biochemistry and relation to pathobiology in human diseases
    • Lewis RA, Austen KF and Soberman RJ: Leukotrienes and other products of the 5-lipoxygenase pathway. Biochemistry and relation to pathobiology in human diseases. N Engl J Med 323: 645-655, 1990.
    • (1990) N Engl J Med , vol.323 , pp. 645-655
    • Lewis, R.A.1    Austen, K.F.2    Soberman, R.J.3
  • 3
    • 0030945376 scopus 로고    scopus 로고
    • 5-Nitrosoglutathione as a substrate for gamma-glutamyl transpeptidase
    • Hogg N, Singh RJ, Konorev E, Joseph J and Kalyanaraman B: 5-Nitrosoglutathione as a substrate for gamma-glutamyl transpeptidase. Biochem J 323(Pt 2): 477-481, 1997.
    • (1997) Biochem J , vol.323 , Issue.PART 2 , pp. 477-481
    • Hogg, N.1    Singh, R.J.2    Konorev, E.3    Joseph, J.4    Kalyanaraman, B.5
  • 5
    • 0029794573 scopus 로고    scopus 로고
    • Immunohistochemical detection of gamma-glutamyl transpeptidase in normal human tissue
    • Hanigan MH and Frierson HF Jr: Immunohistochemical detection of gamma-glutamyl transpeptidase in normal human tissue. J Histochem Cytochem 44: 1101-1108, 1996. (Pubitemid 26337286)
    • (1996) Journal of Histochemistry and Cytochemistry , vol.44 , Issue.10 , pp. 1101-1108
    • Hanigan, M.H.1    Frierson Jr., H.F.2
  • 6
    • 0033048835 scopus 로고    scopus 로고
    • Altered expression of gamma-glutamyl transpeptidase in human tumors
    • Hanigan MH, Frierson HF Jr, Swanson PE and De Young BR: Altered expression of gamma-glutamyl transpeptidase in human tumors. Hum Pathol 30(3): 300-305, 1999. (Pubitemid 29125150)
    • (1999) Human Pathology , vol.30 , Issue.3 , pp. 300-305
    • Hanigan, M.H.1    Frierson Jr., H.F.2    Swanson, P.E.3    De Young, B.R.4
  • 7
    • 29144438058 scopus 로고    scopus 로고
    • Expression of gamma-glutamyltransferase in cancer cells and its significance in drug resistance
    • Pompella A, De Tata V, Paolicchi A and Zunino F: Expression of gamma-glutamyltransferase in cancer cells and its significance in drug resistance. Biochem Pharmacol 71(3): 231-238, 2006.
    • (2006) Biochem Pharmacol , vol.71 , Issue.3 , pp. 231-238
    • Pompella, A.1    De Tata, V.2    Paolicchi, A.3    Zunino, F.4
  • 10
    • 58149095551 scopus 로고    scopus 로고
    • Metabolism of the tumor angiogenesis inhibitor 4-(N-(S- glutathionylacetyl)amino)phenylarsinous acid
    • Dilda PJ, Ramsey EE, Corti A, Pompella A and Hogg PJ: Metabolism of the tumor angiogenesis inhibitor 4-(N-(S-glutathionylacetyl)amino)phenylarsinous acid. J Biol Chem 283(51): 35428-35434, 2008.
    • (2008) J Biol Chem , vol.283 , Issue.51 , pp. 35428-35434
    • Dilda, P.J.1    Ramsey, E.E.2    Corti, A.3    Pompella, A.4    Hogg, P.J.5
  • 11
  • 12
    • 0028534953 scopus 로고
    • Gamma-glutamyl transpeptidase is increased by oxidative stress in rat alveolar L2 epithelial cells
    • Kugelman A, Choy HA, Liu R, Shi MM, Gozal E and Forman HJ: Gamma-glutamyl transpeptidase is increased by oxidative stress in rat alveolar L2 epithelial cells. Am J Respir Cell Mol Biol 11: 586-592, 1994.
    • (1994) Am J Respir Cell Mol Biol , vol.11 , pp. 586-592
    • Kugelman, A.1    Choy, H.A.2    Liu, R.3    Shi, M.M.4    Gozal, E.5    Forman, H.J.6
  • 14
    • 0031897028 scopus 로고    scopus 로고
    • Quinones increase gamma-glutamyl transpeptidase expression by multiple mechanisms in rat lung epithelial cells
    • Liu RM, Shi MM, Giulivi C and Forman HJ: Quinones increase gamma-glutamyl transpeptidase expression by multiple mechanisms in rat lung epithelial cells. Am J Physiol Lung Cell Mol Physiol 274: 330-336, 1998.
    • (1998) Am J Physiol Lung Cell Mol Physiol , vol.274 , pp. 330-336
    • Liu, R.M.1    Shi, M.M.2    Giulivi, C.3    Forman, H.J.4
  • 15
    • 0033819563 scopus 로고    scopus 로고
    • Regulation of gamma-glutamyltransferase in cisplatin-resistant and -sensitive colon carcinoma cells after acute cisplatin and oxidative stress exposures
    • Borud O, Mortensen B, Mikkelsen IM, Leroy P, Wellman M and Huseby NE: Regulation of gamma-glutamyltransferase in cisplatin-resistant and -sensitive colon carcinoma cells after acute cisplatin and oxidative stress exposures. Int J Cancer 88: 464-468, 2000.
    • (2000) Int J Cancer , vol.88 , pp. 464-468
    • Borud, O.1    Mortensen, B.2    Mikkelsen, I.M.3    Leroy, P.4    Wellman, M.5    Huseby, N.E.6
  • 16
    • 0037099473 scopus 로고    scopus 로고
    • Activation of the gamma-glutamyltransferase promoter 2 in the rat colon carcinoma cell line CC531 by histone deacetylase inhibitors is mediated through the Sp1-binding motif
    • Mikkelsen IM, Huseby NE, Visvikis A and Moens U: Activation of the gamma-glutamyltransferase promoter 2 in the rat colon carcinoma cell line CC531 by histone deacetylase inhibitors is mediated through the Sp1-binding motif. Biochem Pharmacol 64: 307-315, 2002.
    • (2002) Biochem Pharmacol , vol.64 , pp. 307-315
    • Mikkelsen, I.M.1    Huseby, N.E.2    Visvikis, A.3    Moens, U.4
  • 18
    • 32044466295 scopus 로고    scopus 로고
    • 4-Hydroxynonenal induces rat gamma-glutamyl transpeptidase through mitogen-activated protein kinase-mediated electrophile response element/nuclear factor erythroid 2-related factor 2 signaling
    • Zhang H, Liu H, Iles KE, Liu RM, Postlethwait EM, Laperche Y and Forman HJ: 4-Hydroxynonenal induces rat gamma-glutamyl transpeptidase through mitogen-activated protein kinase-mediated electrophile response element/nuclear factor erythroid 2-related factor 2 signaling. Am J Respir Cell Mol Biol 34(2): 174-181, 2006.
    • (2006) Am J Respir Cell Mol Biol , vol.34 , Issue.2 , pp. 174-181
    • Zhang, H.1    Liu, H.2    Iles, K.E.3    Liu, R.M.4    Postlethwait, E.M.5    Laperche, Y.6    Forman, H.J.7
  • 19
    • 33644615884 scopus 로고    scopus 로고
    • Radiation-induced up-regulation of gamma-glutamyltransferase in colon carcinoma cells is mediated through the Ras signal transduction pathway
    • Pankiv S, Møller S, Bjørkøy G, Moensc U and Huseby NE: Radiation-induced up-regulation of gamma-glutamyltransferase in colon carcinoma cells is mediated through the Ras signal transduction pathway. Biochim Biophys Acta 1760: 151-157, 2006.
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 151-157
    • Pankiv, S.1    Møller, S.2    Bjørkøy, G.3    Moensc, U.4    Huseby, N.E.5
  • 20
    • 37349011293 scopus 로고    scopus 로고
    • Gamma-glutamyltransferase is up-regulated after oxidative stress through the Ras signal transduction pathway in rat colon carcinoma cells
    • Pandur S, Pankiv S, Johannessen M, Moens U and Huseby NE: Gamma-glutamyltransferase is up-regulated after oxidative stress through the Ras signal transduction pathway in rat colon carcinoma cells. Free Radic Res 41(12): 1376-1384, 2007.
    • (2007) Free Radic Res , vol.41 , Issue.12 , pp. 1376-1384
    • Pandur, S.1    Pankiv, S.2    Johannessen, M.3    Moens, U.4    Huseby, N.E.5
  • 22
    • 0037096987 scopus 로고    scopus 로고
    • Gamma-glutamyl transpeptidase expression in Ewing's sarcoma cells: Up-regulation by interferons
    • Bouman L, Sanceau J, Rouillard D and Bauvois B: Gamma-glutamyl transpeptidase expression in Ewing's sarcoma cells: up-regulation by interferons. Biochem J 364: 719-724, 2002.
    • (2002) Biochem J , vol.364 , pp. 719-724
    • Bouman, L.1    Sanceau, J.2    Rouillard, D.3    Bauvois, B.4
  • 25
    • 0031038185 scopus 로고    scopus 로고
    • Microglial cells induce cytotoxic effects toward colon carcinoma cells: Measurement of tumor cytotoxicity with a gamma-glutamyl transpeptidase assay
    • Murata J, Ricciardi-Castagnoli P, Dessous L'Eglise Mange P, Martin F and Juillerat-Jeanneret L: Microglial cells induce cytotoxic effects toward colon carcinoma cells: measurement of tumor cytotoxicity with a gamma-glutamyl transpeptidase assay. Int J Cancer 70(2): 169-174, 1997.
    • (1997) Int J Cancer , vol.70 , Issue.2 , pp. 169-174
    • Murata, J.1    Ricciardi-Castagnoli, P.2    Dessous L'Eglise Mange, P.3    Martin, F.4    Juillerat-Jeanneret, L.5
  • 26
    • 0030004886 scopus 로고    scopus 로고
    • Detection of a unique gamma-glutamyl transpeptidase messenger RNA species closely related to the development of hepatocellular carcinoma in humans: A new candidate for early diagnosis of hepatocellular carcinoma
    • Tsutsumi M, Sakamuro D, Takada A, Zang SC, Furukawa T and Taniguchi N: Detection of a unique gamma-glutamyl transpeptidase messenger RNA species closely related to the development of hepatocellular carcinoma in humans: a new candidate for early diagnosis of hepatocellular carcinoma. Hepatology 23(5): 1093-1097, 1996.
    • (1996) Hepatology , vol.23 , Issue.5 , pp. 1093-1097
    • Tsutsumi, M.1    Sakamuro, D.2    Takada, A.3    Zang, S.C.4    Furukawa, T.5    Taniguchi, N.6
  • 28
    • 0031156696 scopus 로고    scopus 로고
    • Elevation of glutathione and related enzyme activities in high-grade and metastatic extremity soft tissue sarcoma
    • Hochwald SN, Rose DM, Brennan MF and Burt ME: Elevation of glutathione and related enzyme activities in high-grade and metastatic extremity soft tissue sarcoma. Ann Surg Oncol 4(4): 303-309, 1997.
    • (1997) Ann Surg Oncol , vol.4 , Issue.4 , pp. 303-309
    • Hochwald, S.N.1    Rose, D.M.2    Brennan, M.F.3    Burt, M.E.4
  • 29
    • 0027406950 scopus 로고
    • Biological and enzymatic features of human melanoma clones with different invasive potential
    • Supino R, Mapelli E, Sanfilippo O and Silvestro L: Biological and enzymatic features of human melanoma clones with different invasive potential. Melanoma Res 2(5-6): 377-384, 1992. (Pubitemid 23084485)
    • (1993) Melanoma Research , vol.2 , Issue.5-6 , pp. 377-384
    • Supino, R.1    Mapelli, E.2    Sanfilippo, O.3    Silvestro, L.4
  • 31
    • 0028989695 scopus 로고
    • Gamma-glutamyl transpeptidase-cellular expression in populations of normal human mononuclear cells and patients suffering from leukemias
    • Tager M, Ittenson A, Franke A, Frey A, Gassen HG and Ansorge S: Gamma-glutamyl transpeptidase-cellular expression in populations of normal human mononuclear cells and patients suffering from leukemias. Ann Hematol 70(5): 237-242, 1995.
    • (1995) Ann Hematol , vol.70 , Issue.5 , pp. 237-242
    • Tager, M.1    Ittenson, A.2    Franke, A.3    Frey, A.4    Gassen, H.G.5    Ansorge, S.6
  • 32
    • 0027269921 scopus 로고
    • Enhancement of pulmonary metastasis formation and gamma- glutamyltranspeptidase activity in B16 melanoma induced by differentiation in vitro
    • Prezioso JA, Wang N, Duty L, Bloomer WD and Gorelik E: Enhancement of pulmonary metastasis formation and gamma-glutamyltranspeptidase activity in B16 melanoma induced by differentiation in vitro. Clin Exp Metastasis 11(3): 263-274, 1993.
    • (1993) Clin Exp Metastasis , vol.11 , Issue.3 , pp. 263-274
    • Prezioso, J.A.1    Wang, N.2    Duty, L.3    Bloomer, W.D.4    Gorelik, E.5
  • 33
    • 0036140408 scopus 로고    scopus 로고
    • Gamma-glutamyl transpeptidase overexpression increases metastatic growth of B16 melanoma cells in the mouse liver
    • Obrador E, Carretero J, Ortega A, Medina I, Rodila V, Pellicer JA and Estrema JM: Gamma-glutamyl transpeptidase overexpression increases metastatic growth of B16 melanoma cells in the mouse liver. Hepatology 35: 74-81, 2002.
    • (2002) Hepatology , vol.35 , pp. 74-81
    • Obrador, E.1    Carretero, J.2    Ortega, A.3    Medina, I.4    Rodila, V.5    Pellicer, J.A.6    Estrema, J.M.7
  • 34
    • 0022653271 scopus 로고
    • Gamma-glutamyltranspeptidase activity in human breast lesions: An unfavourable prognostic sign
    • Bard S, Noël P, Chauvin F and Quash G: Gamma-glutamyltranspeptidase activity in human breast lesions: an unfavourable prognostic sign. Br J Cancer 53(5): 637-642, 1986. (Pubitemid 16114624)
    • (1986) British Journal of Cancer , vol.53 , Issue.5 , pp. 637-642
    • Bard, S.1    Noel, P.2    Chauvin, F.3    Quash, G.4
  • 35
    • 0342683861 scopus 로고    scopus 로고
    • Gamma-glutamyl transpeptidase in normal and neoplastic prostate glands
    • Frierson HF Jr, Theodorescu D, Mills SE and Hanigan MH: Gamma-glutamyl transpeptidase in normal and neoplastic prostate glands. Mod Pathol 10(1): 1-6, 1997.
    • (1997) Mod Pathol , vol.10 , Issue.1 , pp. 1-6
    • Frierson Jr., H.F.1    Theodorescu, D.2    Mills, S.E.3    Hanigan, M.H.4
  • 37
    • 0030833785 scopus 로고    scopus 로고
    • Gamma-glutamyl transpeptidase immunoreactivity in benign and malignant breast tissue
    • Durham JR, Frierson HF Jr and Hanigan MH: Gamma-glutamyl transpeptidase immunoreactivity in benign and malignant breast tissue. Breast Cancer Res Treat 45(1): 55-62, 1997.
    • (1997) Breast Cancer Res Treat , vol.45 , Issue.1 , pp. 55-62
    • Durham, J.R.1    Frierson Jr., H.F.2    Hanigan, M.H.3
  • 38
    • 0021998639 scopus 로고
    • Gamma-glutamyl transpeptidase-its role in hepatocarcinogenesis
    • Hanigan MH and Pitot HC: Gamma-glutamyl transpeptidase-its role in hepatocarcinogenesis. Carcinogenesis 6(2): 165-172, 1985.
    • (1985) Carcinogenesis , vol.6 , Issue.2 , pp. 165-172
    • Hanigan, M.H.1    Pitot, H.C.2
  • 39
    • 0027753918 scopus 로고
    • Bidirectional membrane transport of intact glutathione in Hep G2 cells
    • Sze G, Kaplowitz N, Ookhtens M and Lu SC: Bidirectional membrane transport of intact glutathione in Hep G2 cells. Am J Physiol 265(6 Pt 1): G1128-1134, 1993.
    • (1993) Am J Physiol , vol.265 , Issue.6 PART 1
    • Sze, G.1    Kaplowitz, N.2    Ookhtens, M.3    Lu, S.C.4
  • 40
    • 0028102778 scopus 로고
    • Glutathione stimulates A549 cell proliferation in glutamine-deficient culture: The effect of glutamate supplementation
    • Kang YJ, Feng Y and Hatcher EL: Glutathione stimulates A549 cell proliferation in glutamine-deficient culture: the effect of glutamate supplementation. J Cell Physiol 161: 589-596, 1994.
    • (1994) J Cell Physiol , vol.161 , pp. 589-596
    • Kang, Y.J.1    Feng, Y.2    Hatcher, E.L.3
  • 42
    • 0026736614 scopus 로고
    • Transfection with gamma-glutamyl transpeptidase enhances recovery from glutathione depletion using extracellular glutathione
    • Rajpert-De Meyts E, Shi M, Chang M, Robison TW, Groffen J, Heisterkamp N and Forman HJ: Transfection with gamma-glutamyl transpeptidase enhances recovery from glutathione depletion using extracellular glutathione. Toxicol Appl Pharmacol 114(1): 56-62, 1992.
    • (1992) Toxicol Appl Pharmacol , vol.114 , Issue.1 , pp. 56-62
    • Rajpert-De Meyts, E.1    Shi, M.2    Chang, M.3    Robison, T.W.4    Groffen, J.5    Heisterkamp, N.6    Forman, H.J.7
  • 43
    • 0028817509 scopus 로고
    • Expression of gamma-glutamyl transpeptidase provides tumor cells with a selective growth advantage at physiologic concentrations of cyst(e)ine
    • Hanigan MH: Expression of gamma-glutamyl transpeptidase provides tumor cells with a selective growth advantage at physiologic concentrations of cyst(e)ine. Carcinogenesis 16: 181-185, 1995.
    • (1995) Carcinogenesis , vol.16 , pp. 181-185
    • Hanigan, M.H.1
  • 45
    • 0033065270 scopus 로고    scopus 로고
    • Gamma-glutamyl transpeptidase accelerates tumor growth and increases the resistance of tumors to cisplatin in vivo
    • Hanigan MH, Gallagher BC, Townsend DM and Gabarra V: Gamma-glutamyl transpeptidase accelerates tumor growth and increases the resistance of tumors to cisplatin in vivo. Carcinogenesis 20(4): 553-559, 1999.
    • (1999) Carcinogenesis , vol.20 , Issue.4 , pp. 553-559
    • Hanigan, M.H.1    Gallagher, B.C.2    Townsend, D.M.3    Gabarra, V.4
  • 47
    • 3042808682 scopus 로고    scopus 로고
    • Inhibition of gamma-glutamyl transpeptidase activity decreases intracellular cysteine levels in cervical carcinoma
    • Ruoso P and Hedley DW: Inhibition of gamma-glutamyl transpeptidase activity decreases intracellular cysteine levels in cervical carcinoma. Cancer Chemother Pharmacol 54(1): 49-56, 2004.
    • (2004) Cancer Chemother Pharmacol , vol.54 , Issue.1 , pp. 49-56
    • Ruoso, P.1    Hedley, D.W.2
  • 49
    • 0031156696 scopus 로고    scopus 로고
    • Elevation of glutathione and related enzyme activities in high-grade and metastatic extremity soft tissue sarcoma
    • Hochwald SN, Rose DM, Brennan MF and Burt ME: Elevation of glutathione and related enzyme activities in high-grade and metastatic extremity soft tissue sarcoma. Ann Surg Oncol 4(4): 303-309, 1997.
    • (1997) Ann Surg Oncol , vol.4 , Issue.4 , pp. 303-309
    • Hochwald, S.N.1    Rose, D.M.2    Brennan, M.F.3    Burt, M.E.4
  • 50
    • 0026594392 scopus 로고
    • High resistance to cisplatin in human ovarian cancer cell lines is associated with marked increase of glutathione synthesis
    • Godwin AK, Meister A, O'Dwyer PJ, Huang CS, Hamilton TC and Anderson ME: High resistance to cisplatin in human ovarian cancer cell lines is associated with marked increase of glutathione synthesis. Proc Natl Acad Sci USA 89(7): 3070-3074, 1992.
    • (1992) Proc Natl Acad Sci USA , vol.89 , Issue.7 , pp. 3070-3074
    • Godwin, A.K.1    Meister, A.2    O'Dwyer, P.J.3    Huang, C.S.4    Hamilton, T.C.5    Anderson, M.E.6
  • 51
    • 0037789550 scopus 로고    scopus 로고
    • Cisplatin induced gamma-glutamyltransferase up-regulation, hypertrophy and differentiation in astrocytic glioma cells in culture
    • Mares V, Lisa V, Malik R, Kozakova H and Sedo A: Cisplatin induced gamma-glutamyltransferase up-regulation, hypertrophy and differentiation in astrocytic glioma cells in culture. Histol Histopathol 18: 687-693, 2003. (Pubitemid 36773212)
    • (2003) Histology and Histopathology , vol.18 , Issue.3 , pp. 687-693
    • Mares, V.1    Lisa, V.2    Malik, R.3    Kozakova, H.4    Sedo, A.5
  • 52
    • 0023942684 scopus 로고
    • Glutathione and glutathione-dependent enzymes in ovarian adenocarcinoma cell lines derived from a patient before and after the onset of drug resistance: Intrinsic differences and cell cycle effects
    • Lewis AL, Hayes JD and Wolf CR: Glutathione and glutathione-dependent enzymes in ovarian adenocarcinoma cell lines derived from a patient before and after the onset of drug resistance: intrinsic differences and cell cycle effects. Carcinogenesis 9: 1283-1287, 1988.
    • (1988) Carcinogenesis , vol.9 , pp. 1283-1287
    • Lewis, A.L.1    Hayes, J.D.2    Wolf, C.R.3
  • 53
    • 14844286405 scopus 로고    scopus 로고
    • Acceleration of glutathione efflux and inhibition of gamma- glutamyltranspeptidase sensitize metastatic B16 melanoma cells to endothelium-induced cytotoxicity
    • Benlloch M, Ortega A, Ferrer P, Segarra R, Obrador E, Asensi M, Carretero J and Estrela JM: Acceleration of glutathione efflux and inhibition of gamma-glutamyltranspeptidase sensitize metastatic B16 melanoma cells to endothelium-induced cytotoxicity. J Biol Chem 280: 6950-6959, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 6950-6959
    • Benlloch, M.1    Ortega, A.2    Ferrer, P.3    Segarra, R.4    Obrador, E.5    Asensi, M.6    Carretero, J.7    Estrela, J.M.8
  • 54
    • 0028670408 scopus 로고
    • Increased expression of gamma-glutamyl transpeptidase in transfected tumor cells and its relationship to drug sensitivity
    • Bailey HH, Gipp JJ and Mulcahy RT: Increased expression of gamma-glutamyl transpeptidase in transfected tumor cells and its relationship to drug sensitivity. Cancer Lett 87: 163-170, 1994.
    • (1994) Cancer Lett , vol.87 , pp. 163-170
    • Bailey, H.H.1    Gipp, J.J.2    Mulcahy, R.T.3
  • 55
    • 0035830919 scopus 로고    scopus 로고
    • Expression of gamma-glutamyl transpeptidase protects ramos B cells from oxidation-induced cell death
    • Karp DR, Shimooku K and Lipsky PE: Expression of gamma-glutamyl transpeptidase protects ramos B cells from oxidation-induced cell death. J Biol Chem 276(6): 3798-3804, 2001.
    • (2001) J Biol Chem , vol.276 , Issue.6 , pp. 3798-3804
    • Karp, D.R.1    Shimooku, K.2    Lipsky, P.E.3
  • 58
    • 0037138424 scopus 로고    scopus 로고
    • Extracellular thiol metabolism in clones of human metastatic melanoma with different gamma-glutamyl transpeptidase expression: Implications for cell response to platinum-based drugs
    • Paolicchi A, Lorenzini E, Perego P, Supino R, Zunino F, Comporti M and Pompella A: Extracellular thiol metabolism in clones of human metastatic melanoma with different gamma-glutamyl transpeptidase expression: implications for cell response to platinum-based drugs. Int J Cancer 97(6): 740-745, 2002.
    • (2002) Int J Cancer , vol.97 , Issue.6 , pp. 740-745
    • Paolicchi, A.1    Lorenzini, E.2    Perego, P.3    Supino, R.4    Zunino, F.5    Comporti, M.6    Pompella, A.7
  • 59
    • 0031800081 scopus 로고    scopus 로고
    • Ovarian cancer cisplatin-resistant cell lines: Multiple changes including collateral sensitivity to Taxol
    • Perego P, Romanelli S, Carenini N, Magnani I, Leone R, Bonetti A, Paolicchi A and Zunino F: Ovarian cancer cisplatin-resistant cell lines: multiple changes including collateral sensitivity to Taxol. Ann Oncol 9(4): 423-430, 1998.
    • (1998) Ann Oncol , vol.9 , Issue.4 , pp. 423-430
    • Perego, P.1    Romanelli, S.2    Carenini, N.3    Magnani, I.4    Leone, R.5    Bonetti, A.6    Paolicchi, A.7    Zunino, F.8
  • 60
    • 0028909965 scopus 로고
    • The role of the glutathione-dependent system in tumor sensitivity to cisplatin: A study of human tumor xenografts
    • Pratesi G, Dal Bo L, Paolicchi A, Tonarelli P, Tongiani R and Zunino F: The role of the glutathione-dependent system in tumor sensitivity to cisplatin: a study of human tumor xenografts. Ann Oncol 6: 283-289, 1995.
    • (1995) Ann Oncol , vol.6 , pp. 283-289
    • Pratesi, G.1    Dal Bo, L.2    Paolicchi, A.3    Tonarelli, P.4    Tongiani, R.5    Zunino, F.6
  • 61
    • 0032867954 scopus 로고    scopus 로고
    • Human germ cell tumours: Expression of gamma-glutamyl transpeptidase and sensitivity to cisplatin
    • Hanigan MH, Frierson HF Jr, Abeler VM, Kaern J and Taylor PT Jr: Human germ cell tumours: expression of gamma-glutamyl transpeptidase and sensitivity to cisplatin. Br J Cancer 81(1): 75-79, 1999.
    • (1999) Br J Cancer , vol.81 , Issue.1 , pp. 75-79
    • Hanigan, M.H.1    Frierson Jr., H.F.2    Abeler, V.M.3    Kaern, J.4    Taylor Jr., P.T.5
  • 62
    • 0033975256 scopus 로고    scopus 로고
    • Sulfur-containing amino acids decrease cisplatin cytotoxicity and uptake in renal tubule epithelial cell lines
    • Kröning R, Lichtenstein AK and Nagami GT: Sulfur-containing amino acids decrease cisplatin cytotoxicity and uptake in renal tubule epithelial cell lines. Cancer Chemother Pharmacol 45: 43-49, 2000. (Pubitemid 30099714)
    • (2000) Cancer Chemotherapy and Pharmacology , vol.45 , Issue.1 , pp. 43-49
    • Kroning, R.1    Lichtenstein, A.K.2    Nagami, G.T.3
  • 63
    • 27644543909 scopus 로고    scopus 로고
    • Cisplatin interaction with cysteine and methionine, a theoretical DFT study
    • Zimmermann T, Zeizinger M and Burda JV: Cisplatin interaction with cysteine and methionine, a theoretical DFT study. J Inorg Biochem 99(11): 2184-2196, 2005.
    • (2005) J Inorg Biochem , vol.99 , Issue.11 , pp. 2184-2196
    • Zimmermann, T.1    Zeizinger, M.2    Burda, J.V.3
  • 65
    • 33646832741 scopus 로고    scopus 로고
    • Oxaliplatin degradation in the presence of important biological sulphur-containing compounds and plasma ultrafiltrate
    • Jerremalm E, Wallin I, Yachnin J and Ehrsson H: Oxaliplatin degradation in the presence of important biological sulphur-containing compounds and plasma ultrafiltrate. Eur J Pharm Sci 28(4): 278-283, 2006.
    • (2006) Eur J Pharm Sci , vol.28 , Issue.4 , pp. 278-283
    • Jerremalm, E.1    Wallin, I.2    Yachnin, J.3    Ehrsson, H.4
  • 67
    • 0024424268 scopus 로고
    • Effect of pH on mutagenesis by thiols in Salmonella typhimurium TA102
    • Stark AA, Arad A, Siskindovich S, Pagano DA and Zeiger E: Effect of pH on mutagenesis by thiols in Salmonella typhimurium TA102. Mutat Res 224(1): 89-94, 1989.
    • (1989) Mutat Res , vol.224 , Issue.1 , pp. 89-94
    • Stark, A.A.1    Arad, A.2    Siskindovich, S.3    Pagano, D.A.4    Zeiger, E.5
  • 69
    • 0141869677 scopus 로고    scopus 로고
    • Cisplatin nephrotoxicity
    • Arany I and Safirstein RL: Cisplatin nephrotoxicity. Semin Nephrol 23(5): 460-464, 2003.
    • (2003) Semin Nephrol , vol.23 , Issue.5 , pp. 460-464
    • Arany, I.1    Safirstein, R.L.2
  • 70
    • 0042433316 scopus 로고    scopus 로고
    • Role of cysteine 5-conjugate beta-lyase in the metabolism of cisplatin
    • Zhang L and Hanigan MH: Role of cysteine 5-conjugate beta-lyase in the metabolism of cisplatin. J Pharmacol Exp Ther 306(3): 988-994, 2003.
    • (2003) J Pharmacol Exp Ther , vol.306 , Issue.3 , pp. 988-994
    • Zhang, L.1    Hanigan, M.H.2
  • 71
    • 0035149381 scopus 로고    scopus 로고
    • Gamma-glutamyl transpeptidase-deficient mice are resistant to the nephrotoxic effects of cisplatin
    • Hanigan MH, Lykissa ED, Townsend DM, Ou CN, Barrios R and Lieberman MW: Gamma-glutamyl transpeptidase-deficient mice are resistant to the nephrotoxic effects of cisplatin. Am J Pathol 159(5): 1889-1894, 2001.
    • (2001) Am J Pathol , vol.159 , Issue.5 , pp. 1889-1894
    • Hanigan, M.H.1    Lykissa, E.D.2    Townsend, D.M.3    Ou, C.N.4    Barrios, R.5    Lieberman, M.W.6
  • 72
    • 0028171462 scopus 로고
    • Inhibition of gamma-glutamyl transpeptidase activity by acivicin in vivo protects the kidney from cisplatin-induced toxicity
    • Hanigan MH, Gallagher BC, Taylor PT Jr and Large MK: Inhibition of gamma-glutamyl transpeptidase activity by acivicin in vivo protects the kidney from cisplatin-induced toxicity. Cancer Res 54(22): 5925-5929, 1994.
    • (1994) Cancer Res , vol.54 , Issue.22 , pp. 5925-5929
    • Hanigan, M.H.1    Gallagher, B.C.2    Taylor Jr., P.T.3    Large, M.K.4
  • 73
    • 0036139415 scopus 로고    scopus 로고
    • Inhibition of gamma-glutamyl transpeptidase or cysteine 5-conjugate beta-lyase activity blocks the nephrotoxicity of cisplatin in mice
    • Townsend DM and Hanigan MH: Inhibition of gamma-glutamyl transpeptidase or cysteine 5-conjugate beta-lyase activity blocks the nephrotoxicity of cisplatin in mice. J Pharmacol Exp Ther 300(1): 142-148, 2002.
    • (2002) J Pharmacol Exp Ther , vol.300 , Issue.1 , pp. 142-148
    • Townsend, D.M.1    Hanigan, M.H.2
  • 74
    • 46449123870 scopus 로고    scopus 로고
    • Cisplatin nephrotoxicity is mediated by gamma-glutamyltranspeptidase, not via a C-S lyase governed biotransformation pathway
    • Wainford RD, Weaver RJ, Stewart KN, Brown P and Hawksworth GM: Cisplatin nephrotoxicity is mediated by gamma-glutamyltranspeptidase, not via a C-S lyase governed biotransformation pathway. Toxicology 249(2-3): 184-193, 2008.
    • (2008) Toxicology , vol.249 , Issue.2-3 , pp. 184-193
    • Wainford, R.D.1    Weaver, R.J.2    Stewart, K.N.3    Brown, P.4    Hawksworth, G.M.5
  • 75
    • 0024334978 scopus 로고
    • Protective effect of reduced glutathione against cisplatin-induced renal and systemic toxicity and its influence on the therapeutic activity of the antitumor drug
    • Zunino F, Pratesi G, Micheloni A, Cavalletti E, Sala F and Tofanetti O: Protective effect of reduced glutathione against cisplatin-induced renal and systemic toxicity and its influence on the therapeutic activity of the antitumor drug. Chem Biol Interact 70(1-2): 89-101, 1989.
    • (1989) Chem Biol Interact , vol.70 , Issue.1-2 , pp. 89-101
    • Zunino, F.1    Pratesi, G.2    Micheloni, A.3    Cavalletti, E.4    Sala, F.5    Tofanetti, O.6
  • 76
    • 0029119416 scopus 로고
    • Characterization of cisplatin-glutathione adducts by liquid chromatography-mass spectrometry. Evidence for their formation in vitro but not in vivo after concomitant administration of cisplatin and glutathione to rats and cancer patients
    • Bernareggi A, Torti L, Facino RM, Carini M, Depta G, Casetta B, Farrell N, Spadacini S, Ceserani R and Tognella S: Characterization of cisplatin-glutathione adducts by liquid chromatography-mass spectrometry. Evidence for their formation in vitro but not in vivo after concomitant administration of cisplatin and glutathione to rats and cancer patients. J Chromatogr B Biomed Appl 669(2): 247-263, 1995.
    • (1995) J Chromatogr B Biomed Appl , vol.669 , Issue.2 , pp. 247-263
    • Bernareggi, A.1    Torti, L.2    Facino, R.M.3    Carini, M.4    Depta, G.5    Casetta, B.6    Farrell, N.7    Spadacini, S.8    Ceserani, R.9    Tognella, S.10
  • 77
    • 0012971643 scopus 로고
    • Translocation of intracellular glutathione to membrane-bound gamma-glutamyltranspeptidase as a discrete step in the gamma-glutamyl cycle: Glutathionuria after inhibition of transpeptidase
    • Griffith OW and Meister A: Translocation of intracellular glutathione to membrane-bound gamma-glutamyltranspeptidase as a discrete step in the gamma-glutamyl cycle: glutathionuria after inhibition of transpeptidase. Proc Natl Acad Sci USA 76: 268-272, 1979.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 268-272
    • Griffith, O.W.1    Meister, A.2
  • 79
    • 0003083299 scopus 로고
    • Metabolism and transport of glutathione and other gamma-glutamyl compounds
    • Larsson A, Orrenius S, Holmgren A and Mannervik B (ed.). New York: Raven Press
    • Meister A: Metabolism and transport of glutathione and other gamma-glutamyl compounds. In: Larsson A, Orrenius S, Holmgren A and Mannervik B (ed.). Functions of Glutathione: Biochemical, Toxicological and Clinical Aspects. New York: Raven Press, pp. 1-22, 1983.
    • (1983) Functions of Glutathione: Biochemical, Toxicological and Clinical Aspects , pp. 1-22
    • Meister, A.1
  • 80
    • 0023183746 scopus 로고
    • Characterization of the reactions of platinum antitumor agents with biologic and nonbiologic sulfur-containing nucleophiles
    • Dedon PC and Borch RF: Characterization of the reactions of platinum antitumor agents with biologic and nonbiologic sulfur-containing nucleophiles. Biochem Pharmacol 36(12): 1955-1964, 1987.
    • (1987) Biochem Pharmacol , vol.36 , Issue.12 , pp. 1955-1964
    • Dedon, P.C.1    Borch, R.F.2
  • 81
    • 0027305406 scopus 로고
    • Glutathione-associated cis-diamminedichloroplatinum(II) metabolism and ATP-dependent efflux from leukemia cells. Molecular characterization of glutathione-platinum complex and its biological significance
    • Ishikawa T and Ali-Osman F: Glutathione-associated cis- diamminedichloroplatinum(II) metabolism and ATP-dependent efflux from leukemia cells. Molecular characterization of glutathione-platinum complex and its biological significance. J Biol Chem 268(27): 20116-20125, 1993.
    • (1993) J Biol Chem , vol.268 , Issue.27 , pp. 20116-20125
    • Ishikawa, T.1    Ali-Osman, F.2
  • 83
    • 0037518294 scopus 로고    scopus 로고
    • High pressure liquid chromatography and mass spectrometry characterization of the nephrotoxic biotransformation products of cisplatin
    • Townsend DM, Marto JA, Deng M, Macdonald TJ and Hanigan MH: High pressure liquid chromatography and mass spectrometry characterization of the nephrotoxic biotransformation products of Cisplatin. Drug Metab Dispos 31(6): 705-713, 2003. (Pubitemid 36617657)
    • (2003) Drug Metabolism and Disposition , vol.31 , Issue.6 , pp. 705-713
    • Townsend, D.M.1    Marto, J.A.2    Deng, M.3    MacDonald, T.J.4    Hanigan, M.H.5
  • 85
    • 0028021850 scopus 로고
    • Thiol-mediated NTA-Fe(III) reduction and lipid peroxidation
    • Spear N and Aust SD: Thiol-mediated NTA-Fe(III) reduction and lipid peroxidation. Arch Biochem Biophys 312(1): 198-202, 1994.
    • (1994) Arch Biochem Biophys , vol.312 , Issue.1 , pp. 198-202
    • Spear, N.1    Aust, S.D.2
  • 86
    • 0028343817 scopus 로고
    • Localization of oxidative damage by a glutathione-gamma-glutamyl transpeptidase system in preneoplastic lesions in sections of livers from carcinogen-treated rats
    • Stark AA, Russel JJ, Langenbach R, Pagano DA, Zeiger E and Huberman E: Localization of oxidative damage by a glutathione-gamma-glutamyl transpeptidase system in preneoplastic lesions in sections of livers from carcinogen-treated rats. Carcinogenesis 15: 343-348, 1994. (Pubitemid 24121672)
    • (1994) Carcinogenesis , vol.15 , Issue.2 , pp. 343-348
    • Stark, A.-A.1    Russell, J.J.2    Langenbach, R.3    Pagano, D.A.4    Zeiger, E.5    Huberman, E.6
  • 87
    • 0023917659 scopus 로고
    • Glutathione mutagenesis in Salmonella typhimurium is a gamma-glutamyltranspeptidase-enhanced process involving active oxygen species
    • Stark AA, Zeiger E and Pagano DA: Glutathione mutagenesis in Salmonella typhimurium is a gamma-glutamyltranspeptidase-enhanced process involving active oxygen species. Carcinogenesis 9(5): 771-777, 1988.
    • (1988) Carcinogenesis , vol.9 , Issue.5 , pp. 771-777
    • Stark, A.A.1    Zeiger, E.2    Pagano, D.A.3
  • 88
    • 0031056695 scopus 로고    scopus 로고
    • Role of copper and ceruloplasmin in oxidative mutagenesis induced by the glutathione-gamma-glutamyl transpeptidase system and by other thiols
    • Stark AA and Glass GA: Role of copper and ceruloplasmin in oxidative mutagenesis induced by the glutathione-gamma-glutamyl transpeptidase system and by other thiols. Environ Mol Mutagen 29(1): 63-72, 1997.
    • (1997) Environ Mol Mutagen , vol.29 , Issue.1 , pp. 63-72
    • Stark, A.A.1    Glass, G.A.2
  • 90
    • 0032212468 scopus 로고    scopus 로고
    • Gamma-glutamyltransferase dependent generation of reactive oxygen species from a glutathione/transferrin system
    • Drozdz R, Parmentier C, Hachad H, Leroy P, Siest G and Wellman M: Gamma-glutamyltransferase dependent generation of reactive oxygen species from a glutathione/transferrin system. Free Radic Biol Med 25(7): 786-792, 1998.
    • (1998) Free Radic Biol Med , vol.25 , Issue.7 , pp. 786-792
    • Drozdz, R.1    Parmentier, C.2    Hachad, H.3    Leroy, P.4    Siest, G.5    Wellman, M.6
  • 91
    • 0032905740 scopus 로고    scopus 로고
    • Hydrogen peroxide produced during gamma-glutamyl transpeptidase activity is involved in prevention of apoptosis and maintainance of proliferation in U937 cells
    • Del Bello B, Paolicchi A, Comporti M, Pompella A and Maellaro E: Hydrogen peroxide produced during gamma-glutamyl transpeptidase activity is involved in prevention of apoptosis and maintainance of proliferation in U937 cells. FASEB J 13(1): 69-79, 1999.
    • (1999) FASEB J , vol.13 , Issue.1 , pp. 69-79
    • Del Bello, B.1    Paolicchi, A.2    Comporti, M.3    Pompella, A.4    Maellaro, E.5
  • 93
    • 0029740522 scopus 로고    scopus 로고
    • Selective colocalization of lipid peroxidation and protein thiol loss in chemically induced hepatic preneoplastic lesions: The role of gamma-glutamyltranspeptidase activity
    • Pompella A, Paolicchi A, Dominici S, Comporti M and Tongiani R: Selective colocalization of lipid peroxidation and protein thiol loss in chemically induced hepatic preneoplastic lesions: the role of gamma-glutamyltranspeptidase activity. Histochem Cell Biol 106(3): 275-282, 1996.
    • (1996) Histochem Cell Biol , vol.106 , Issue.3 , pp. 275-282
    • Pompella, A.1    Paolicchi, A.2    Dominici, S.3    Comporti, M.4    Tongiani, R.5
  • 94
    • 0031018546 scopus 로고    scopus 로고
    • Gamma-glutamyl transpeptidase-dependent lipid peroxidation in isolated hepatocytes and HepG2 hepatoma cells
    • Paolicchi A, Tongiani R, Tonarelli P, Comporti M and Pompella A: Gamma-glutamyl transpeptidase-dependent lipid peroxidation in isolated hepatocytes and HepG2 hepatoma cells. Free Radic Biol Med 22(5): 853-860, 1997.
    • (1997) Free Radic Biol Med , vol.22 , Issue.5 , pp. 853-860
    • Paolicchi, A.1    Tongiani, R.2    Tonarelli, P.3    Comporti, M.4    Pompella, A.5
  • 96
    • 70349152500 scopus 로고    scopus 로고
    • Membrane gamma-glutamyl transferase activity promotes iron-dependent oxidative DNA damage in melanoma cells
    • Corti A, Duarte TL, Giommarelli C, De Tata V, Paolicchi A, Jones GD and Pompella A: Membrane gamma-glutamyl transferase activity promotes iron-dependent oxidative DNA damage in melanoma cells. Mutat Res 669(1-2): 112-121, 2009
    • (2009) Mutat Res , vol.669 , Issue.1-2 , pp. 112-121
    • Corti, A.1    Duarte, T.L.2    Giommarelli, C.3    De Tata, V.4    Paolicchi, A.5    Jones, G.D.6    Pompella, A.7
  • 97
    • 7444264606 scopus 로고    scopus 로고
    • Plasma membrane gamma-glutamyltransferase activity facilitates the uptake of vitamin C in melanoma cells
    • Corti A, Raggi C, Franzini M, Paolicchi A, Pompella A and Casini AF: Plasma membrane gamma-glutamyltransferase activity facilitates the uptake of vitamin C in melanoma cells. Free Radic Biol Med 37(11): 1906-1915, 2004.
    • (2004) Free Radic Biol Med , vol.37 , Issue.11 , pp. 1906-1915
    • Corti, A.1    Raggi, C.2    Franzini, M.3    Paolicchi, A.4    Pompella, A.5    Casini, A.F.6
  • 98
    • 0031039138 scopus 로고    scopus 로고
    • Promotion of glutathione-gamma-glutamyl transpeptidase-dependent lipid peroxidation by copper and ceruloplasmin: The requirement for iron and the effects of antioxidants and antioxidant enzymes
    • Glass GA and Stark AA: Promotion of glutathione-gamma-glutamyl transpeptidase-dependent lipid peroxidation by copper and ceruloplasmin: the requirement for iron and the effects of antioxidants and antioxidant enzymes. Environ Mol Mutagen 29(1): 73-80, 1997.
    • (1997) Environ Mol Mutagen , vol.29 , Issue.1 , pp. 73-80
    • Glass, G.A.1    Stark, A.A.2
  • 99
    • 2942521653 scopus 로고    scopus 로고
    • Possible role of membrane gamma-glutamyltransferase activity in the facilitation of transferrin-dependent and -independent iron uptake by cancer cells
    • Dominici S, Pieri L, Comporti M and Pompella A: Possible role of membrane gamma-glutamyltransferase activity in the facilitation of transferrin-dependent and -independent iron uptake by cancer cells. Cancer Cell Int 3(1): 7-14, 2003.
    • (2003) Cancer Cell Int , vol.3 , Issue.1 , pp. 7-14
    • Dominici, S.1    Pieri, L.2    Comporti, M.3    Pompella, A.4
  • 100
    • 0028900690 scopus 로고
    • Persistent oxidative stress in cancer
    • Toyokuni S, Okamoto K, Yodoi J and Hiai H: Persistent oxidative stress in cancer. FEBS Lett 358(1): 1-3, 1995.
    • (1995) FEBS Lett , vol.358 , Issue.1 , pp. 1-3
    • Toyokuni, S.1    Okamoto, K.2    Yodoi, J.3    Hiai, H.4
  • 101
    • 0032100603 scopus 로고    scopus 로고
    • Redox signaling and the emerging therapeutic potential of thiol antioxidants
    • Sen CK: Redox signaling and the emerging therapeutic potential of thiol antioxidants. Biochem Pharmacol 55(11): 1747-1758, 1998.
    • (1998) Biochem Pharmacol , vol.55 , Issue.11 , pp. 1747-1758
    • Sen, C.K.1
  • 102
    • 0032488513 scopus 로고    scopus 로고
    • Recent trends in glutathione biochemistry-glutathione-protein interactions: A molecular link between oxidative stress and cell proliferation?
    • Cotgreave IA and Gerdes RG: Recent trends in glutathione biochemistry-glutathione-protein interactions: a molecular link between oxidative stress and cell proliferation? Biochem Biophys Res Commun 242(1): 1-9, 1998.
    • (1998) Biochem Biophys Res Commun , vol.242 , Issue.1 , pp. 1-9
    • Cotgreave, I.A.1    Gerdes, R.G.2
  • 104
    • 22044437820 scopus 로고    scopus 로고
    • The S-thiolating activity of membrane gamma-glutamyltransferase: Formation of cysteinyl-glycine mixed disulfides with cellular proteins and in the cell microenvironment
    • Corti A, Paolicchi A, Franzini M, Dominici S, Casini AF and Pompella A: The S-thiolating activity of membrane gamma-glutamyltransferase: formation of cysteinyl-glycine mixed disulfides with cellular proteins and in the cell microenvironment. Antioxid Redox Signal 7(7-8): 911-918, 2005.
    • (2005) Antioxid Redox Signal , vol.7 , Issue.7-8 , pp. 911-918
    • Corti, A.1    Paolicchi, A.2    Franzini, M.3    Dominici, S.4    Casini, A.F.5    Pompella, A.6
  • 105
    • 15044359739 scopus 로고    scopus 로고
    • Endogenous oxidative stress induces distinct redox forms of tumor necrosis factor receptor-1 in melanoma cells
    • Dominici S, Pieri L, Paolicchi A, De Tata V, Zunino F and Pompella A: Endogenous oxidative stress induces distinct redox forms of tumor necrosis factor receptor-1 in melanoma cells. Ann NY Acad Sci 1030: 62-68, 2004.
    • (2004) Ann NY Acad Sci , vol.1030 , pp. 62-68
    • Dominici, S.1    Pieri, L.2    Paolicchi, A.3    De Tata, V.4    Zunino, F.5    Pompella, A.6
  • 107
    • 0142041923 scopus 로고    scopus 로고
    • Redox modulation of NF-κB nuclear translocation and DNA binding in metastatic melanoma - The role of endogenous and gamma-glutamyltransferase- dependent oxidative stress
    • Dominici S, Visvikis A, Pieri L, Paolicchi A, Valentini M, Comporti M and Pompella A: Redox modulation of NF-κB nuclear translocation and DNA binding in metastatic melanoma - the role of endogenous and gamma- glutamyltransferase-dependent oxidative stress. Tumori 89: 428-435, 2003.
    • (2003) Tumori , vol.89 , pp. 428-435
    • Dominici, S.1    Visvikis, A.2    Pieri, L.3    Paolicchi, A.4    Valentini, M.5    Comporti, M.6    Pompella, A.7
  • 110
  • 111
    • 0030970686 scopus 로고    scopus 로고
    • The cell-specific antiproliferative effect of reduced glutathione is mediated by gamma-glutamyl transpeptidase dependent extracellular prooxidant reactions
    • Perego P, Paolicchi A, Pompella A, Carenini N, Romanelli S and Zunino F: The cell-specific antiproliferative effect of reduced glutathione is mediated by gamma-glutamyl transpeptidase dependent extracellular prooxidant reactions. Int J Cancer 71: 246-250, 1997.
    • (1997) Int J Cancer , vol.71 , pp. 246-250
    • Perego, P.1    Paolicchi, A.2    Pompella, A.3    Carenini, N.4    Romanelli, S.5    Zunino, F.6
  • 112
    • 40849119480 scopus 로고    scopus 로고
    • Cellular response to oxidative stress and ascorbic acid in melanoma cells overexpressing gamma-glutamyltransferase
    • Giommarelli C, Corti A, Supino R, Favini E, Paolicchi A, Pompella A and Zunino F: Cellular response to oxidative stress and ascorbic acid in melanoma cells overexpressing gamma-glutamyltransferase. Eur J Cancer 44(5): 750-759, 2008.
    • (2008) Eur J Cancer , vol.44 , Issue.5 , pp. 750-759
    • Giommarelli, C.1    Corti, A.2    Supino, R.3    Favini, E.4    Paolicchi, A.5    Pompella, A.6    Zunino, F.7
  • 113
    • 0042033156 scopus 로고
    • Serine-borate complex as a transition-state inhibitor of gamma-glutamyl transpeptidase
    • Tate SS and Meister A: Serine-borate complex as a transition-state inhibitor of gamma-glutamyl transpeptidase. Proc Natl Acad Sci USA 75(10): 4806-4809, 1978.
    • (1978) Proc Natl Acad Sci USA , vol.75 , Issue.10 , pp. 4806-4809
    • Tate, S.S.1    Meister, A.2
  • 114
    • 0018891998 scopus 로고
    • The inhibition of gamma-glutamyl transpeptidase from human pancreatic carcinoma cells by (alpha S,5S)-alpha-amino-3-chloro-4,5-dihydro-5- isoxazoleacetic acid (AT-125; NSC-163501)
    • Allen L, Meck R and Yunis A: The inhibition of gamma-glutamyl transpeptidase from human pancreatic carcinoma cells by (alpha S,5S)-alpha-amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid (AT-125; NSC-163501). Res Commun Chem Pathol Pharmacol 27(1): 175-182, 1980.
    • (1980) Res Commun Chem Pathol Pharmacol , vol.27 , Issue.1 , pp. 175-182
    • Allen, L.1    Meck, R.2    Yunis, A.3
  • 115
    • 0035862175 scopus 로고    scopus 로고
    • Development and evaluation of a boronate inhibitor of gamma-glutamyl transpeptidase
    • London RE and Gabel SA: Development and evaluation of a boronate inhibitor of gamma-glutamyl transpeptidase. Arch Biochem Biophys 385(2): 250-258, 2001.
    • (2001) Arch Biochem Biophys , vol.385 , Issue.2 , pp. 250-258
    • London, R.E.1    Gabel, S.A.2
  • 116
    • 2942585593 scopus 로고    scopus 로고
    • Synthesis of S-alkyl L-homocysteine analogues of glutathione and their kinetic studies with gamma-glutamyl transpeptidase
    • Lherbet C, Gravel C and Keillor JW: Synthesis of S-alkyl L-homocysteine analogues of glutathione and their kinetic studies with gamma-glutamyl transpeptidase. Bioorg Med Chem Lett 14(13): 3451-3455, 2004.
    • (2004) Bioorg Med Chem Lett , vol.14 , Issue.13 , pp. 3451-3455
    • Lherbet, C.1    Gravel, C.2    Keillor, J.W.3
  • 117
    • 33846845012 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of gamma-phosphono diester analogues of glutamate as highly potent inhibitors and active site probes of gamma-glutamyl transpeptidase
    • Han L, Hiratake J, Kamiyama A and Sakata K: Design, synthesis, and evaluation of gamma-phosphono diester analogues of glutamate as highly potent inhibitors and active site probes of gamma-glutamyl transpeptidase. Biochemistry 46(5): 1432-1447, 2007.
    • (2007) Biochemistry , vol.46 , Issue.5 , pp. 1432-1447
    • Han, L.1    Hiratake, J.2    Kamiyama, A.3    Sakata, K.4
  • 118
    • 0025232412 scopus 로고
    • Metabolism and action of amino acid analog anticancer agents
    • Ahluwalia GS, Grem JL, Hao Z and Cooney DA: Metabolism and action of amino acid analog anticancer agents. Pharmacol Ther 46(2): 243-271, 1990.
    • (1990) Pharmacol Ther , vol.46 , Issue.2 , pp. 243-271
    • Ahluwalia, G.S.1    Grem, J.L.2    Hao, Z.3    Cooney, D.A.4
  • 119
    • 0025296425 scopus 로고
    • Cytotoxic mechanisms of glutamine antagonists in mouse L1210 leukemia
    • Lyons SD, Sant ME and Christopherson RI: Cytotoxic mechanisms of glutamine antagonists in mouse L1210 leukemia. J Biol Chem 265(19): 11377-11381, 1990. (Pubitemid 20200150)
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.19 , pp. 11377-11381
    • Lyons, S.D.1    Sant, M.E.2    Christopherson, R.I.3
  • 121
    • 66149155033 scopus 로고    scopus 로고
    • A novel, species-specific class of uncompetitive inhibitors of gamma-glutamyl transpeptidase
    • King JB, West MB, Cook PF and Hanigan MH: A novel, species-specific class of uncompetitive inhibitors of gamma-glutamyl transpeptidase. J Biol Chem 284(14): 9059-9065, 2009.
    • (2009) J Biol Chem , vol.284 , Issue.14 , pp. 9059-9065
    • King, J.B.1    West, M.B.2    Cook, P.F.3    Hanigan, M.H.4
  • 122
    • 67349181337 scopus 로고    scopus 로고
    • Gamma-glutamyltransferase-dependent resistance to arsenic trioxide in melanoma cells and cellular sensitization by ascorbic acid
    • Giommarelli C, Corti A, Supino R, Favini E, Paolicchi A, Pompella A and Zunino F: Gamma-glutamyltransferase-dependent resistance to arsenic trioxide in melanoma cells and cellular sensitization by ascorbic acid. Free Radic Biol Med 46(11): 1516-1526, 2009.
    • (2009) Free Radic Biol Med , vol.46 , Issue.11 , pp. 1516-1526
    • Giommarelli, C.1    Corti, A.2    Supino, R.3    Favini, E.4    Paolicchi, A.5    Pompella, A.6    Zunino, F.7
  • 123
    • 0028307739 scopus 로고
    • Hypoxia and drug resistance
    • Teicher BA: Hypoxia and drug resistance. Cancer Metastasis Rev 13(2): 139-168, 1994.
    • (1994) Cancer Metastasis Rev , vol.13 , Issue.2 , pp. 139-168
    • Teicher, B.A.1
  • 124
    • 45549089561 scopus 로고    scopus 로고
    • Chemosensitization of cancer by nitric oxide
    • Sullivan R and Graham CH: Chemosensitization of cancer by nitric oxide. Curr Pharm Des 14(11): 1113-1123, 2008.
    • (2008) Curr Pharm des , vol.14 , Issue.11 , pp. 1113-1123
    • Sullivan, R.1    Graham, C.H.2
  • 126
    • 60749093948 scopus 로고    scopus 로고
    • Growth inhibition and chemosensitization of exogenous nitric oxide released from NONOates in glioma cells in vitro
    • Weyerbrock A, Baumer B and Papazoglou A: Growth inhibition and chemosensitization of exogenous nitric oxide released from NONOates in glioma cells in vitro. J Neurosurg 110(1): 128-136, 2009.
    • (2009) J Neurosurg , vol.110 , Issue.1 , pp. 128-136
    • Weyerbrock, A.1    Baumer, B.2    Papazoglou, A.3
  • 128
    • 67649810742 scopus 로고    scopus 로고
    • Exogenous vs. endogenous gamma-glutamyltransferase activity: Implications for the specific determination of S-nitrosoglutathione in biological samples
    • Bramanti E, Angeli V, Franzini M, Vecoli C, Baldassini R, Paolicchi A, Barsacchi R and Pompella A: Exogenous vs. endogenous gamma-glutamyltransferase activity: Implications for the specific determination of S-nitrosoglutathione in biological samples. Arch Biochem Biophys 487: 146-152, 2009.
    • (2009) Arch Biochem Biophys , vol.487 , pp. 146-152
    • Bramanti, E.1    Angeli, V.2    Franzini, M.3    Vecoli, C.4    Baldassini, R.5    Paolicchi, A.6    Barsacchi, R.7    Pompella, A.8
  • 129
    • 0034495137 scopus 로고    scopus 로고
    • Presence of closely spaced protein thiols on the surface of mammalian cells
    • Donoghue N, Yam PT, Jiang XM and Hogg PJ: Presence of closely spaced protein thiols on the surface of mammalian cells. Protein Sci 9(12): 2436-2445, 2000. (Pubitemid 32105726)
    • (2000) Protein Science , vol.9 , Issue.12 , pp. 2436-2445
    • Donoghue, N.1    Yam, P.T.W.2    Jiang, X.-M.3    Hogg, P.J.4
  • 131
    • 27144434430 scopus 로고    scopus 로고
    • Mechanism of selectivity of an angiogenesis inhibitor from screening a genome-wide set of Saccharomyces cerevisiae deletion strains
    • Dilda PJ, Don AS, Tanabe KM, Higgins VJ, Allen JD, Dawes IW and Hogg PJ: Mechanism of selectivity of an angiogenesis inhibitor from screening a genome-wide set of Saccharomyces cerevisiae deletion strains. J Natl Cancer Inst 97(20): 1539-1547, 2005.
    • (2005) J Natl Cancer Inst , vol.97 , Issue.20 , pp. 1539-1547
    • Dilda, P.J.1    Don, A.S.2    Tanabe, K.M.3    Higgins, V.J.4    Allen, J.D.5    Dawes, I.W.6    Hogg, P.J.7
  • 132
    • 29244447109 scopus 로고    scopus 로고
    • Para to Ortho repositioning of the arsenical moiety of the angiogenesis inhibitor 4-(N-(S-glutathionylacetyl)amino) nphenylarsenoxide results in a markedly increased cellular accumulation and antiproliferative activity
    • Dilda PJ, Decollogne S, Rossiter-Thornton M and Hogg PJ: Para to Ortho repositioning of the arsenical moiety of the angiogenesis inhibitor 4-(N-(S-glutathionylacetyl)amino) nphenylarsenoxide results in a markedly increased cellular accumulation and antiproliferative activity. Cancer Res 65(24): 11729-11734, 2005.
    • (2005) Cancer Res , vol.65 , Issue.24 , pp. 11729-11734
    • Dilda, P.J.1    Decollogne, S.2    Rossiter-Thornton, M.3    Hogg, P.J.4
  • 133
    • 30144433165 scopus 로고    scopus 로고
    • Gamma-glutamyltranspeptidase: Disulfide bridges, propeptide cleavage, and activation in the endoplasmic reticulum
    • Kinlough CL, Poland PA, Bruns JB and Hughey RP: Gamma- glutamyltranspeptidase: disulfide bridges, propeptide cleavage, and activation in the endoplasmic reticulum. Meth Enzymol 401: 426-449, 2005.
    • (2005) Meth Enzymol , vol.401 , pp. 426-449
    • Kinlough, C.L.1    Poland, P.A.2    Bruns, J.B.3    Hughey, R.P.4
  • 134
    • 1242272023 scopus 로고    scopus 로고
    • Gamma-glutamyltranspeptidase stimulates receptor activator of nuclear factor-kappaB ligand expression independent of its enzymatic activity and serves as a pathological bone-resorbing factor
    • Niida S, Kawahara M, Ishizuka Y, Ikeda Y, Kondo T, Hibi T, Suzuki Y, Ikeda K and Taniguchi N: Gamma-glutamyltranspeptidase stimulates receptor activator of nuclear factor-kappaB ligand expression independent of its enzymatic activity and serves as a pathological bone-resorbing factor. J Biol Chem 279: 5752-5756, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 5752-5756
    • Niida, S.1    Kawahara, M.2    Ishizuka, Y.3    Ikeda, Y.4    Kondo, T.5    Hibi, T.6    Suzuki, Y.7    Ikeda, K.8    Taniguchi, N.9
  • 137
    • 33748778777 scopus 로고    scopus 로고
    • Gamma-glutamyltransferase as a cardiovascular risk factor
    • Emdin M, Passino C, Pompella A and Paolicchi A: Gamma-glutamyltransferase as a cardiovascular risk factor. Eur Heart J 27(18): 2145-2146, 2006.
    • (2006) Eur Heart J , vol.27 , Issue.18 , pp. 2145-2146
    • Emdin, M.1    Passino, C.2    Pompella, A.3    Paolicchi, A.4
  • 138
    • 0041866784 scopus 로고    scopus 로고
    • Gamma-Glutamyltransferase is a predictor of incident diabetes and hypertension: The Coronary Artery Risk Development in Young Adults (CARDIA) study
    • DOI 10.1373/49.8.1358
    • Lee DH, Jacobs DR Jr, Gross M, Kiefe CI, Roseman J, Lewis CE and Steffes M: Gamma-glutamyltransferase is a predictor of incident diabetes and hypertension: the Coronary Artery Risk Development in Young Adults (CARDIA) Study. Clin Chem 49(8): 1358-1366, 2003. (Pubitemid 36900623)
    • (2003) Clinical Chemistry , vol.49 , Issue.8 , pp. 1358-1366
    • Lee, D.-H.1    Jacobs Jr., D.R.2    Gross, M.3    Kiefe, C.I.4    Roseman, J.5    Lewis, C.E.6    Steffes, M.7
  • 139
    • 8744291010 scopus 로고    scopus 로고
    • Gamma-glutamyltransferase, obesity, and the risk of type 2 diabetes: Observational cohort study among 20,158 middle-aged men and women
    • Lee DH, Silventoinen K, Jacobs DR Jr, Jousilahti P and Tuomileto J: Gamma-glutamyltransferase, obesity, and the risk of type 2 diabetes: observational cohort study among 20,158 middle-aged men and women. J Clin Endocrinol Metab 89(11): 5410-5414, 2004.
    • (2004) J Clin Endocrinol Metab , vol.89 , Issue.11 , pp. 5410-5414
    • Lee, D.H.1    Silventoinen, K.2    Jacobs Jr., D.R.3    Jousilahti, P.4    Tuomileto, J.5
  • 141
    • 33846007117 scopus 로고    scopus 로고
    • Gamma-glutamyltransferase as a predictor of chronic kidney disease in nonhypertensive and nondiabetic Korean men
    • Ryu S, Chang Y, Kim DI, Kim WS and Suh BS: Gamma-glutamyltransferase as a predictor of chronic kidney disease in nonhypertensive and nondiabetic Korean men. Clin Chem 53: 71-77, 2007.
    • (2007) Clin Chem , vol.53 , pp. 71-77
    • Ryu, S.1    Chang, Y.2    Kim, D.I.3    Kim, W.S.4    Suh, B.S.5
  • 143
    • 0026653048 scopus 로고
    • Diagnostic value of serum gamma-glutamyl transferase isoenzyme for hepatocellular carcinoma: A 10-year study
    • Xu K, Meng XY, Wu JW, Shen B, Shi YC and Wei Q: Diagnostic value of serum gamma-glutamyl transferase isoenzyme for hepatocellular carcinoma: a 10-year study. Am J Gastroenterol 87(8): 991-995, 1992.
    • (1992) Am J Gastroenterol , vol.87 , Issue.8 , pp. 991-995
    • Xu, K.1    Meng, X.Y.2    Wu, J.W.3    Shen, B.4    Shi, Y.C.5    Wei, Q.6
  • 144
    • 0031797238 scopus 로고    scopus 로고
    • Diagnosis of hepatocellular carcinoma by quantitative detection of hepatoma-specific bands of serum gamma-glutamyltransferase
    • Yao DF, Huang ZW, Chen SZ, Huang JF, Lu JX, Xiao MB and Meng XY: Diagnosis of hepatocellular carcinoma by quantitative detection of hepatoma-specific bands of serum gamma-glutamyltransferase. Am J Clin Pathol 110(6): 743-749, 1998.
    • (1998) Am J Clin Pathol , vol.110 , Issue.6 , pp. 743-749
    • Yao, D.F.1    Huang, Z.W.2    Chen, S.Z.3    Huang, J.F.4    Lu, J.X.5    Xiao, M.B.6    Meng, X.Y.7
  • 147
    • 0022352968 scopus 로고
    • Variant gamma-glutamyltransferase in colorectal carcinoma and liver metastasis. A case study
    • Huseby NE and Eide TJ: Variant gamma-glutamyltransferase in colorectal carcinoma and liver metastasis. A case study. Clin Biochem 18(4): 217-219, 1985.
    • (1985) Clin Biochem , vol.18 , Issue.4 , pp. 217-219
    • Huseby, N.E.1    Eide, T.J.2
  • 148
    • 0024358246 scopus 로고
    • Comparative study of the sugar chains of gamma-glutamyltranspeptidases purified from human hepatocellular carcinoma and from human liver
    • Yamashita K, Totani K, Iwaki Y, Takamisawa I, Tateishi N, Higashi T, Sakamoto Y and Kobata A: Comparative study of the sugar chains of gamma-glutamyltranspeptidases purified from human hepatocellular carcinoma and from human liver. J Biochem 105(5): 728-735, 1989.
    • (1989) J Biochem , vol.105 , Issue.5 , pp. 728-735
    • Yamashita, K.1    Totani, K.2    Iwaki, Y.3    Takamisawa, I.4    Tateishi, N.5    Higashi, T.6    Sakamoto, Y.7    Kobata, A.8
  • 149
    • 0026796049 scopus 로고
    • Differences in the enzymatic nature and the sugar-chain structure of gamma-glutamyl transferase between normal and carcinomatous human kidney and prostate
    • Arai K, Yoshida K, Komoda T, Kobayashi N and Sakagishi Y: Differences in the enzymatic nature and the sugar-chain structure of gamma-glutamyl transferase between normal and carcinomatous human kidney and prostate. Clin Chim Acta 210(1-2): 35-46, 1992.
    • (1992) Clin Chim Acta , vol.210 , Issue.1-2 , pp. 35-46
    • Arai, K.1    Yoshida, K.2    Komoda, T.3    Kobayashi, N.4    Sakagishi, Y.5
  • 150
    • 0032194814 scopus 로고    scopus 로고
    • Serum gamma-glutamyltransferase and alkaline phosphatase during experimental liver metastases. Detection of tumour-specific isoforms and factors affecting their serum levels
    • Li X, Mortensen B, Rushfeldt C and Huseby NE: Serum gamma- glutamyltransferase and alkaline phosphatase during experimental liver metastases. Detection of tumour-specific isoforms and factors affecting their serum levels. Eur J Cancer 34(12): 1935-1940, 1998.
    • (1998) Eur J Cancer , vol.34 , Issue.12 , pp. 1935-1940
    • Li, X.1    Mortensen, B.2    Rushfeldt, C.3    Huseby, N.E.4
  • 151
    • 0034651861 scopus 로고    scopus 로고
    • Abnormal expression of hepatoma specific gamma-glutamyl transferase and alteration of gamma-glutamyl transferase gene methylation status in patients with hepatocellular carcinoma
    • Yao D, Jiang D, Huang Z, Lu J, Tao Q, Yu Z and Meng X: Abnormal expression of hepatoma specific gamma-glutamyl transferase and alteration of gamma-glutamyl transferase gene methylation status in patients with hepatocellular carcinoma. Cancer 88(4): 761-769, 2000.
    • (2000) Cancer , vol.88 , Issue.4 , pp. 761-769
    • Yao, D.1    Jiang, D.2    Huang, Z.3    Lu, J.4    Tao, Q.5    Yu, Z.6    Meng, X.7
  • 152
    • 9444278351 scopus 로고    scopus 로고
    • Abnormal expression of hepatoma-derived gamma-glutamyltransferase subtyping and its early alteration for carcinogenesis of hepatocytes
    • Yao DF, Dong ZZ, Yao DB, Wu XH, Wu W, Qiu LW, Wang HM and Meng XY: Abnormal expression of hepatoma-derived gamma-glutamyltransferase subtyping and its early alteration for carcinogenesis of hepatocytes. Hepatobiliary Pancreat Dis Int 3(4): 564-570, 2004.
    • (2004) Hepatobiliary Pancreat Dis Int , vol.3 , Issue.4 , pp. 564-570
    • Yao, D.F.1    Dong, Z.Z.2    Yao, D.B.3    Wu, X.H.4    Wu, W.5    Qiu, L.W.6    Wang, H.M.7    Meng, X.Y.8
  • 153
    • 0037629943 scopus 로고    scopus 로고
    • Heterogeneity in gamma-glutamyltransferase mRNA expression and glycan structures. Search for tumor-specific variants in human liver metastases and colon carcinoma cells
    • Pettersen I, Andersen JA, Bjornland K, Mathisen Ø, Bremnes R, Wellman M, Visvikis A and Huseby NE: Heterogeneity in gamma-glutamyltransferase mRNA expression and glycan structures. Search for tumor-specific variants in human liver metastases and colon carcinoma cells. Biochim Biophys Acta 1648: 210-218, 2003.
    • (2003) Biochim Biophys Acta , vol.1648 , pp. 210-218
    • Pettersen, I.1    Andersen, J.A.2    Bjornland, K.3    Mathisen, Ø.4    Bremnes, R.5    Wellman, M.6    Visvikis, A.7    Huseby, N.E.8
  • 154
    • 0031031323 scopus 로고    scopus 로고
    • The role of gamma-glutamyl transpeptidase in the preoperative metastatic evaluation of renal cell carcinoma
    • Sandock DS, Seftel AD and Resnick MI: The role of gamma-glutamyl transpeptidase in the preoperative metastatic evaluation of renal cell carcinoma. J Urol 157: 798-799, 1997.
    • (1997) J Urol , vol.157 , pp. 798-799
    • Sandock, D.S.1    Seftel, A.D.2    Resnick, M.I.3
  • 155
    • 34247647159 scopus 로고    scopus 로고
    • Serum gamma glutamyl-transferase is a sensitive but unspecific marker of metastatic renal cell carcinoma
    • Simic T, Dragicevic D, Savic-Radojevic A, Cimbaljevic S, Tulic C and Mimic-Oka J: Serum gamma glutamyl-transferase is a sensitive but unspecific marker of metastatic renal cell carcinoma. Int J Urol 14(4): 289-293, 2007.
    • (2007) Int J Urol , vol.14 , Issue.4 , pp. 289-293
    • Simic, T.1    Dragicevic, D.2    Savic-Radojevic, A.3    Cimbaljevic, S.4    Tulic, C.5    Mimic-Oka, J.6
  • 156
    • 33746273227 scopus 로고    scopus 로고
    • Evaluation of tumour necrosis factor-alpha, soluble P-selectin, gamma-glutamyl transferase, glutathione S-transferase-pi and alpha-fetoprotein in patients with hepatocellular carcinoma before and during chemotherapy
    • Morsi MI, Hussein AE, Mostafa M, El-Abd E and El-Moneim NA: Evaluation of tumour necrosis factor-alpha, soluble P-selectin, gamma-glutamyl transferase, glutathione S-transferase-pi and alpha-fetoprotein in patients with hepatocellular carcinoma before and during chemotherapy. Br J Biomed Sci 63(2): 74-78, 2006.
    • (2006) Br J Biomed Sci , vol.63 , Issue.2 , pp. 74-78
    • Morsi, M.I.1    Hussein, A.E.2    Mostafa, M.3    El-Abd, E.4    El-Moneim, N.A.5
  • 157
    • 0031939826 scopus 로고    scopus 로고
    • Tumour tissue is a source of gamma-glutamyl transpeptidase sialoform in the sera of melanoma-bearing mice
    • Melezínek I, Borovanský J, Elleder M and Bubnová E: Tumour tissue is a source of gamma-glutamyl transpeptidase sialoform in the sera of melanoma-bearing mice. Melanoma Res 8(1): 39-45, 1998.
    • (1998) Melanoma Res , vol.8 , Issue.1 , pp. 39-45
    • Melezínek, I.1    Borovanský, J.2    Elleder, M.3    Bubnová, E.4
  • 159
    • 51949106668 scopus 로고    scopus 로고
    • Prospective study of the association of gamma-glutamyltransferase with cancer incidence in women
    • Vorarlberg Health Monitoring and Promotion Program Study Group
    • Strasak AM, Pfeiffer RM, Klenk J, Hilbe W, Oberaigner W, Gregory M, Concin H, Diem G, Pfeiffer KP, Ruttmann E, Ulmer H and Vorarlberg Health Monitoring and Promotion Program Study Group: Prospective study of the association of gamma-glutamyltransferase with cancer incidence in women. Int J Cancer 123(8): 1902-1906, 2008.
    • (2008) Int J Cancer , vol.123 , Issue.8 , pp. 1902-1906
    • Strasak, A.M.1    Pfeiffer, R.M.2    Klenk, J.3    Hilbe, W.4    Oberaigner, W.5    Gregory, M.6    Concin, H.7    Diem, G.8    Pfeiffer, K.P.9    Ruttmann, E.10    Ulmer, H.11


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