Hostname: page-component-848d4c4894-pjpqr Total loading time: 0 Render date: 2024-07-02T07:14:15.541Z Has data issue: false hasContentIssue false
  • English
  • Français

Protein metabolism in lambs from lines divergently selected for weaning weight

Published online by Cambridge University Press:  27 March 2009

V. H. Oddy ,
P. A. Speck ,
H. M. Warren  and
P. C. Wynn
V. H. Oddy
Affiliation:
1NSW AgricultureElizabeth Macarthur Agricultural InstitutePMB 8Camden 2570 NSWAustralia
P. A. Speck
Affiliation:
2Department of Animal ScienceUniversity of New EnglandArmidale 2351 NSWAustralia
H. M. Warren
Affiliation:
1NSW AgricultureElizabeth Macarthur Agricultural InstitutePMB 8Camden 2570 NSWAustralia
P. C. Wynn
Affiliation:
3CSIRO Division of Animal ProductionLocked Bag 1Delivery CentreBlacktown 2148 NSWAustralia
Get access Rights & Permissions [Opens in a new window]

Summary

The physiological consequences of selection for weaning weight were investigated using 14-month-old castrated male Merino lambs from lines selected for (W +) and against (W – ) weight at weaning for over 10 generations. The selection experiment commenced in 1953 and was conducted at Trangie, NSW, Australia. Lambs from these lines now differ by 42% in weight at weaning and maturity, and have a proportionately similar composition of protein, fat and ash in their bodies at similar stages of maturity. In the whole body, there were no apparent between-strain differences in protein synthesis, but W + lambs had lower (P < 0·05) rates of phenylalanine oxidation than W – lambs. In hind limb muscle, protein metabolism of W + lambs was more responsive to food intake than in W – lambs. In particular, the rate of change of protein degradation differed (P < 0·05) between the lines in response to food intake per unit liveweight with protein degradation decreasing with increased feed intake in W + lambs. W + lambs had lower (P < 0·05) rates of blood flow to, and used less (P < 0·05) oxygen per kg hind limb muscle than W— lambs. Endocrine differences between the lines included increased (P < 0·05) plasma insulin-like growth factor-I (IGF-1) concentration in W + compared to W— lambs and, from regression analysis, an indication that there was a higher (P < 0·01) response in hind limb protein gain to insulin in the W + lambs.

These results suggest that selection for weaning weight has altered the dynamics of protein metabolism in lambs, principally through alterations in protein breakdown in muscle. Moreover, they suggest that there are associated genetic differences in endocrine control of protein metabolism which involve insulin and possibly IGF-I.

Type
Animals
Information
The Journal of Agricultural Science , Volume 124 , Issue 1 , February 1995 , pp. 129 - 137
Copyright
Copyright © Cambridge University Press 1995

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

Baker, R. L., Peterson, A. J., Bass, J. J., Amyes, N. C., Breier, B. H. & Gluckman, P. D. (1991). Replicated selection for insulin-like growth factor-I and body weight in mice. Theoretical and Applied Genetics 81, 685–692.CrossRefGoogle Scholar
Barrett, E. J., Revkin, J. H., Young, L. H., Zaret, B. L., Jacob, R. & Gelfand, R. A. (1987). An isotopic method for measurement of muscle protein synthesis and degradation in vivo. Biochemical Journal 245, 223–228.CrossRefGoogle ScholarPubMed
Baxter, R. C. & Martin, J. L. (1989). Structure of the Mr 140,000 growth hormone-dependent insulin-like growth factor binding protein complex: determination by reconstitution and affinity-labeling. Proceedings of the National Academy of Sciences USA 86, 6898–6902.CrossRefGoogle ScholarPubMed
Blair, H. T., McCutcheon, S. N., Mackenzie, D. D. S., Gluckman, P. D., Ormsby, J. E. & Breier, B. H. (1989). Responses to divergent selection for plasma concentrations of insulin-like growth factor-I in mice. Genetical Research, Cambridge 53, 187–191.CrossRefGoogle ScholarPubMed
Blair, H. T., McCutcheon, S. N. & MaCkenzie, D. D. S. (1990). Physiological predictors of genetic merit. Proceedings of the Australasian Association of Animal Breeding and Genetics 8, 133–142.Google Scholar
Chan, C. P., Hansen, R. J. & Stern, J. S. (1985). Protein turnover in insulin-treated, alloxan-diabetic lean and obese Zucker rats. Journal of Nutrition 115, 959–969.CrossRefGoogle ScholarPubMed
Cocimano, M. R. & Leng, R. A. (1967). Metabolism of urea in sheep. British Journal of Nutrition 21, 353–371.CrossRefGoogle ScholarPubMed
Daughaday, W. H., Mariz, I. K. & Blethen, S. L. (1980). Inhibition of access of bound somatomedin to membrane receptor and immunobinding sites: a comparison of radioreceptor and radioimmunoassay of somatomedin in native and acid-ethanol-extracted serum. Journal of Clinical Endocrinology and Metabolism 51, 781–788.CrossRefGoogle Scholar
Davis, G. P. (1987). Genetic relationships between lamb growth and lifetime productivity in Merino sheep. PhD thesis, The University of New England, Armidale.Google Scholar
Douglas, R. G., Gluckman, P. D., Ball, K. T., Breier, B. H. & Shaw, J. H. F. (1991). The effects of infusion of IGF-I, IGF-II and insulin on glucose and protein metabolism in fasted lambs. Journal of Clinical Investigation 88, 614–622.CrossRefGoogle ScholarPubMed
Elgenmann, J. E., Patterson, D. F. & Froesch, E. R. (1984). Body size parallels insulin-like growth factor I levels but not growth hormone secretory capacity. Ada Endocrinologica 106, 448–453.Google Scholar
Fuller, M. F., Reeds, P. J., Cadenhead, A., Seve, B. & Preston, T. (1987). Effects of the amount and quality of dietary protein on nitrogen metabolism and protein turnover of pigs. British Journal of Nutrition 58, 287–300.CrossRefGoogle ScholarPubMed
Gilmour, A. R. (1988). REG – a Generalised Linear Models Program. Miscellaneous Bulletin No. 1, Department of Agriculture, New South Wales.Google Scholar
Herd, R. M., Oddy, V. H. & Lee, G. J. (1993). Effect of divergent selection for weaning weight on liveweight and wool growth responses to feed intake in Merino ewes. Australian Journal of Experimental Agriculture 33, 699–705.CrossRefGoogle Scholar
Lobley, G. E., Harris, P. M., Skene, P. A., Brown, D., Milne, E., Calder, A. G., Anderson, S. E., Garlick, P. J., Nevison, I. & Connell, A. (1992). Responses in tissue protein synthesis to sub- and supra-maintenance intake in young growing sheep: comparison of large-dose and continuous-infusion techniques. British Journal of Nutrition 68, 373–388.CrossRefGoogle ScholarPubMed
Lund-Larsen, T. B. & Bakke, H. (1975). Growth hormone and somatomedin activities in lines of pigs selected for rate of gain and thickness of backfat. Ada Agriculturae Scandinavica 25, 231–234.CrossRefGoogle Scholar
Maruyama, K., Sunde, M. L. & Swick, R. W. (1978). Growth and muscle protein turnover in the chick. Biochemical Journal 176, 573–582.CrossRefGoogle ScholarPubMed
McCarthy, F. D., Bergen, W. G. & Hawkins, D. R. (1983). Muscle protein turnover in cattle of differing genetic backgrounds as measured by urinary NT-methylhistidine excretion. Journal of Nutrition 113, 2455–2463.CrossRefGoogle Scholar
Merimee, T. J., Zapf, J., Hewlett, B. & Cavalii-Sforza, L. L. (1987). Insulin-like growth factors in pygmies. New England Journal of Medicine 316, 906–911.CrossRefGoogle ScholarPubMed
Ministry of Agriculture, Fisheries and Food (1975). Energy Allowances and Feeding Systems for Ruminants. MAFF Technical Bulletin No. 33. London: HMSO.Google Scholar
Oddy, V. H. (1993). Regulation of muscle protein metabolism in sheep and lambs: nutritional, endocrine and genetic aspects. Australian Journal of Agricultural Research 44, 901–913.CrossRefGoogle Scholar
Oddy, V. H. & Lindsay, D. B. (1986). Determination of rates of protein synthesis, gain and degradation in intact hind-limb muscle of lambs. Biochemical Journal 233, 417–425.CrossRefGoogle ScholarPubMed
Oddy, V. H., Brown, B. W. & Jones, A. W. (1981). Measurement of organ blood flow using tritiated water. I. Hind limb muscle blood flow in conscious ewes. Australian Journal of Biological Sciences 43, 419–425.CrossRefGoogle Scholar
Oddy, V. H., Jones, A. W. & Warren, H. M. (1988). Phenylalanine as a marker of muscle protein synthesis. Proceedings of the Nutrition Society of Australia 13, 119.Google Scholar
Oddy, V. H., Speck, P. A., Warren, H. M. & Ewoldt, C. L. (1989 a). Decreased muscle and whole body protein breakdown in lambs with genetically high weaning weight. Proceedings of the Nutrition Society of Australia 14, 107.Google Scholar
Oddy, V. H., Warren, H. M., Ewoldt, C. L. & Riley, K. D. (1989 b). Pre-weaning growth and body composition of lambs genetically different in weight at weaning. Proceedings of the Nutrition Society of Australia 14, 139.Google Scholar
Oddy, V. H., Warren, H. M., Moyes, K. J. & Owens, P. C. (1991). 1GF-I inhibits muscle protein breakdown in sheep. Proceedings of the 2nd International IGF Symposium, Abstract D13, p. 281.Google Scholar
Owens, P. C., Johnson, R. J., Campbell, R. G. & Ballard, F. J. (1990). Growth hormone increases insulin-like growth factor-I (1GF-1) and decreases IGF-II in plasma of growing pigs. Journal of Endocrinology 124, 269–275.CrossRefGoogle Scholar
Pattie, W. A. & Williams, A. J. (1966). Growth and efficiency of post-weaning gain in lambs from Merino flocks selected for high and low weaning weight. Proceedings of the Australian Society of Animal Production 6, 305–309.Google Scholar
Perry, B. N. (1978). The incorporation of radioactively labelled amino acids into skeletal muscle protein by Pietrain and Large White pigs. Journal of Agricultural Science, Cambridge 84, 191–200.CrossRefGoogle Scholar
Siddiqui, R. A., Blair, H.T., McCutcheon, S. N., Mackenzie, D. D. S., Gluckman, P. D. & Breier, B. H. (1990). Developmental patterns of plasma insulin-like growth factor-I (IGF-I) and body growth in mice from lines divergently selected on the basis of plasma IGF-I. Journal of Endocrinology 124, 151–158.CrossRefGoogle ScholarPubMed
Speck, P. A., Oddy, V. H. & Wynn, P. C. (1989). Insulinrole in regulation of growth potential? Proceedings of the Nutrition Society of Australia 14, 108.Google Scholar
Speck, P. A., Oddy, V. H. & Wynn, P. C. (1990). Insulinregulation of growth potential? Proceedings of the Australian Society of Animal Production 18, 552.Google Scholar
Speck, P. A., Oddy, V. H., Hinch, G. N. & Wynn, P. C. (1991 a). Prolonged selection for liveweight gain alters insulin and GH receptor characteristics and circulating IGF-I levels in sheep. Proceedings of the US Endocrine Society, Abstract 1316.Google Scholar
Speck, P. A., Wynn, P. C., Hinch, G. N. & Oddy, V. H. (1991 b). Circulating IGF-I is correlated with body size, but not muscle protein gain in sheep selected for and against growth potential. Proceedings of the 2nd International IGF Symposium, Abstract D25, p. 293.Google Scholar
Thompson, J. M., Parks, J. R. & Perry, D. (1985). Food intake, growth and body composition in Australian Merino sheep selected for high and low weaning weight. Animal Production 40, 55–70.Google Scholar
Tomas, F. M., Jones, L. M. & Pym, R. A. (1988 a). Rates of muscle protein breakdown in chickens selected for increased growth rate, food consumption or efficiency of food utilisation as assessed by NT-methylhistidine excretion. British Poultry Science 29, 359–370.CrossRefGoogle ScholarPubMed
Tomas, F. M., Quinn, S. L. & Chandler, C. S. (1988 b). Effect of protein deficiency on muscle protein turnover in fast and slow growing rats. Proceedings of the Nutrition Society of Australia 13, 120.Google Scholar
Vandehaar, M. J., Moats-Staats, B. M., Davenport, M. L., Walker, J. L., Ketelslegers, J.-M., Sharma, B. K. & Underwood, L. E. (1991). Reduced serum concentrations of insulin-like growth factor-I (IGF-I) in protein-restricted growing rats are accompanied by reduced IGF-I mRNA levels in liver and skeletal muscle. Journal of Endocrinology 130, 305–312.CrossRefGoogle ScholarPubMed
Waterlow, J. C., Garlick, P. J. & Mill Ward, D. J. (1978). Protein Turnover in Mammalian Tissues and in the Whole Body. Amsterdam: North-Holland.Google Scholar