Hostname: page-component-84b7d79bbc-l82ql Total loading time: 0 Render date: 2024-07-26T03:18:26.070Z Has data issue: false hasContentIssue false
  • English
  • Français

Collagen metabolism in folic acid deficiency

Published online by Cambridge University Press:  24 July 2007

J. G. A. J. Hautvast  and
M. J. Barnes
J. G. A. J. Hautvast
Affiliation:
MRC Dunn Nutrition Unit, Dunn Nutritional Laboratory, University of Cambridge and Medical Research Council, Milton Road, Cambridge
M. J. Barnes
Affiliation:
MRC Dunn Nutrition Unit, Dunn Nutritional Laboratory, University of Cambridge and Medical Research Council, Milton Road, Cambridge
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. The effect of folic acid deficiency on collagen formation, with respect to the level of collagen-protein synthesis and the extent of collagen-proline hydroxylation, has been studied. A folic acid-free diet containing 10 g sulphasuxidine/kg was used to induce folate deficiency in young male rats. Animals were judged folic acid-deficient on the grounds of retardation of growth, characteristic haematological changes and the urinary excretion of formimino-L-glutamic acid.

2. From isotope incorporation studies it was found that folic acid deficiency caused a marked impairment in collagen synthesis. It was shown, however, from the use of pair-fed control animals, that this was due in part to a reduced food intake accompanying the vitamin deficiency. The further reduction in synthesis in addition to that attributable to inanition was considered to arise from an involvement of folic acid in general protein synthesis, since it was found that the synthesis of elastin and non-collagenous skin proteins was similarly impaired.

3. Reduced synthesis of collagen was not considered attributable to lack of hydroxylation of peptidyl proline that may occur in ascorbic acid deficiency. Hydroxylation of collagen- and elastin-proline was only very slightly impaired in folic acid deficiency. It was concluded that, at least when ascorbic acid is present, folic acid is not directly essential for the hydroxylation, in vivo, of peptidyl proline. The results support the view that ascorbic acid participates direct, in vivo, in this hydroxylation rather than indirect by simply maintaining an adequate level of reduced folates. They do not, however, exclude the possibility, arising from the known ability of tetrahydrofolate to participate in the hydroxylation of collagen proline in vitro, that when both ascorbate and folate are present, the latter may, in some measure, share in the role of reducing agent in the hydroxylation of peptidyl proline in vivo.

Type
General Nutrition
Information
British Journal of Nutrition , Volume 32 , Issue 2 , September 1974 , pp. 457 - 469
Copyright
Copyright © The Nutrition Society 1974

References

REFERENCES

Barnes, M. J., Constable, B. J. & Kodicek, E. (1969). Biochem. J. 113, 387.CrossRefGoogle Scholar
Barnes, M. J., Constable, B. J., Morton, L. F. & Kodicek, E. (1970). Biochem. J. 119, 575.CrossRefGoogle Scholar
Barnes, M. J. & Kodicek, E. (1972). Vitams Horm. 30, I.Google Scholar
Bergman, I. & Loxley, R. (1963). Analyt. Chem. 35, 1961.CrossRefGoogle Scholar
Broquist, H. P., Stokstad, E. L. R. & Jukes, T. H. (1951). J. Lab. clin. Med. 38, 95.Google Scholar
Brown, G. M. (1971). Adv. Enzymol. 35, 35.Google Scholar
Clegg, J. W. & King, E. J. (1942). Br. med. J. ii, 329.CrossRefGoogle Scholar
Cox, E. V. (1968). Vitams Horm. 26, 635.CrossRefGoogle Scholar
Craig, L. C., King, T. P. & Stracher, A. (1957). J. Am. chem. Soc. 79, 3729.CrossRefGoogle Scholar
Gabuzda, C. J., Philips, G. B., Schilling, R. F. R. & Davidson, C. I. (1951). J. clin. Invest. 31, 756.CrossRefGoogle Scholar
Gould, B. S. (1970). In Chemistry and Molecular Biology of the Intercellular Matrix Vol. I, p. 431. [Balazs, E. A., editor]. London and New York: Academic Press.Google Scholar
Hautvast, J. G. A. J & Barnes, M. J. (1972). Int. Congr. Nutr. IX, Mexico City, Abstr.Google Scholar
Herbert, V. & Bertino, J. R. (1967). In The Vitamins Vol. 7, 2nd ed., p. 243 [Gyorgy, P. and Pearson, W. N. editors]. New York and London: Academic Press.CrossRefGoogle Scholar
Hutton, J. J., Tappel, A. L. & Udenfriend, S. (1967). Archs Biochem. Biophys. 118, 231.CrossRefGoogle Scholar
Ikeda, M., Fahien, L. A. & Udenfriend, S. (1966). J. biol. Chem. 241, 4452.CrossRefGoogle Scholar
Kennedy, J. F. (1969). Experientia 25, 1120.CrossRefGoogle Scholar
Kaufman, S. (1971). Adv. Enzymol. 35, 245.Google Scholar
Kodicek, E. & Carpenter, K. J. (1950). Blood 5, 522.CrossRefGoogle Scholar
Lovenberg, W., Bensinger, R. E., Jackson, R. L. & Daly, J. W. (1971). Analyt. Biochem. 43, 269.CrossRefGoogle Scholar
May, C. D., Hamilton, A. & Stewart, C. T. (1952). Blood 7, 978.CrossRefGoogle Scholar
Nakashima, Y., Suzue, R., Sanada, H. & Kawada, S. (1970). J. Vitam. 16, 276.CrossRefGoogle Scholar
Nichol, C. A. & Welch, A. D. (1950). Proc. Soc. exp. Biol. Med. 74, 52.CrossRefGoogle Scholar
Priest, R. E. & Bublitz, C. (1967). Lab. Invest. 17, 371.Google Scholar
Prockop, D. J. (1970). In Chemistry and Molecular Biology of the Intercellular Matrix Vol. I, p. 335 [Balazs, E. A. editor]. London and New York: Academic Press.Google Scholar
Rabinowitz, J. C. & Tabor, H. (1958). J. biol. Chem. 233, 252.CrossRefGoogle Scholar
Shiota, T. (1971). In Comprehensive Biochemistry Vol. 21, p. III [Florkin, M. and Stotz, E. H. editors]. Amsterdam: Elsevier.Google Scholar
Stokstad, E. L. R. (1968). Vitams Horm. 26, 443.CrossRefGoogle Scholar
Stokstad, E. L. R. & Koch, J. (1967). Physiol. Rev. 47, 83.CrossRefGoogle Scholar
Stone, K. J. & Townsley, B. H. (1973). Biochem. J. 131, 611.CrossRefGoogle Scholar
Tabor, H. & Wyngarden, L. (1958). J. clin. Invest. 37, 824.CrossRefGoogle Scholar
Udenfriend, S. (1970). In Chemistry and Molecular Biology of the Intercellular Matrix Vol. 1, p. 371 [Balazs, E. A. editor]. London and New York: Academic Press.Google Scholar
Vilter, P. W. (1964). Medicine, Baltimore 43, 727.CrossRefGoogle Scholar
Welch, A. D., Nichol, C. A., Anker, R. M. & Boehne, J. W. (1951). J. Pharmac. exp. Ther. 103, 403.Google Scholar