The Red Blood Cell Membrane Proteins in Rabbits with Experimental Ketosis

This study investigated the effects of experimentally induced ketosis on erythrocyte membrane proteins in rabbits by sodium dodecyl sulfate/polyacrylamide gel electrophoresis (SDS-PAGE). The animals were allocated to 2 groups; ketosis and control. The experiment was lasted 13 days. Food was withheld for 5 days in the ketosis group, and then the animals were fed for 8 days. The control group was fed standard rabbit rations. Erythrocyte membrane proteins were isolated from the blood, and analyzed by SDS-PAGE using 10% (w/v) acrylamide monomer. Erythrocyte membrane proteins separated on the polyacrylamide gel were quantified by densitometry. Band 3 and actin on day 1, and spectrin on day 5 were significantly increased (P < 0.05), while glyceraldehyde-3-phosphate dehydrogenase (G3PD, E.C. 1.2.1.12) was significantly decreased (P < 0.01) on day 5 in the ketosis group. On the other hand, ankyrin increased (P < 0.05) when compared to the controls on day 6 of the trial. The results show that ketosis may lead to quantitative changes in erythrocyte membrane proteins including band 3, actin, spectrin, G3PD and ankyrin.

The Red Blood Cell Membrane Proteins in Rabbits with Experimental Ketosis

This study investigated the effects of experimentally induced ketosis on erythrocyte membrane proteins in rabbits by sodium dodecyl sulfate/polyacrylamide gel electrophoresis (SDS-PAGE). The animals were allocated to 2 groups; ketosis and control. The experiment was lasted 13 days. Food was withheld for 5 days in the ketosis group, and then the animals were fed for 8 days. The control group was fed standard rabbit rations. Erythrocyte membrane proteins were isolated from the blood, and analyzed by SDS-PAGE using 10% (w/v) acrylamide monomer. Erythrocyte membrane proteins separated on the polyacrylamide gel were quantified by densitometry. Band 3 and actin on day 1, and spectrin on day 5 were significantly increased (P < 0.05), while glyceraldehyde-3-phosphate dehydrogenase (G3PD, E.C. 1.2.1.12) was significantly decreased (P < 0.01) on day 5 in the ketosis group. On the other hand, ankyrin increased (P < 0.05) when compared to the controls on day 6 of the trial. The results show that ketosis may lead to quantitative changes in erythrocyte membrane proteins including band 3, actin, spectrin, G3PD and ankyrin.

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  • Lean, I.J., Bruss, M.L., Baldwin, R.L., Troutt, H.F.: Bovine
  • ketosis: a review. I. Epidemiology and pathogenesis. Vet. Bull., 1991; 61: 1209-1218.
  • Oresnik, A.: Effect of health and reproductive disorders on milk yield and fertility in dairy cows. Bovine Pract., 1995; 29: 43-45.
  • Singh, B., Kasaralikar, V.R.: Biochemistry and treatment of
  • clinical ketosis in buffaloes ( 67: 163-165.
  • Vrzgula, L.: Metabolic disorders and their prevention in farm animals. Dev. Anim. Vet. Sci., 1991; 24: 68-76.
  • Anantwar, L.G., Bhoop, S., Singh, B.: Epidemiology, clinico- pathology and treatment of sub-clinical ketosis in buffaloes (Bubalus bubalis). Indian Vet. J., 1994; 71: 56-60.
  • Ergun, H.: Çeflitli yaflama payı enerji düzeyinde beslenen
  • danalarda açlığın kan keton cisimleri, plazma glikoz ve yağ asiti değerleri ile canlı ağırlığa etkisi (ketozis oluflumu) üzerine arafltırmalar, Doçentlik tezi, Ankara Üniv., 1982, 25-50.
  • Erkurt, A.: Tavflanlarda deneysel ketozis olgularında ve ketozisli ineklerde kanda lipit peroksidasyonu ve enzimatik antioksidan sistemler (katalaz, süperoksitdismutaz, glutathion peroksidaz, malondialdehid). Doktora Tezi, Ankara Üniv., 1998, 67-121.
  • Christopher, M.M., Broussard, J.D., Peterson, M.E.: Heinz body formation associated with ketoacidosis in diabetic cats. J. Vet. Intern. Med., 1995; 9: 24-31.
  • Jarolim, P., Lahav, M., Liu, S.C., Palek, P.: Effect of hemoglobin oxidation products on the stability of red blood cell membrane skeletons and the associations of skeletal proteins: Correlation with a release of hemin. Blood, 1990; 76: 2125-2131.
  • Dodge, J.T., Mitchell, C., Hanahan, D.J.: The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Arch. Biochem. Biophys., 1963; 100: 119-130.
  • Steck, T.L., Weinstein, R.S., Wallach, D.F.H.: Inside-out cell membrane vesicles: Preparation and purification. Science, 1970; 15: 255-257.
  • Morle, L., Garbarz, M., Alloisio, N., Girot, R., Chaveroche, I., Boivin, P., Delaunay, J.: The characterization of protein 4.1 Presles, a shortened variant of RBC membrane protein 4.1. Blood, 1985; 65: 1511-1517.
  • Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J.: Protein measurement with the folin phenol reagent. J. Biol. Chem., 1951; 193: 265-275.
  • Laemmli, U.K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 1970; 227: 680-685.
  • Calvin, S.E., Wolf, C., Minneapolis, M. N.: Does fasting in pregnant sheep cause a syndrome analogous to human preeclampsia. Online J. Vet. Res., 1999; 1: 45-53.
  • Liu, S.C., Yi, S.J., Mehta, J.R., Nichols, P.E., Ballas, S.K., Yacono, P.W., Golan, D.E., Palek, J.: Red cell membrane remodeling in sickle cell anemia. Sequestration of membrane lipids and proteins in Heinz bodies. J. Clin. Invest., 1996; 97: 29-36.
  • Bennet, V.: The spectrin-actin junction of erythrocyte membrane skeletons. Biochim. Biophys. Acta., 1989; 988: 107-121.
  • Granner, D.K.: Membranes: Structure, Assembly and Function. Harper’s Biochemistry. Murray, R.K., Granner, D.K., Mayes, P.A., Rodwell, V.W., Eds. Typopress, Lebanon, 1988, 445-452.
Turkish Journal of Veterinary and Animal Sciences-Cover
  • ISSN: 1300-0128
  • Yayın Aralığı: Yılda 6 Sayı
  • Yayıncı: TÜBİTAK