Hostname: page-component-cd9895bd7-jn8rn Total loading time: 0 Render date: 2024-12-27T09:54:41.642Z Has data issue: false hasContentIssue false
  • English
  • Français

Effect of litter size and bacitracin administration on tissue protein synthesis of lactating rabbit does

Published online by Cambridge University Press:  23 August 2010

L. Abecia ,
G. E. Lobley ,
A. Belenguer ,
M. Fondevila ,
N. R. McEwan  and
J. Balcells
L. Abecia*
Affiliation:
Facultad de Veterinaria, Departamento de Producción Animal y Ciencia de los Alimentos, University of Zaragoza, Miguel Servet 177, 50013, Zaragoza, Spain Metabolic Health Group, Rowett Institute of Nutrition and Health, University of Aberdeen, Bucksburn, Aberdeen AB21 9SB, UK
G. E. Lobley
Affiliation:
Metabolic Health Group, Rowett Institute of Nutrition and Health, University of Aberdeen, Bucksburn, Aberdeen AB21 9SB, UK
A. Belenguer
Affiliation:
Nutrition and Production of Herbivores, Instituto de Ganadería de Montaña (CSIC – Universidad de León), Finca Marzanas s/n. 24346 Grulleros, León, Spain
M. Fondevila
Affiliation:
Facultad de Veterinaria, Departamento de Producción Animal y Ciencia de los Alimentos, University of Zaragoza, Miguel Servet 177, 50013, Zaragoza, Spain
N. R. McEwan
Affiliation:
Metabolic Health Group, Rowett Institute of Nutrition and Health, University of Aberdeen, Bucksburn, Aberdeen AB21 9SB, UK Institute of Biological, Environmental and Rural Sciences, Aberystwyth University, Aberystwyth, SY23 3AL, Wales, UK
J. Balcells
Affiliation:
Facultad de Veterinaria, Departamento de Producción Animal y Ciencia de los Alimentos, University of Zaragoza, Miguel Servet 177, 50013, Zaragoza, Spain
*
†E-mail: labecia@unizar.es
Get access

Abstract

Bacitracin is an antibiotic used in rabbit husbandry to control microbial digestive pathologies. Collateral effects on absorption and mucosal development have been reported and these may impact on protein metabolism. This study aims to analyse the effect of the antibiotic on protein synthesis in lactating does because mammary gland metabolism and milk output should provide a sensitive index of any undesirable action of bacitracin. Rates of protein synthesis were measured in mammary gland, liver, intestinal mucosa and muscle of lactating rabbits does by injecting a flooding dose of [2H5]phenylalanine into the auricular artery of two groups (each n = 8) of New Zealand White does fed different experimental diets. The control group (C) received the basal diet and the bacitracin group (B) ingested the same diet but supplemented with bacitracin (100 mg/kg). Animals received the experimental diet from day 28 of pregnancy until day 26 of lactation when they were slaughtered. Just after birth, litter size was adjusted by cross-fostering either to five or nine pups (four does per dietary treatment). The relative weight of the liver tended to be greater in those females receiving the B diet (27 v. 22.5 g/kg BW; P < 0.07), while diet did not affect mammary gland weight (255.7 ± 10.59 g). Fractional protein synthesis rate (FSR) was higher for intestinal mucosa (duodenum; 51.7% ± 2.09%/day) followed by mammary gland and liver (38.29 ± 2.62%/day and 40.2 ± 1.98%/day, respectively), and the lowest value was observed in muscle (2.92 ± 0.26%/day; P < 0.0001). Bacitracin treatment lowered FSR in the mammary gland by 23% (P = 0.024) and this was independent of litter size. Conversely, FSR in the duodenum was not affected by antibiotic treatment but reduced by 15% (P = 0.021) for the larger litter size.

Keywords

protein synthesismammary tissueliverrabbits does
Type
Full Paper
Information
animal , Volume 5 , Issue 1 , January 2011 , pp. 100 - 106
Copyright
Copyright © The Animal Consortium 2010

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Abecia, L, Balcells, J, Fondevila, M, Belenguer, A, Calleja, L 2005. Effect of therapeutic doses of antibiotics in the diet on the digestibility and caecal fermentation in growing rabbits. Animal Research 54, 307–314.CrossRefGoogle Scholar
Abecia, L, Fondevila, M, Balcells, J, Edwards, JE, Newbold, CJ, McEwan, NR 2007. Effect of antibiotics on the bacterial population of the rabbit caecum. FEMS Microbiology Letters 272, 144–153.CrossRefGoogle ScholarPubMed
Abecia, L, Balcells, J, Fondevila, M, Belenguer, A, Holtrop, G, Lobley, GE 2008. Contribution of gut microbial lysine to liver and milk amino acids in lactating does. British Journal of Nutrition 100, 977–983.CrossRefGoogle ScholarPubMed
Association of Official Analytical Chemists 1995. Official methods of analysis, 16th edition. AOAC, Washington, DC, USA.Google Scholar
Attaix, D, Aurousseau, E, Manghebati, A, Arnal, M 1988. Contribution of liver, skin and skeletal muscle to whole-body protein synthesis in the young lamb. British Journal of Nutrition 60, 77–84.CrossRefGoogle ScholarPubMed
Baracos, VE, Brun-Bellut, J, Marie, M 1991. Tissue protein synthesis in lactating and dry goats. British Journal of Nutrition 66, 451–465.CrossRefGoogle ScholarPubMed
Bonser, AM, Garcia-Webb, P, Bhagat, CI 1983. Studies on the inhibitory effect of bacitracin on 125I-labelled insulin internalization in the rat hepatocyte. Biochimica et Biophysica Acta 762, 390–397.CrossRefGoogle ScholarPubMed
Calder, AG, Anderson, SE, Grant, I, McNurlan, MA, Garlick, PJ 1992. The determination of low d5-phenylalanine enrichment (0.002–0.09 atom percent excess), after conversion to phenylethylamine, in relation to protein turnover studies by gas chromatography/electron ionization mass spectrometry. Rapid Communications in Mass Spectrometry 6, 421–424.CrossRefGoogle ScholarPubMed
Connell, A, Calder, AG, Anderson, SE, McNurlan, MA, Garlick, PJ 1997. Hepatic protein synthesis in the sheep: effect of intake as monitored by use of stable-isotope-labelled glycine, leucine and phenylalanine. British Journal of Nutrition 77, 255–271.CrossRefGoogle ScholarPubMed
De Santiago, S, Hernandez Montes, H, Flores-Huerta, S, Villapando, S 1991. Changes of mammary tissue, liver and muscle of rat damns during lactation and after weaning. Journal of Nutrition 121, 37–43.CrossRefGoogle Scholar
Ericson, MC, Gafford, J, Elbein, AD 1978. Bacitracin inhibits the synthesis of lipid-linked saccharides and glycoproteins in plants. Plant Physiology 62, 373–376.CrossRefGoogle ScholarPubMed
Garlick, PJ, Millward, DJ, James, WP 1973. The diurnal response of muscle and liver protein synthesis in vivo in meal-fed rats. Biochemical Journal 136, 935–945.CrossRefGoogle ScholarPubMed
Garlick, PJ, McNurlan, MA, Preedy, VR 1980. A rapid and convenient technique for measuring the rate of protein synthesis in tissues by injection of [3H]phenylalanine. Biochemical Journal 192, 719–723.CrossRefGoogle ScholarPubMed
Grabowski, H, Le Bars, D, Chene, N, Attal, J, Malienou-Ngassa, R, Puissant, C, Houdebine, LM 1991. Rabbit whey acidic protein concentration in milk, serum, mammary gland extract, and culture medium. Journal of Dairy Science 74, 4143–4150.CrossRefGoogle ScholarPubMed
Heckemeyer, C, Solomon, SS, Barker, J, Duckworth, WC 1982. Selective antilipolytic effect of bacitracin in the isolated fat cell. Biochemical and Biophysical Research Communication 108, 336–343.CrossRefGoogle ScholarPubMed
Herscovics, A, Bugge, B, Jeanloz, RW 1977. Effect of bacitracin on the biosynthesis of dolichol derivatives in calf pancreas microsomes. FEBS Letters 82, 215–218.CrossRefGoogle ScholarPubMed
King, JO 1980. Effect of feeding zinc bacitracin on the fertility of rabbit does and the development of young rabbits. British Veterinary Journal 136, 240–244.CrossRefGoogle ScholarPubMed
Laurent, GJ 1982. Rates of collagen synthesis in lung, skin and muscle obtained in vivo by simplified method using [3H] proline. Biochemical Journal 206, 535–544.CrossRefGoogle ScholarPubMed
Lobley, GE 1993. Species comparisons of tissue protein metabolism: effects of age and hormonal action. Journal of Nutrition 123, 337–343.CrossRefGoogle ScholarPubMed
McKelvy, JF, LeBlanc, P, Laudes, C, Perrie, S, Grimm-Jorgensen, Y, Kordon, C 1976. The use of bacitracin as an inhibitor of the degradation of thyrotropin releasing factor and luteinizing hormone releasing factor. Biochemical and Biophysical Research Communications 73, 507–515.CrossRefGoogle ScholarPubMed
Millican, PE, Vernon, RG, Pain, VM 1987. Protein metabolism in the mouse during pregnancy and lactation. Biochemical Journal 248, 251–257.CrossRefGoogle ScholarPubMed
Millward, DJ, Garlick, PJ, Stewart, RJ, Nnanyelugo, DO, Waterlow, JC 1975. Skeletal-muscle growth and protein turnover. Biochemical Journal 150, 235–243.CrossRefGoogle ScholarPubMed
Nicholas, GA, Lobley, GE, Harris, CI 1977. Use of the constant infusion technique for measuring rates of protein synthesis in the New Zealand white rabbit. British Journal of Nutrition 38, 1–17.CrossRefGoogle ScholarPubMed
Palmer, RM, Robins, SP, Lobley, GE 1980. Measurement of the synthesis rates of collagen and total protein in rabbit muscle. Biochemical Journal 192, 631–636.CrossRefGoogle ScholarPubMed
Patthy, A, Gráf, L, Kenessey, A, Székely, JI, Bajusz, S 1977. Effect of bacitracin on the biodegradation of beta-endorphin. Biochemical and Biophysical Research Communications 79, 254–259.CrossRefGoogle ScholarPubMed
Roth, SI, Conaway, HH, Sanders, LL, Casali, RE, Boyd, AE 1980. Spontaneous diabetes mellitus in the New Zealand white rabbit: preliminary morphologic characterization. Laboratory Investigation 42, 571–579.Google ScholarPubMed
Sampson, DA, Hunsaker, HA, Jansen, GR 1986. Dietary protein quality, protein quantity and food intake: effects on lactation and on protein synthesis and tissue composition in mammary tissue and liver in rats. Journal of Nutrition 116, 365–375.CrossRefGoogle ScholarPubMed
SAS Institute Inc. 2000. Statistical Analysis System Institute Inc., SAS/STAT version 8. SAS Institute Inc., Cary, NC, USA.Google Scholar
Signoret, A, Vigneron, P, Moretti, J 1973. Metabolism of myosin in three different striated muscle types in the rabbit. Annales de Biologie Animale, Biochimie, Biophysique 13, 419–427.CrossRefGoogle ScholarPubMed
Storm, DR, Strominger, JL 1973. Complex formation between bacitracin peptides and isoprenyl pyrophosphates. The specificity of lipid-peptide interactions. Journal of Biological Chemistry 248, 3940–3945.CrossRefGoogle ScholarPubMed
Storm, DR, Strominger, JL 1974. Binding of bacitracin to cells and protoplasts of Micrococcus lysodeikticus. Journal of Biological Chemistry 249, 1823–1827.CrossRefGoogle ScholarPubMed
Waechter, CJ, Lennarz, WJ 1976. The role of polyprenol-linked sugars in glycoprotein synthesis. Annual Review of Biochemistry 45, 95–112.CrossRefGoogle ScholarPubMed
Waterlow, JC 1991. Protein-energy malnutrition: challenges and controversies. Proceedings of the Nutrition Society of India 37, 59–86.Google Scholar