메뉴 건너뛰기




Volumn 44, Issue 10, 1996, Pages 1101-1108

Immunohistochemical detection of γ-glutamyl transpeptidase in normal human tissue

Author keywords

GGT129; Glutathione; Human; Immunohistochemistry; Peptide antibody; Glutamyl transpeptidase

Indexed keywords

ANTIBODY; FORMALDEHYDE; GAMMA GLUTAMYLTRANSFERASE;

EID: 0029794573     PISSN: 00221554     EISSN: None     Source Type: Journal    
DOI: 10.1177/44.10.8813074     Document Type: Article
Times cited : (176)

References (39)
  • 1
    • 0023263375 scopus 로고
    • Gammaglutamyl-transpeptidase and maintenance of thiol pools in tumor cells resistant to alkylating agents
    • Ahmad S, Okine L, Wood R, Aljian J, Vistica DT (1987) Gammaglutamyl-transpeptidase and maintenance of thiol pools in tumor cells resistant to alkylating agents. J Cell Physiol 131:240-246
    • (1987) J Cell Physiol , vol.131 , pp. 240-246
    • Ahmad, S.1    Okine, L.2    Wood, R.3    Aljian, J.4    Vistica, D.T.5
  • 2
    • 0002771773 scopus 로고
    • Histochemical and biochemical investigations of gamma-glutamyl transpeptidase in the tissues of man and laboratory rodents
    • Albert Z, Orlowska J, Orlowski M, Szewczuk A (1964) Histochemical and biochemical investigations of gamma-glutamyl transpeptidase in the tissues of man and laboratory rodents. Acta Histochem 18:78-89
    • (1964) Acta Histochem , vol.18 , pp. 78-89
    • Albert, Z.1    Orlowska, J.2    Orlowski, M.3    Szewczuk, A.4
  • 3
    • 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, Sakagishi Y (1992) 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 210:35-46
    • (1992) Clin Chim Acta , vol.210 , pp. 35-46
    • Arai, K.1    Yoshida, K.2    Komoda, T.3    Kobayashi, N.4    Sakagishi, Y.5
  • 4
    • 0025599402 scopus 로고
    • Secretion of gamma-glutamyl transpeptidase by the pancreas: Evidence for a membrane shedding process during exocytosis
    • Battistini B, Chailler P, Briere N, Beaudoin AR (1990) Secretion of gamma-glutamyl transpeptidase by the pancreas: evidence for a membrane shedding process during exocytosis. Life Sci 47:2435-2441
    • (1990) Life Sci , vol.47 , pp. 2435-2441
    • Battistini, B.1    Chailler, P.2    Briere, N.3    Beaudoin, A.R.4
  • 5
    • 0025355982 scopus 로고
    • Mechanism of gamma-glutamyl transpeptidase release in serum during intrahepatic and extrahepatic cholestasis in the rat: A histochemical, biochemical and molecular approach
    • Bulle F, Mavier P, Zafrani ES, Preux A, Lescs M, Siegrist S, Dhumeaux D, Guellaen D (1990) Mechanism of gamma-glutamyl transpeptidase release in serum during intrahepatic and extrahepatic cholestasis in the rat: a histochemical, biochemical and molecular approach. Hepatology 11:545-550
    • (1990) Hepatology , vol.11 , pp. 545-550
    • Bulle, F.1    Mavier, P.2    Zafrani, E.S.3    Preux, A.4    Lescs, M.5    Siegrist, S.6    Dhumeaux, D.7    Guellaen, D.8
  • 7
    • 0018640906 scopus 로고
    • Characterization and physiological function of rat renal gamma-glutamyl transpeptidase
    • Curthoys NP, Hughey RP (1979) Characterization and physiological function of rat renal gamma-glutamyl transpeptidase. Enzyme 24:383-403
    • (1979) Enzyme , vol.24 , pp. 383-403
    • Curthoys, N.P.1    Hughey, R.P.2
  • 8
    • 0028190695 scopus 로고
    • Formation and fate of nephrotoxic and cytotoxic glutathione S-conjugates: Cysteine conjugate beta-lyase pathway
    • Anders MW, Dekant W, eds. New York, Academic Press
    • Dekant W, Vamvakas S, Anders MW (1995) Formation and fate of nephrotoxic and cytotoxic glutathione S-conjugates: cysteine conjugate beta-lyase pathway. In Anders MW, Dekant W, eds. Advances in Pharmacology. Vol 27. New York, Academic Press, 115-162
    • (1995) Advances in Pharmacology , vol.27 , pp. 115-162
    • Dekant, W.1    Vamvakas, S.2    Anders, M.W.3
  • 9
    • 0019829991 scopus 로고
    • Demonstration of gamma-glutamyl transferase, alkaline phosphatase, CEA and HCG in human lung cancer
    • Dempo K, Elliott KAC, Desmond W, Fishman WH (1981) Demonstration of gamma-glutamyl transferase, alkaline phosphatase, CEA and HCG in human lung cancer. Oncodev Biol Medicine 2:21-37
    • (1981) Oncodev Biol Medicine , vol.2 , pp. 21-37
    • Dempo, K.1    Elliott, K.A.C.2    Desmond, W.3    Fishman, W.H.4
  • 10
    • 0021733746 scopus 로고
    • Renal processing of glutathione conjugates, role in nephrotoxicity
    • Elfarra AA, Anders MW (1984) Renal processing of glutathione conjugates, role in nephrotoxicity. Biochem Pharmacol 33:3729-3732
    • (1984) Biochem Pharmacol , vol.33 , pp. 3729-3732
    • Elfarra, A.A.1    Anders, M.W.2
  • 11
    • 0001904502 scopus 로고
    • Gamma-glutamyl transpeptidase: Molecular cloning and structural and functional features of a blood-brain barrier marker protein
    • Pardridge WM, ed. New York, Raven Press
    • Frey A (1993) Gamma-glutamyl transpeptidase: molecular cloning and structural and functional features of a blood-brain barrier marker protein. In Pardridge WM, ed. The Blood Brain Barrier. New York, Raven Press, 339-368
    • (1993) The Blood Brain Barrier , pp. 339-368
    • Frey, A.1
  • 12
    • 0037641871 scopus 로고
    • Histochemical demonstration of a gamma-glutamyl transpeptidase-like activity
    • Glenner GG, Folk JE, McMillan PJ (1962) Histochemical demonstration of a gamma-glutamyl transpeptidase-like activity. J Histochem Cytochem 10:481-489
    • (1962) J Histochem Cytochem , vol.10 , pp. 481-489
    • Glenner, G.G.1    Folk, J.E.2    McMillan, P.J.3
  • 13
    • 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, Anderson ME (1992) High resistance to cisplatin in human ovarian cancer cell lines is associated with marked increase of glutathione synthesis. Proc Natl Acad Sci USA 89:3070-3074
    • (1992) Proc Natl Acad Sci USA , vol.89 , 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
  • 15
    • 0022438848 scopus 로고
    • Models of hepatocarcinogenesis in the rat-contrasts and comparisons
    • Goldsworthy TL, Hanigan MH, Pitot HC (1986) Models of hepatocarcinogenesis in the rat-contrasts and comparisons. CRC Crit Rev Toxicol 17:61-89
    • (1986) CRC Crit Rev Toxicol , vol.17 , pp. 61-89
    • Goldsworthy, T.L.1    Hanigan, M.H.2    Pitot, H.C.3
  • 16
    • 0012971643 scopus 로고
    • Translocation of intracellular glutathione to membrane-bound gamma-glutamyl transpeptidase as a discrete step in the gamma-glutamyl cycle: Glutathionuria after inhibition of transpeptidase
    • Griffith OW, Meister A (1979) Translocation of intracellular glutathione to membrane-bound gamma-glutamyl transpeptidase as a discrete step in the gamma-glutamyl cycle: glutathionuria after inhibition of transpeptidase. Proc Natl Acad Sci USA 76:268-272
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 268-272
    • Griffith, O.W.1    Meister, A.2
  • 17
    • 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 (1995) 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) Carcinogenesis , vol.16 , pp. 181-185
    • Hanigan, M.H.1
  • 19
    • 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, Large MK (1994b) Inhibition of gamma-glutamyl transpeptidase activity by acivicin in vivo protects the kidney from cisplatin-induced toxicity. Cancer Res 54:5925-5929
    • (1994) Cancer Res , vol.54 , pp. 5925-5929
    • Hanigan, M.H.1    Gallagher, B.C.2    Taylor Jr., P.T.3    Large, M.K.4
  • 20
    • 0021998639 scopus 로고
    • Gamma-glutamyl transpeptidase - Its role in hepatocarcinogenesis
    • Hanigan MH, Pitot HC (1985) Gamma-glutamyl transpeptidase - its role in hepatocarcinogenesis. Carcinogenesis 6:165-172
    • (1985) Carcinogenesis , vol.6 , pp. 165-172
    • Hanigan, M.H.1    Pitot, H.C.2
  • 21
    • 0027263185 scopus 로고
    • Extracellular glutathione is a source of cysteine for cells that express gamma-glutamyl transpeptidase
    • Hanigan MH, Ricketts WA (1993) Extracellular glutathione is a source of cysteine for cells that express gamma-glutamyl transpeptidase. Biochemistry 32:6302-6306
    • (1993) Biochemistry , vol.32 , pp. 6302-6306
    • Hanigan, M.H.1    Ricketts, W.A.2
  • 22
    • 0021165717 scopus 로고
    • Mechanism of biliary secretion of membranous enzymes: Bile acids are important factors for biliary occurrence of gamma-glutamyltransferase and other hydrolases
    • Hirata E, Inoue M, Morino Y (1984) Mechanism of biliary secretion of membranous enzymes: bile acids are important factors for biliary occurrence of gamma-glutamyltransferase and other hydrolases. J Biochem 96:289-297
    • (1984) J Biochem , vol.96 , pp. 289-297
    • Hirata, E.1    Inoue, M.2    Morino, Y.3
  • 23
    • 0025949649 scopus 로고
    • Multifactorial mechanisms associated with broad cross-resistance of ovarian carcinoma cells selected by cyanomorpholino doxorubicin
    • Lau HM, Lewis AD, Ehsan MN, Sikic BI (1991) Multifactorial mechanisms associated with broad cross-resistance of ovarian carcinoma cells selected by cyanomorpholino doxorubicin. Cancer Res 51:5181-5187
    • (1991) Cancer Res , vol.51 , pp. 5181-5187
    • Lau, H.M.1    Lewis, A.D.2    Ehsan, M.N.3    Sikic, B.I.4
  • 25
    • 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, Wolf CR (1988) 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) Carcinogenesis , vol.9 , pp. 1283-1287
    • Lewis, A.L.1    Hayes, J.D.2    Wolf, C.R.3
  • 26
    • 0019794485 scopus 로고
    • Mediation of local homeostasis and inflammation by leukotrienes and other mast cell-dependent compounds
    • Lewis RA, Austen KF (1981) Mediation of local homeostasis and inflammation by leukotrienes and other mast cell-dependent compounds. Nature 293:103-108
    • (1981) Nature , vol.293 , pp. 103-108
    • Lewis, R.A.1    Austen, K.F.2
  • 28
    • 0028199225 scopus 로고
    • Glial extracellular matrix modulates gamma-glutamyl transpeptidase activity in cultured bovine brain capillary and bovine aortic endothelial cells
    • Mizuguchi H, Hashioka Y, Fujii A, Utoguchi N, Kubo K, Nakagwa S, Baba A, Mayumi T (1994) Glial extracellular matrix modulates gamma-glutamyl transpeptidase activity in cultured bovine brain capillary and bovine aortic endothelial cells. Brain Res 651:155-159
    • (1994) Brain Res , vol.651 , pp. 155-159
    • Mizuguchi, H.1    Hashioka, Y.2    Fujii, A.3    Utoguchi, N.4    Kubo, K.5    Nakagwa, S.6    Baba, A.7    Mayumi, T.8
  • 29
    • 0019171509 scopus 로고
    • Inhibition of leukotriene C and leukotriene D biosynthesis
    • Orning L, Hammarstrom S (1980) Inhibition of leukotriene C and leukotriene D biosynthesis. J Biol Chem 255:8023-8026
    • (1980) J Biol Chem , vol.255 , pp. 8023-8026
    • Orning, L.1    Hammarstrom, S.2
  • 31
    • 0016411013 scopus 로고
    • Gamma-glutamyl transpeptidase
    • Rosalki SB (1975) Gamma-glutamyl transpeptidase. Adv Clin Chem 17:53-107
    • (1975) Adv Clin Chem , vol.17 , pp. 53-107
    • Rosalki, S.B.1
  • 33
    • 0023214578 scopus 로고
    • Renal clearance of glutathione measured in rats pretreated with inhibitors of glutathione metabolism
    • Scott RD, Curthoys N (1987) Renal clearance of glutathione measured in rats pretreated with inhibitors of glutathione metabolism. Am J Physiol 252:F877-F882
    • (1987) Am J Physiol , vol.252
    • Scott, R.D.1    Curthoys, N.2
  • 34
    • 0024409806 scopus 로고
    • A monoclonal antibody against human kidney gamma-glutamyl transpeptidase: Preparation, immunochemical and immunohistochemical characterization
    • Shiozawa M, Yamashita S, Aiso S, Yasuda K (1989) A monoclonal antibody against human kidney gamma-glutamyl transpeptidase: preparation, immunochemical and immunohistochemical characterization. J Histochem Cytochem 37:1053-1061
    • (1989) J Histochem Cytochem , vol.37 , pp. 1053-1061
    • Shiozawa, M.1    Yamashita, S.2    Aiso, S.3    Yasuda, K.4
  • 35
    • 0027397823 scopus 로고
    • Distribution of gamma-glutamyl transpeptidase in human salivary glands: Immunohistochemical study using a monoclonal antibody
    • Shiozawa M, Yasuda K, Yamashita S, Aiso S (1993) Distribution of gamma-glutamyl transpeptidase in human salivary glands: Immunohistochemical study using a monoclonal antibody. J Histochem Cytochem 41:205-213
    • (1993) J Histochem Cytochem , vol.41 , pp. 205-213
    • Shiozawa, M.1    Yasuda, K.2    Yamashita, S.3    Aiso, S.4
  • 36
    • 0023178371 scopus 로고
    • A human hepatoma cell line expresses a single-chain form of gamma-glutamyl transpeptidase
    • Tate SS, Galbraith RA (1987) A human hepatoma cell line expresses a single-chain form of gamma-glutamyl transpeptidase. J Biol Chem 262:11403-11406
    • (1987) J Biol Chem , vol.262 , pp. 11403-11406
    • Tate, S.S.1    Galbraith, R.A.2
  • 37
    • 0017068122 scopus 로고
    • Higher transpeptidation activity and broad acceptor specificity of gamma-glutamyltransferase of tumors
    • Tateishi N, Higashi T, Nomura T, Naruse A, Nakashima K, Shiozaki H, Sakamoto Y (1976) Higher transpeptidation activity and broad acceptor specificity of gamma-glutamyltransferase of tumors. Gann 67:215-222
    • (1976) Gann , vol.67 , pp. 215-222
    • Tateishi, N.1    Higashi, T.2    Nomura, T.3    Naruse, A.4    Nakashima, K.5    Shiozaki, H.6    Sakamoto, Y.7
  • 38
    • 0019995474 scopus 로고
    • Comparative ontogenesis of gamma-glutamyl transpeptidase in rat tissue
    • Wapnir RA, Mancusi VJ, Goldstein LA (1982) Comparative ontogenesis of gamma-glutamyl transpeptidase in rat tissue. Experientia 38:647-648
    • (1982) Experientia , vol.38 , pp. 647-648
    • Wapnir, R.A.1    Mancusi, V.J.2    Goldstein, L.A.3
  • 39
    • 0024323809 scopus 로고
    • Characterization of variant gamma-glutamyl transpeptidase produced by pancreatocholangiocarcinoma cell lines in a protein-free, chemically defined medium
    • Yamaguchi N, Koyama K, Shiroeda O, Chung S, Ashihara T, Imanishi J (1989) Characterization of variant gamma-glutamyl transpeptidase produced by pancreatocholangiocarcinoma cell lines in a protein-free, chemically defined medium. Pancreas 4:406-417
    • (1989) Pancreas , vol.4 , pp. 406-417
    • Yamaguchi, N.1    Koyama, K.2    Shiroeda, O.3    Chung, S.4    Ashihara, T.5    Imanishi, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.