Collagen cross-linking in sun-exposed and unexposed sites of aged human skin

J Invest Dermatol. 1991 Nov;97(5):938-41. doi: 10.1111/1523-1747.ep12491727.

Abstract

A recently described nonreducible, acid-heat stable compound, histidinohydroxylysinonorleucine (HHL), is a collagen cross-link isolated from mature skin tissue. Its abundance is related to chronologic aging of skin. The present communication describes the quantity of HHL from aged human skin of the same individuals in sun-exposed (wrist) and unexposed (buttock) sites. Punch biopsies were obtained from these sites from nine people of age 60 or older. HHL contents (moles/mole of collagen) at these sites were for wrist 0.13 +/- 0.07 and for buttock 0.69 +/- 0.17 (mean +/- SD, p less than 0.001). In addition, it was found that acute irradiation of the cross-linked peptides with UVA (up to 250 J/cm2) and UVB (up to 1 J/cm2) had no effect on HHL structure. The same treatment significantly degraded another nonreducible, stable collagen cross-link, pyridinoline. The results suggest that chronic sunlight exposure may be associated with an impediment to normal maturation of human dermal collagen resulting in tenuous amount of HHL. Thus, the process of photoaging in dermal collagen is different from that of chronologic aging in human skin.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adult
  • Aged
  • Amino Acids / pharmacology
  • Collagen / chemistry
  • Collagen / pharmacology*
  • Cross-Linking Reagents*
  • Humans
  • Hydroxyproline / pharmacology
  • Oligopeptides / analysis
  • Oligopeptides / pharmacology
  • Oligopeptides / radiation effects
  • Skin / chemistry
  • Skin / radiation effects*
  • Ultraviolet Rays*

Substances

  • Amino Acids
  • Cross-Linking Reagents
  • Oligopeptides
  • pyridinoline
  • Collagen
  • Hydroxyproline