Total and differential bulk cow milk somatic cell counts and their relation with antioxidant factors

Comptes Rendus - Biologies

Volumn 331, Issue 2, 2008, Pages 144-151

  Hamed, Houda ^a   El Feki, Abdelfettah ^a   Gargouri, Ahmed ^a  

^a University of Sfax   (Tunisia)

Author keywords

Bulk milk somatic cell counts; Differential somatic cell counts; Oxidative stress; Polymorphonuclear leukocytes

Indexed keywords

ANTIOXIDANT; CATALASE; GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE; HYDROXYL RADICAL; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE;

ANTIOXIDANT; DAIRY FARMING; ENZYME; HYDROGEN PEROXIDE; HYDROXYL RADICAL; METABOLITE; MILK;

ANIMAL CELL; ARTICLE; CELL COUNT; CELL SECRETION; CELL TYPE; CONTROLLED STUDY; CORRELATION ANALYSIS; DAIRY CATTLE; DAIRYING; ENZYME ANALYSIS; FOOD ANALYSIS; LYMPHOCYTE COUNT; MACROPHAGE; MAMMARY GLAND; MILK; NEUTROPHIL COUNT; NONHUMAN; OXIDATIVE STRESS; SOMATIC CELL; TUNISIA; WINTER;

ANIMALS; ANTIOXIDANTS; CATALASE; CATTLE; CELL COUNT; DAIRYING; FEMALE; GLUTATHIONE PEROXIDASE; LYMPHOCYTES; MACROPHAGES; MILK; NEUTROPHILS; SUPEROXIDE DISMUTASE; TUNISIA;

AFRICA; NORTH AFRICA; SFAX [TUNISIA]; TUNISIA;

EID: 38549138365     PISSN: 16310691     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.crvi.2007.11.008     Document Type: Article

References (55)

1. Dosogne H., Vangroenweghe F., Mehrzad J., Massart-Leën A.M., and Burvenich C. Differential leukocyte count method for bovine low somatic cell count milk. J. Dairy Sci. 86 (2003) 828-834
2. Lindmark-Månsson H., Bränning C., Aldén G., and Paulsson M. Relationship between somatic cell count, individual leukocyte populations and milk components in bovine udder quarter milk. I. Dairy J. 16 (2006) 717-727
3. Ryšánek D., Babák V., Sládek Z., and Toman M. Variations among unbred heifers in the activities of polymorphonuclear leucocytes from the mammary gland and blood. J. Vet. Med. B: Infect. Dis. Vet. Public Health 48 (2001) 31-41
4. Verdi R.J., and Barbano D.M. Preliminary investigation of the properties of somatic cell proteases. J. Dairy Sci. 71 (1988) 534-538
5. Kelly A.L., Tiernan D., O'Sullivan C., and Joyce P. Correlation between bovine milk somatic cell count and polymorphonuclear leukocyte level for samples of bulk milk and milk from individual cows. J. Dairy Sci. 83 (2000) 300-304
6. Sládek Z., Ryznarova H., and Ryšánek D. Macrophages of the bovine heifer mammary gland: Morphological features during initiation and resolution of the inflammatory response. Anat. Histol. Embryol. 35 (2006) 116-124
7. Kehrli M.E., and Shuster D.E. Factors affecting milk somatic cells and their role in health of the bovine mammary gland. J. Dairy Sci. 77 (1994) 619-627
8. Zecconi A., Bronzo V., Piccinini R., Spreafico G., and Rufo G. Phagocytic activity of bovine polymorphonuclear leukocytes. J. Dairy Res. 61 (1994) 271-279
9. Paape M.J., Guidry A.J., Jain N.C., and Miller R.H. Leukocyte defense mechanisms in the udder. Flemish Vet. J. 62 (1991) 95-109
10. Barber M.R., and Yang T.J. Chemotactic activities in non mastitic and mastitic mammary secretions: presence of interleukin-8 in mastitic but not non mastitic secretions. Clin. Diagn. Lab. Immunol. 5 (1998) 82-86
11. Caswell J.L., Middleton D.M., and Gordon J.R. Production and functional characterization of recombinant bovine interleukin-8 as a specific neutrophil. Vet. Immunol. Immunopathol. 67 (1998) 327-340
12. Hampton M.B., Kettle A.J., and Winterbourn C.C. Inside the neutrophil phagosome: oxidants, myeloperoxidase, and bacterial killing. Blood 92 (1998) 3007-3017
13. Weiss S.J. Tissue destruction by neutrophils. N. Engl. J. Med. 320 (1989) 365-376
14. Van Asbeck B.S. Oxygen toxicity: Role of hydrogen peroxide and iron. Adv. Exp. Med. Biol. 264 (1990) 235-246
15. Miller J.K., Brezezinska-Slebodzinska E., and Madsen F.C. Oxidative stress, antioxidants and animal function. J. Dairy Sci. 76 (1993) 2812-2823
16. Brzezinska-Slebodzinska E., Miller J.K., Quigley J.D., Moore J.R., and Madsen F.C. Antioxidant status of dairy cows supplemented preparatum with vitamin E and selenium. J. Dairy Sci. 77 (1994) 3087-3095
17. Lindmark-Månsson H., and Akesson B. Antioxidative factors in milk. Br. J. Nutr. 84 (2000) S103-S110
18. Knaapen A.M., Seiler F., Schilderman P.A.E.L., Nehls P., Bruch J., Schins R.P.F., and Borm J.A. Neutrophils cause oxidative DNA damage in alveolar epithelial cells. Free Radic Biol. Med. 27 (1999) 234-240
19. W.P. Weiss, Éléments nutritifs antioxydants et qualité du lait. Symposium sur les bovins laitiers, Quebec, 2004, p. 14
20. Gargouri A., Hamed H., and ElFeki A. Total and differential bulk cow milk somatic cell counts and their relation with lipolysis. Livest. Sci. (2007)
21. Aebi H. Catalase in vitro. Methods Enzymol. 105 (1984) 121-126
22. Asada K., Takahashi M., and Nagate M. Assay and inhibitors of spinach superoxide dismutase. Agric. Biol. Chem. 38 (1974) 471-473
23. Flohe L., and Gunzler W.A. Assays of glutathione peroxidase. Methods Enzymol. 105 (1984) 14-21
24. Lowry O.H., Rosebrugh N.J., Farr A.L., and Raudall R.J. Protein measurement with folin phenol reagent. J. Biol. Chem. 193 (1951) 265-275
25. Verdi R.J., and Barbano D.M. Properties of proteases from milk somatic cells and blood leukocytes. J. Dairy Sci. 74 (1991) 2077-2081
26. Harmon R.J. Physiology of mastitis and factors affecting somatic cell counts. J. Dairy Sci. 77 (1994) 2103-2112
27. Somers J.M., O'Brien B., Meaney W.J., and Kelly A.L. Heterogeneity of proteolytic enzyme activities in milk samples of different somatic cell count. J. Dairy Res. 70 (2003) 45-50
28. Pillai S.R., Kunze E., Sordillo L.M., and Jayarao B.M. Application of differential inflammatory cell count as a tool to monitor udder health. J. Dairy Sci. 84 (2001) 1413-1420
29. Y.H. Schukken, G. Bennet, L. Green, T. van Werven, Can somatic cell counts get too low? in: National Mastitis Council, Inc. 40th Annual Meeting Proceedings, 2001, pp. 19-28
30. Pyörälä S. Indicators of inflammation in the diagnosis of mastitis. Vet. Res. 34 (2003) 565-578
31. L'Abbe M.R., and Friel J.K. Superoxyde dismutase and glutathione peroxidase content of human milk from mothers of premature and full-term infants during the first 3 months of lactation. J. Pediatr. Gastroenterol. Nutr. 31 (2000) 270-274
32. Filipović D., Kasapović J., Pejić S., Nićiforović A., Pajović S.B., and Radojčić M.B. Superoxide dismutase activity in various fractions of full bovine milk. Acta Aliment. 34 3 (2005) 219-226
33. Kasapovic J., Pejic S., Marija M., and Radlovic N. Superoxyde dismutase activity in colostrum, transitional and mature human milk. Turk. J. Pediatr. 47 (2005) 343-347
34. Kovaceva J., Platenik J., Vejrazka M., Stipek S., Ardan T., Cejka C., Midelfart A., and Cejkova J. Differences in activities of antioxidant superoxide dismutase, glutathione peroxidase and prooxidant xanthine oxidoreductase/xanthine oxidase in the normal corneal epithelium of various mammalia. Physiol. Res. 56 (2007) 105-112
35. Hicks C.L. Occurrence and consequence of superoxide dismutase in milk products: a review. J. Dairy Sci. 63 (1980) 1199-1204
36. Koryka-Dahl M., Richardson T., and Hicks C.L. Superoxide dismutase activity in bovine milk serum. J. Food Prot. 42 (1979) 867-871
37. Holbrook J., and Hicks C.L. Variation of superoxide dismutase in bovine milk. J. Dairy Sci. 61 (1978) 1072-1077
38. Boulanger V., Zhao X., and Lacasse P. Protective effect of melatonin and catalase in bovine neutrophil-induced model of mammary cell damage. J. Dairy Sci. 85 (2002) 562-569
39. Kitchen B.J., Taylor G.C., and White I.C. Milk enzymes: their distribution and activity. J. Dairy Res. 37 (1970) 279-288
40. Read R.B., Reyes A.L., Bradshaw J.G., and Peeler J.T. Evaluation mastitis. J. Dairy Sci. 52 (1969) 1359-1367
41. Phillips J.D., and Griffiths M.W. A note on the use of the Catalasemetre in assessing the quality of milk. J. Appl. Bacteriol. 62 (1987) 223-226
42. Silanikove N., Shapiro F., Shamay A., and Leitner G. Role of xanthine oxidase, lactoperoxidase, and NO in the innate immune system of mammary secretion during active involution in dairy cows: manipulation with casein hydrolyzates. Free Radic. Biol. Med. 38 (2005) 1139-1151
43. Johsen H.A. The composition of milk. In: Webb B.H., Johsen A.H., and Alford J.A. (Eds). Fundamentals of Dairy Chemistry. second ed. (1974), AVI Publishing Co. Inc., Westport, CT, USA 1-57
44. Hirvi Y., and Griffiths M.W. Milk catalase activity as an indicator of thermization treatments used in the manufacture of Cheddar cheese. J. Dairy Sci. 81 (1998) 338-345
45. Esworthy R.S., Chu F.F., Geiger P., Girrotti A.W., and Doroshow J.H. Reactivity of plasma glutathione peroxidase with hydroperoxidase substrates and glutathione. Arch. Biochem. Biophys. 307 (1993) 29-34
46. Burk R.F. Selenium-dependent glutathione peroxidases. In: Guengerich F.P. (Ed). Biotransformation vol. 3 (1997), Pergamon Press, Oxford, UK 229-242
47. Chen J., Lindmark-Månsson H., and Akesson B. Optimisation of a coupled enzymatic assay of glutathione peroxidase activity in bovine milk and whey. Int. Dairy J. 10 (2000) 347-351
48. Hojo Y. Sequential study on glutathione peroxidase selenium contents of human milk. Total Environ. 52 (1986) 83-91
49. Debski B., Picciano M.F., and Milner J.A. Selenium content and distrusting of human, cow and goat milk. J. Nutr. 117 (1987) 1091-1097
50. Bhattacharya I.D., Pacciano M.F., and Milner J.A. Characteristics of human milk glutathione peroxidase. Biol. Trace Element Res. 18 (1988) 59-70
51. Paape M., Bennerman D.D., Zahoo X., and Lee J.W. The bovine neutrophile: Structure and function in blood and milk. Vet. Res. 34 (2003) 597-627
52. Person K., Larson I., and Hallen Sandgren C. Effects of certain inflammatory mediators on bovine neutrophile migration in vivo and in vitro. Vet. Immunol. Immunopathol. 3 (1993) 99-112
53. Smith J.A. Neutrophils, host defense, and inflammation: A double-edged sword. J. Leukoc. Biol. 56 (1994) 672-686
54. Chance B., Sies H., and Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59 (1979) 527-605
55. Michiels C., Raes M., Toussaint O., and Remacle J. Importance of Se-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress. Free Radic. Biol. Med. 17 (1994) 235-248