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Mechanism of impaired skin collagen maturity in riboflavin or pyridoxine deficiency

Abstract

To elucidate the biochemical basis of impaired skin collagen maturity in pyridoxine-or riboflavin-deficient rats the following two mechanistic possibilities were tested: (i) Reduction in the activity of skin lysyl oxidase (EC 1·4·3·13) which initiates the cross-linking of collagen and (ii) putative rise in homocysteine level leading to neutralization of allysine (α-aminoadipic acid δ-5-semialdehyde)or hydroxyallysine (hydroxy α-aminoadepic acid (δ-semialdehyde) in collagen by the formation of thiazine complexes.

Skin lysyl oxidase activity was not affected in pyridoxine deficiency suggesting that pyridoxal phosphate may not be its cofactor. In riboflavin deficiency, lysyl oxidase activity was not altered in the newly regenerated rat skin but a slight reduction was observed in the skin of 18-day-old rat pups. This could be related to the body weight deficit rather than deficiencyper se. Aldehyde content of purified salt soluble collagen of regenerated skin was significantly reduced in both the deficiencies. A 2 to 4-fold increase in the concentration of skin homocysteine was observed in both the deficiencies. The results suggest that increase in skin homocysteine level may be responsible for the impaired skin collagen maturity in riboflavin or pyridoxine deficiency.

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Lakshmi, R., Lakshmi, A.V. & Bamji, M.S. Mechanism of impaired skin collagen maturity in riboflavin or pyridoxine deficiency. J Biosci 15, 289–295 (1990). https://doi.org/10.1007/BF02702670

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  • DOI: https://doi.org/10.1007/BF02702670

Keywords

  • Impaired skin collagen maturity
  • riboflavin deficiency
  • pyridoxine deficiency