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2006 | 15 | 4 |

Tytuł artykułu

Effect of dietary bovine lactoferrin on lipid peroxidation and activities, and mRNA levels of antioxidant enzymes of piglets

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
The experiment was conducted to evaluate effect of dietary bovine lactoferrin (bLF) on lipid peroxidation and activities as well as mRNA levels of antioxidant enzymes of piglets. Duroc×Landrace×Yorkshire crossbred female piglets (n=120, 35 days of age, liveweight 9.70±0.71 kg) were fed a diet containing 0, 1250, or 2500 mg/kg bLF for 30 days. After completion of the feeding experiment, twelve female piglets with 4 animals in each treatment were randomly selected to determine malondialdehyde (MDA) and total antioxidant capacity (TAOC) levelsczinc- superoxide dismutase (CuZnSOD), glutathione perioxidase (GPx), catalase (CAT) activities in serum and liver, and CuZnSOD, GPx and CAT mRNA levels in liver. Results showed that piglets treated with 2500 mg/kg bLF significantly increased (P<0.05) TAOC levels, the activities of GPx, CuZnSOD and CAT, and mRNA levels of CuZnSOD, GPx and CAT, and decreased (P<0.05) the contents of MDA as compared with control. Supplementation with 1250 mg/kg bLF also increased (P<0.05) the activities of CuZnSOD, GPx and CAT and mRNA levels of GPx and CAT, and decreased (P<0.05) the contents of MDA as compared with control, but the effect was not better than that of dietary addition of 2500 mg/kg bLF (P<0.05). The study indicated that addition of bLF improved the antioxidant function of piglets by up-regulation of mRNA levels and activities of certain antioxidant enzymes associated with free radicals metabolism.

Słowa kluczowe

Wydawca

-

Rocznik

Tom

15

Numer

4

Opis fizyczny

p.609-620,fig.,ref.

Twórcy

autor
  • Zhejiang University, No. 164 Qiutao North Road, Hongzhou, 310029, P.R. China
autor
autor
autor
autor

Bibliografia

  • Abe H., Saito H., Miyakawa H., Tamura Y., Shimamura S., Nagao E., 1991. Heat stability of bovine lactoferrin at acidic pH. J. Dairy Sci. 74, 65-71
  • Aebi H., 1984. Catalase in vitro. Methods Enzymol. 105, 121-126
  • Baker H.M., Baker E.N., 2004. Lactoferrin and iron: structural and dynamic aspects of binding and release. Biometals 17, 209-216
  • Benzie I.E.F., Stain J.J., 1996. The ferric reducing ability of plasma (FRAP) as a measure of “antioxidant power”, the FRAP assay. Anal Biochem. 239, 70-76
  • Bonkovsky H.L., 1991. Iron and the liver. Amer. J. Med. Sci. 301, 32-43
  • Britigan B.E., Rosen G.M., Thompson B.Y., Chai Y., Cohen M.S., 1986. Stimulated neutrophils limit iron-catalyzed hydroxyl radical formation as defected by spin trapping techniques. J. Biol. Chem. 261, 17026-17039
  • Chandra Mohan K.V.P., Ramasamy K., Duvuru P., Siddavaram N., 2006 Modulation of xenobioticmetabolizing enzymes and redox during chemoprevention of hamster buccal carcinogenesis by bovine lactoferrin. Nutrition 22, 940-946
  • Cornish J., Callon K.E., Naot D., Palmano K.P., Banovic T., Bava U., 2004. Lactoferrin is a potent regulator of bone cell activity and increases bone formation in vivo. Endocrinolology 145, 4366-4374
  • Fillebeen C., Mitchell V., Dexter D., Benaissa M., Beauvillain J.-C., Spik G., Pierce A., 1999.
  • Lactoferrin is synthesized by mouse brain tissue and its expression is enhanced after MPTP treatment. Mol. Brain Res. 72, 183-194
  • Freeman B.A., Crapo J.D., 1982. Biology of disease: free radicals and tissue injury. Lab. Invest. 47, 412-426
  • Gutteridge J.M.C., Rowley D.A., Halliwell B., 1982. Superoxide-dependent formation of hydroxyl radical and lipid peroxidation in the presence of iron salt: detection of catalytic iron and antioxidant activity in extracellular fluids. J. Biochem. 206, 605-609
  • Hafemen D.G., 1974. Effect of dietary selenium on erythrocyte and liver glutathione peroxidase in the rats. J. Nutr. 104, 580-587
  • Harrison P.M., Arosio P., 1996. The ferritins, molecular properties, iron storage function, and cellular regulation. Biochem. Biophys. Acta 1275, 161-203
  • He J., Furmanski P., 1995. Sequence specificity and transcriptional activation in the binding of lactoferrin to DNA. Nature 373, 721-724
  • Lindmark-Mansson H., Akesson B., 2000. Antioxidative factors in milk. Brit. J. Nutr. 84, Suppl. 1, 103-110
  • Luo Y.M., Zhen Q., Zhen H., Zhang X.M., Ding D., Fu J.H., Zhang W.D., Chen J., 2004. Astragaloside IV protects against ischemic brain injury in a murine model of transient focal ischemia. Neurosci. Lett. 363, 218-223
  • Mccord J.M., 1998. Iron free radicals, and oxidative injury. Hematology 35, 5-12
  • Moldeus P., 1995. Defence mechanisms in free radical induced toxicities. Toxicol. Lett. 78, Suppl. 1, 1-88
  • Natsuko T., Hiroyuki W., Hiroko I., Koji Y., Susumu T., Yoshitaka T., Hideyo Y., Shigeru A., 2004. Effect of orally administered bovine lactoferrin on the immune response in the oral candidiasis murine model. J. Med. Microbiol. 54, 495-500
  • Placer Z.A., Cushman L.L., Johnson B.C., 1966. Estimation of production of lipid peroxidation, malindialdehyde in biochemical system. Anal. Biochem. 16, 359-367
  • Raghuveer T.S., McGuire E.M., Martin S.M., Balansky R.M., Noonan D., Albini A., 2002. Lactoferrin in the preterm infants diet attenuated iron - induced oxidation products. Pediat. Res. 52, 964-972
  • Rebelo I., Carvalho-Guerra F., Pereira-Leite L., Quintanilha A., 1995. Lactoferrin as a sensitive blood marker of neutrophil activation in normal pregnancies. Eur. J. Obstet. Gyn. Reprod. Biol. 62, 189-194
  • Roiron D., Amouric M., Marvaldi J., Flgarella C., 1989. Lactoferrin-binding sites at the surface of HT29-D4 cells. Eur. J. Biochem. 186, 367-373
  • Sandomirsky B.P., Galchemko S.E., Galchenko K.S., 2003. Antioxidative properties of lactoferrin from bovine colostrums before and after its lyophilization. Cryo-lett. 24, 275-280
  • Satue-Gracia M.T., Frankel E.N., Rangavajhyala N., German J.B., 2000. Lactoferrin in infant formulas: effect on oxidation. J. Agr. Food Chem. 48, 4984-4990
  • Shinmoto H., Dosako S., Nakajima I., 1992. Antioxidant activity of bovine lactoferrin on iron/ ascorbate induced lipid peroxidation. Biosci. Biochnol. Biochem. 56, 2079-2080
  • Steijns J.M., Van Hooijdonk A.C.M., 2000. Occurrence, structure, biochemical properties and technological characteristics of lactoferrin. Brit. J. Nutr. 84, Suppl. 1, S11-S17
  • Teraguchi S., Wakabayashi H., Kuwata H., Yamauchi K., Tamura Y., 2004. Protection agaist infections by oral lactoferrin: Evaluation in animal models. Biometals 17, 231-234
  • Troost F.J., Straub P.W., Brummer R.J.M., 2001 Gastric digestion of bovine lactoferrin in vivo in adults. J. Nutr. 131, 2101-2104
  • Van Snick J.L., Markowetz B., Masson P.L., 1977. The ingestion and digestion of human lactoferrin by mouse peritoneal macrophages and the transfer of its iron into ferritin. J. Exp. Med. 146, 817-827
  • Wakabayashi H., Yamauchi K., Takase M., 2006. Lactoferrin research, technology and applications. Inter. J. Dairy (in press)
  • Wang Y.Z., Shan T. Z., Xu Z.R., Liu J.X., Feng J., 2006. Effect of lactoferrin on the growth performance, intestinal morphology, and expression of PR-39 and protegrin-1 genes in weaned piglets. J. Anim. Sci. 84, 2636-2641
  • Wang Y.Z., Tu Y.J., Han F.F., Wang J.H., 2005b. Developmental gene expression of lactoferrin and effect of dietary iron on gene regulation of lactoferrin in the mice mammary gland. J. Dairy Sci. 88, 2065-2071
  • Wang Y.Z., Wu X.F., Liu G.F, Cao C.P., Huang H.Q., Xu Z.R. Liu J.X., 2005a. Expression of porcine lactoferrin by using recombinant baculovirus in silkworm, Bombyx mori L, and its purification and characterization. Appl. Microbiol. Biotechnol. 69, 385-389
  • Weinberg E.D., 1993. The development of awareness of iron-withholding defense. Perspect. Biol. Med. 36, 215-223
  • Winterbourn C.C., Hawkins R.E., Brain M., Carrell R., 1975. The estimation of red cell superoxide dismutase activity. J. Lab. Clin. Med. 85, 337-341

Typ dokumentu

Bibliografia

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Identyfikator YADDA

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