Glutathione and GSH-dependent enzymes in patients with liver cirrhosis and hepatocellular carcinoma

• Autorzy: Czeczot H. , Scibior D. , Skrzycki M. , Podsiad M.
• Języki publikacji: EN

Abstrakty

EN

We investigated glutathione level, activities of selenium independent GSH peroxidase, selenium dependent GSH peroxidase, GSH S-transferase, GSH reductase and the rate of lipid peroxidation expressed as the level of malondialdehyde in liver tissues obtained from patients diagnosed with cirrhosis or hepatocellular carcinoma. GSH level was found to be lower in malignant tissues compared to adjacent normal tissues and it was higher in cancer than in cirrhotic tissue. Non-Se-GSH-Px activity was lower in cancer tissue compared with adjacent normal liver or cirrhotic tissue, while Se-GSH-Px activity in cancer was found to be similar to its activity in cirrhotic tissue and lower compared to control tissue. An increase in GST activity was observed in cirrhotic tissue compared with cancer tissue, whereas the GST activity in cancer was lower than in adjacent normal tissue. The activity of GSH-R was similar in cirrhotic and cancer tissues, but higher in cancer tissue compared to control liver tissue. An increased level of MDA was found in cancer tissue in comparison with control tissue, besides its level was higher in cancer tissue than in cirrhotic tissue. Our results show that the antioxidant system of cirrhosis and hepatocellular carcinoma is severely impaired. This is associated with changes of glutathione level and activities of GSH-dependent enzymes in liver tissue. GSH and enzymes cooperating with it are important factors in the process of liver diseases development.

Słowa kluczowe

EN

human disease; glutathione S-transferase; patient; hepatocellular carcinoma; enzyme; malondialdehyde; glutathione reductase; glutathione; glutathione peroxidase; liver cirrhosis

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2006
• Tom: 53
• Numer: 1
• Opis fizyczny: p.237-241,ref.

Twórcy

autor

Czeczot H.

• Medical University of Warsaw, Warsaw, Poland

autor

Scibior D.

autor

Skrzycki M.

autor

Podsiad M.

Bibliografia

• Abou Ghalia AH, Fouad IM (2000) Clin Biochem 33: 657–662.
• Ahn J, Flamm SL (2004) Dis Monitor 50: 556–573.
• Badvie S (2000) Postgrad Med J 76: 4–11.
• Balasubramanian S, Kowdley KV (2005) Clin Liver Dis 9: 83–101.
• Bradford MM (1976) Anal Biochem 72: 248–254.
• Buljevac M, Romic Z, Vucelic B, Banic M, Krznaric Z, Plesko S (1996) Acta Med Croatica 50: 11–14.
• Casaril M, Gabrielli GB, Dusi S, Nicoli N, Bellisola G, Corrocher R (1985) Eur J Cancer Clin Oncol 21: 941–944.
• Casaril M, Corso F, Bassi A, Capra F, Gabrielli GB, Stanzial AM, Nicoli N, Corrocher R (1994) Int J Clin Lab Res 24: 94–97.
• Chrobot AM, Szaflarska-Szczepanik A, Drewa G (2000) Med Sci Monit 6: 713–718.
• Chu FF, Esworthy RS, Doroshow JH (2004) Free Radic Biol Med 36: 1481–1495.
• Corrocher R, Casaril M, Bellisola G, Gavarielli GB, Nicoli N, Guidi GC, De Sandre G (1986) Cancer 15: 1658–1662.
• Czuczejko J, Halota W, Zachara BA, Staubach-Topczewska E (2002 ) Pol Merk Lek 13: 312–315.
• Dalhoff K, Ranek L, Mantoni M, Poulsen HE (1992) Liver 12: 341–343.
• Dreher D, Junod AF (1996) Eur J Cancer 32A: 30–38.
• Fernandez-Checa JC, Kaplowitz N (2005) Toxicol Appl Pharmacol 204: 263–273.
• Fisher AB, Dodia C, Manevich Y, Chen JW, Feinstein SI (1999) J Biol Chem 274: 21326–21334.
• Gate L, Paul J, Nguyen BA, Tew KD, Tapiero H (1999) Biomed Pharmacother 53: 169–180.
• Golberg DM, Spooner RJ (1987) In Methods of Enzymatic Analysis (Bregmayer HV, ed) pp 258–265, Verlag Chemie.
• Habig WH, Pabst M, Jacoby W (1974) J Biol Chem 249: 7130–7139.
• Halliwell B, Gutteridge JMC (1996) Arch Biochem Biophys 280: 1–8.
• Hayes JD, McLellan LI (1999) Free Radic Res 31: 273–300.
• Jungst C, Cheng B, Gehrke R, Schmitz V, Nischalke HD, Ramakers J, Schramel P, Schirmacher P, Sauerbruch T, Caselmann WH (2004) Hepatology 39: 1663–1672.
• Kamel IR, Bluemke DA (2002) J Vasc Intervent Radiol 13: 173–184.
• Kikkawa S, Kadohara M, Kawasaki H (1992) Res Commun Chem Pathol Pharmacol 78: 289–309.
• Loguercio C, Di Pierro M (1999) Ital J Gastroenterol Hepatol 31: 401–407.
• Lotersztajn S, Julien B, Teixeira-Clerc F, Grenard P, Mallat A (2005) Annu Rev Pharmacol Toxicol 45: 605–628.
• Marnett LJ (1999) Mutat Res 424: 83–95.
• Matiushin BN, Loginov AS, Tkachev VD (1998) Klein Lab Diagn 4: 16–8.
• Murphy ME, Scholich H, Sies H (1992) Eur J Biochem 210: 139–146.
• Mylonas C, Kouritas D (1999) In Vivo 13: 295–309.
• Oberley TD, Oberley LW (1997) Histol Histhopathol 12: 525–535.
• Ohkawa H, Ohishi N, Yagi K (1968) Anal Biochem 25: 192–205.
• Paglia D, Valentine W (1967) J Lab Clin Med 70: 158–168.
• Peng RX, Wang H, Wang YS, Fu LS, Ding H (1998) Zhongguo Yao Li Xue Bao 19: 167–171.
• Piekarska A, Matusiak K (2004) Pol Arch Med Wewn 111: 397–403.
• Rehermann B, Nascimbeni M (2005) Nat Rev Immunol 5: 215–229.
• Sedlak J, Lindsay RH (1968) Anal Biochem 25: 192–205.
• Sherman M, Campbell JA, Titmuss SA, Kew MC, Kirsch RE (1983) Hepatology 3: 170–176.
• Sies H (1999) Free Radic Biol Med 27: 916–921. Skrzydlewska E, Kożusko B, Sulkowska M, Bogdan Z, Kozłowski M, Snarska J, Puchalski Z, Sulkowski S, Skrzydlewski Z (2003) Hepatogastroenterology 50: 126–131.
• Snel CAW, Zhao Y, Mulder GJ, Pang KS (1993) Anal Biochem 212: 28–34.
• Szatrowski TP, Nathan CF (1991) Cancer Res 51: 794–798.
• Tew KD, Ronai Z (1999) Drug Resist Updat 2: 143–147.
• Tsuchida S, Sato K (1992) Crit Rev Biochem Mol Biol 27: 337–384.
• Ursini F, Bindoli A (1987) Chem Phys Lipids 44: 255–276.
• Voigt MD (2005) Clin Liver Dis 9: 151–169.
• Wendel A (1981) Methods Enzymol 77: 325–333.