Changes in collagen cross-linking and lysyl oxidase by estrogen

Biochim Biophys Acta. 1978 Jul 3;541(3):408-13. doi: 10.1016/0304-4165(78)90199-x.

Abstract

Dermal collagen solubility and lysyl oxidase activity of bones were measured in DDD mice of advancing age. Insoluble fractions of the dermal collagen increased more rapidly in females than in males after 5 weeks of age. Activity of the lysyl oxidase extracted from bones was higher in females than in males after 4 weeks of age. After sexual maturation, such sex differences were always observed in skin as well as in bone tissue. In other experimental animals, dermal collagen solubility was markedly decreased by estrogen treatment and lysyl oxidase was remarkably activated by estrogen in both skin and bone. Thus it is clear that estrogen stimulates the enzyme activity and accelerates the maturation of collagen and elastin in extracellular space.

Publication types

  • Comparative Study

MeSH terms

  • Aging
  • Amino Acid Oxidoreductases / metabolism*
  • Animals
  • Bone and Bones / drug effects
  • Castration
  • Collagen / metabolism*
  • Estradiol / pharmacology*
  • Female
  • Male
  • Mice
  • Progesterone / pharmacology
  • Protein-Lysine 6-Oxidase / metabolism*
  • Sex Factors
  • Skin / drug effects
  • Solubility
  • Testosterone / pharmacology

Substances

  • Testosterone
  • Progesterone
  • Estradiol
  • Collagen
  • Amino Acid Oxidoreductases
  • Protein-Lysine 6-Oxidase