Hostname: page-component-77c89778f8-7drxs Total loading time: 0 Render date: 2024-07-18T13:32:21.467Z Has data issue: false hasContentIssue false

The effects of dietary nitrogen level on the collagen of rat skin

Published online by Cambridge University Press:  24 July 2007

R. Dawson
Affiliation:
Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB, Scotland
G. Milne
Affiliation:
Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB, Scotland
Rights & Permissions [Opens in a new window]

Abstract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

1. Male rats of approximately 120 g body-weight were maintained on a commercial stock diet containing 204 g crude protein (nitrogen × 6.25)/kg, a hydroxyproline-free high-protein (HP) diet containing 200 g casein/kg as the only protein source, or a low-protein (LP) diet containing 40 g casein/kg. After 6 weeks on these diets half of each group was transferred to a non-protein (NP) diet and the experiment was continued for a further 6 weeks. Animals from each group were killed at 4 d, 3 weeks and 6 weeks after the transfer to the NP diet.

2. Throughout the experiment the urinary excretion of N, hydroxyproline and creatinine, and the content and solubility of the skin collagen were determined.

3. When compared with a control group killed at the beginning of the experiment the rats maintained on the LP diet showed an increase of 25% in total N content of the skin but collagen content increased by 100%. Rats transferred from the HP to the NP diet lost both N and collagen from the skin, but those transferred from the LP to the NP diet lost N but increased the collagen content by 42%.

4. Protein deprivation brought about marked changes in the solubility of the skin collagen, suggesting an increase in the rate of maturation of skin collagen.

Type
Papers on General Nutrition
Copyright
Copyright © The Nutrition Society 1978

References

Anasuya, A. & Narasinga Rao, B. S. (1970). Br. J. Nutr. 24, 97.CrossRefGoogle Scholar
ARC/MRC Committee on Food and Nutrition Research (1974). Report of the ARC/MRC Committee, p. 64. London: H. M. Stationery Office.Google Scholar
Bailey, A. J. (1969). Gerontologia 15, 65.CrossRefGoogle Scholar
Bailey, A. J., Bazin, S. & Delaunay, A. (1973). Biochim. biophys. Acta 320, 383.CrossRefGoogle Scholar
Bannister, D. W. & Burns, A. B. (1970). Analyst, Lond. 95, 596.CrossRefGoogle Scholar
Čabak, V., Dickerson, J. W. T. & Widdowson, E. M. (1963). Br. J. Nutr. 17, 601.CrossRefGoogle Scholar
Dawson, R. & Milne, G. (1976 a). Proc. Nutr. Soc. 35, 81A.Google Scholar
Dawson, R. & Milne, G. (1976 b). Proc. 5th Mtg Eur. Fedn Connective Tissue Clubs Abstr. no. 133.Google Scholar
Firschein, H. E. & Shill, J. P. (1966). Analyt. Biochem. 14, 296.CrossRefGoogle Scholar
Harkness, M. L. R., Harkness, R. D. & James, D. W. (1958). J. Physiol., Lond. 144, 307.CrossRefGoogle Scholar
Love, R. M., Yamaguchi, K., Créaćh, Y. & Lavéty, J. (1976). Comp. Biochem. Physiol. 55, 487.Google Scholar
McClain, P. E., Wiley, E. R. & Beecher, G. R. (1975). Nurt. Rep. int. 12, 317.Google Scholar
Palmer, R. M., McIntosh, A. D. & Pusztai, A. (1973). J. Sci. Fd Agric. 24, 937.CrossRefGoogle Scholar
Picou, D., Halliday, D. & Garrow, J. S. (1966). Clin. Sci. 30, 345.Google Scholar
Robins, S. P. & Bailey, A. J. (1972). Biochem. Biophys. Res. Commun. 48, 76.CrossRefGoogle Scholar
Ross, M. H., Lustbader, E. & Bras, G. (1976). Nature, Lond. 262, 548.CrossRefGoogle Scholar
Sinex, F. M. (1968). In Treatise on Collagen, Vol. 2B, p. 410 [Ramachandran, G. N. editor]. London: Academic Press.Google Scholar
Technicon Instruments Co. Ltd. (1967). Technicon Method N-11 B Basingstoke, Hants: Technicon Instruments Co. Ltd.Google Scholar
Verzar, F. (1964). Int. Rev. Connective Tissue Res. 2, 243.CrossRefGoogle Scholar
Waterlow, J. C. & Stephen, J. M. L. (1966). Br. J. Nutr. 20, 461.CrossRefGoogle Scholar