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The effects of intradermal injections of spermidine on the growth rate of fibres and mitosis of wool follicles in Merino lambs

Published online by Cambridge University Press:  18 August 2016

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Abstract

Polyamines (putrescine, spermidine and spermine) are required for optimal growth in all cells, and are essential for cell proliferation and growth of cultured wool follicles, with an optimal concentration of spermidine required for the fibre elongation. The effects of a local supply of exogenous spermidine on the rate of cell division in the wool follicles, the length growth rate and diameter of fibres were therefore examined in Merino lambs. Three groups of eight lambs (40 kg) were given food at 1·2 ✕ maintenance. Spermidine was injected intradermally into a small patch (3 ✕ 3 cm) on the left flank three times per day for 7 days at one of three concentrations: 1·38, 2·75 or 4·58 џmol in 0·8 ml volume. The same volume of saline was injected into the contralateral side as a control. The concentration of spermidine in the skin patch 3 h after injection on day 7 increased by proportionately 018, 0·33 or 0·41 (P < 0001) respectively. The rates of cell division in the follicle bulb 3 h after the spermidine injection were proportionately 0104, 0184 and 0·283 higher compared with the contralateral side (P = 0078 overall) for the low, medium and high doses of spermidine respectively and differed between the three doses (P < 005). The fibre length growth rate, as measured using autoradiography, was proportionately 0099, 0117 and 0156 higher than that of the contralateral side (P < 0001 overall) for the low, medium and high doses of spermidine respectively, but differences between doses were not significant (P > 005). Spermidine injection did not result in a significant change in fibre diameter during the treatment period. The ratio of fibre length growth rate to fibre diameter was increased by the injection of spermidine (P < 0001). The results suggest that injecting extra spermidine into the skin altered spermidine homeostasis in the skin, stimulated cell proliferation and resulted in increased fibre growth.

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Research Article
Copyright
Copyright © British Society of Animal Science 2002

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References

Agricultural Research Council. 1984. The nutrient requirements of ruminant livestock. Commonwealth Agricultural Bureaux, Slough, UK.Google Scholar
Alhonen, L., Halmekyto, M., Kramer, D. L., Janne, J. and Porter, C. W. 1999. Transgenic mice with activated polyamine catabolism due to overexpression of spermidine/spermine N1-acetyltransferase show enhanced sensitivity to the polyamine analogue, N1, N11 -diethylnorspermine. Molecular Pharmacology 55: 693698.Google Scholar
Bardócz, S. and White, A. 1998. Effect of lectins on uptake of polyamines. Lectin methods and protocols (ed. Phodes, J. M. and Milton, J. D.), pp. 393405. Humana Press, New Jersey.Google Scholar
Black, J. L. and Reis, P. J. 1979. Speculation on the control of nutrient partition between wool growth and other body functions. Physiological and environmental limitations to wool growth (ed. Black, J. L. and Reis, P. J.), pp. 269294. University of New England Publishing Unit, Armidale.Google Scholar
Cooper, A. J. L. 1983. Biochemistry of sulphur-containing amino acids. Annual Review of Biochemistry 52: 187222.Google Scholar
Eliassen, K. A. 1982. Formation of polyamines in the rumen of goats during growth. Acta Veterinaria Scandinavica 23: 275294.CrossRefGoogle ScholarPubMed
Harris, P. M., Lee, J., Sinclair, B. R., Treloar, B. P. and Gurnsey, M. P. 1994. Effect of food intake on energy and protein metabolism in the skin of Romney sheep. British Journal of Nutrition 71: 647660.Google Scholar
Hynd, P. I. 1989a. Effects of nutrition on wool follicle cell kinetics in sheep differing in efficiency of wool production. Australian Journal of Agricultural Research 40: 409417.CrossRefGoogle Scholar
Hynd, P. I. 1989b. Factors influencing cellular events in the wool follicle. In The biology of wool and hair (ed. G. E. Rogers, P. J. Reis, K. A. Ward and Marshall, R. C.), pp. 169184. Chapman and Hall, London.Google Scholar
Hynd, P. I. 1994. Follicular determinants of the length and diameter of wool fibres. 1. Comparison of sheep differing in fibre length/diameter ratio at two levels of nutrition. Australian Journal of Agricultural Research 45: 11371147.Google Scholar
Hynd, P. I. and Nancarrow, M. J. 1996. Inhibition of polyamine synthesis alters hair follicle function and fibre composition. Journal of Investigative Dermatology 106: 249253.Google Scholar
Hynd, P. I., Schlink, A. C., Phillips, P. M. and Scobie, D. R. 1986. Mitotic activity in cells of the wool follicle bulb. Australian Journal of Biological Sciences 39: 329339.Google Scholar
Janne, J. 1999. Polyamines: from molecular biology to clinical applications. Polyamines in health and nutrition (ed. Bardócz, S. and White, A.), pp. 8798. Kluwer Academic Publishers, Dordrecht.Google Scholar
Janne, J., Alhonen, L., Halmekyto, M. and Peitila, M. 1999. Genetic engineering of polyamine metabolism: consequences of the activation of polyamine biosynthesis or catabolism in transgenic rodents. Polyamines in health and nutrition (ed. S., Bardócz and White, A.), pp. 8798. Kluwer Academic Publishers, Dordrecht.Google Scholar
Liu, S. M., Mata, G., Figliomeni, S., Powell, B. C., Nesci, A. and Masters, D. G. 2000. Trans-sulphuration, protein synthesis rate and follicle mRNA in the skin of young Merino lambs in response to infusions of methionine and serine. British Journal of Nutrition 83: 401409.Google Scholar
Luk, G. D. 1990. Polyamines in intestinal growth. Biochemical Society Transactions 18: 10901091.Google Scholar
MacRae, J. C., Walker, A., Brown, D. and Lobley, G. E. 1993. Accretion of total protein and individual amino acids by organs and tissues of growing lambs and the ability of nitrogen balance techniques to quantitate protein retention. Animal Production 57: 237245.Google Scholar
Mata, G., Masters, D. G., Buscall, D., Street, K. and Schlink, A. C. 1995. Responses in wool growth, liveweight, glutathione and amino acids, in Merino wethers fed increasing amounts of methionine protected from degradation in the rumen. Australian Journal of Agricultural Research 46: 11891204.CrossRefGoogle Scholar
Morgan, D. M. L. 1999. Polyamine biosynthesis, catabolism and homeostasis: an overview. Polyamines in health and nutrition (ed. Bardócz, S. and White, A.), pp. 126. Kluwer Academic Publishers, Dordrecht.Google Scholar
Muskiet, F. A. J., Dorhout, B., Berg, G. A. van den and Hessels, J. 1995. Investigation of polyamine metabolism by high-performance liquid chromatographic and gas chromatographic profiling methods. Journal of Chromatography B: Biomedical Applications 667: 189198.Google Scholar
Os, M. van, Lassalas, B., Toillon, S., Jouany, J. P. and Os, M. van. 1995. In vitro degradation of amines by rumen micro-organisms. Journal of Agricultural Science, Cambridge 125: 299305.Google Scholar
Panteleyev, A. A., Christiano, A. M., O’Brien, T. G. and Sundberg, J. P. 2000. Ornithine decarboxylase transgenic mice as a model for human atrichia with papular lesions. Experimental Dermatology 9: 146151.CrossRefGoogle Scholar
Persson, L., Dartsch, C., Wallstrom, E. L. and Svensson, F. 1999. Regulation of cellular polyamine homeostasis. Polyamines in health and nutrition (ed. Bardócz, S. and White, A.), pp. 2734. Kluwer Academic Publishers, Dordrecht.Google Scholar
Phuntsok, T., Froetschel, M. A., Amos, H. E., Zheng, M. and Huang, Y. W. 1998. Biogenic amines in silage, apparent post-ruminal passage, and the relationship between biogenic amines and digestive function and intake by steers. Journal of Dairy Science 81: 21932203.Google Scholar
Pietila, M., Alhonen, L., Halmekyto, M., Kanter, P. and Janne, J. 1997. Activation of polyamine catabolism profoundly alters tissue polyamine pools and affects hair growth and female fertility in transgenic mice overexpressing spermidine/spermine N1-acetyltransferase. Journal of Biological Chemistry 272: 1874618751.Google Scholar
Pietila, M., Parkkinen, J. J., Alhonen, L. and Janne, J. 2001. Relation of skin polyamines to the hairless phenotype in transgenic mice overexpressing spermidine/spermine N1-acetyltransferase. Journal of Investigative Dermatology 116: 801805.Google Scholar
Reis, P. J. 1979. Effects of amino acids on the growth and properties of wool. Physiological and environmental limitations to wool growth (ed. Black, J. L. and Reis, P. J.), pp. 223242. University of New England Publishing Unit, Armidale.Google Scholar
Reis, P. J. 1989. The influence of absorbed nutrients on wool growth. In The biology of wool and hair (ed. Rogers, G. E., Reis, P. J., Ward, K. A. and Marshall, R. C.), pp. 185215. Chapman and Hall, London.Google Scholar
Reis, P. J. and Hynd, P. I. 1989. The influence of a -difluoromethylornithine on the activity of wool follicles. Asian-Australian Journal of Animal Sciences 2: 204205.Google Scholar
Reis, P. J., Tunks, D. A. and Munro, S. G. 1990. Effects of the infusion of amino acids into the abomasum of sheep, with emphasis on the relative value of methionine, cysteine and homocysteine for wool growth. Journal of Agricultural Science, Cambridge 114: 5968.Google Scholar
Schlink, A. C., Mata, G., Lea, J. M. and Ritchie, A. J. M. 1999. Seasonal variations in fibre diameter and length in wool of grazing Merino sheep with low or high staple strength. Australian Journal of Experimental Agriculture 39: 507517.CrossRefGoogle Scholar
Seiler, N. 1990. Polyamine metabolism. Digestion 46: 319330.Google Scholar
Seiler, N., Delcros, J. G. and Moulinoux, J. P. 1996. Polyamine transport in mammalian cells. An update. International Journal of Biochemistry and Cell Biology 28: 843861.Google Scholar
Shipe, J. R., Hunt, J. D. F. and Savory, J. 1979. Plasma polyamines determined by negative-ion chemical ionization/mass spectrometry. Clinical Chemistry 25: 15641571.Google Scholar
Stipanuk, M. H. 1986. Metabolism of sulphur-containing amino acids. Annual Review of Nutrition 6: 179209.CrossRefGoogle Scholar
Suppola, S., Pietila, M., Parkkinen, J. J., Korhonen, V. P., Alhonen, L., Halmekyto, M., Porter, C. W. and Janne, J. 1999. Overexpression of spermidine N1-acetyltransferase under the control of mouse metallothionein I promoter in transgenic mice: evidence for a striking post-transcriptional regulation of transgene expression by a polyamine analogue. Biochemical Journal 338: 311316.Google Scholar
Tabor, C. W. and Tabor, H. 1984. Polyamines. Annual Review of Biochemistry 53: 749790.Google Scholar
Wallace, H. M. 1996. Polyamines in human health. Proceedings of the Nutrition Society 55: 419431.Google Scholar
White, A. and Bardócz, S. 1999. Estimation of the polyamine body pool: contribution by de novo biosynthesis, diet and luminal bacteria. Polyamines in health and nutrition (ed. Bardócz, S. and White, A.), pp. 117122. Kluwer Academic Publishers, Boston.Google Scholar
Williams, A. J. and Winston, R. J. 1987. A study of the characteristics of wool follicle and fibre in Merino sheep genetically different in wool production. Australian Journal of Agricultural Research 38: 743755.Google Scholar