Age-related changes in the composition of the cornified envelope in human skin

Exp Dermatol. 2013 May;22(5):329-35. doi: 10.1111/exd.12135.

Abstract

The main function of the epidermis is to protect us against a multitude of hostile attacks from the environment. Its main cell type, the keratinocytes have a sophisticated system of different proteins and lipids available to form the cornified envelope, which is responsible for the barrier function of the skin. During ageing, dramatic changes are taking place. Some proteins of the SPRR-, S100- and LCE3-family are massively up-regulated, whereas others like loricrin, filaggrin and the LCE1&2 protein families are significantly down-regulated. The latter ones are known to be under control of calcium and/or 'calcium response elements'. We were able to show that the calcium peak specific for the stratum granulosum, which is the site where loricrin and the LCE1&2 families are synthesized, is reduced during ageing. The resulting cornified envelope in old skin has an extensively changed composition on the molecular level compared to young skin. This knowledge is of critical importance to understand chronic wound formation and ulcers in old age.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adolescent
  • Adult
  • Aged
  • Calcium / metabolism
  • Calgranulin B / genetics
  • Child
  • Child, Preschool
  • Cornified Envelope Proline-Rich Proteins / genetics*
  • Epidermal Cells
  • Epidermis / physiology*
  • Female
  • Filaggrin Proteins
  • Foreskin / cytology
  • Foreskin / physiology
  • Humans
  • Infant
  • Infant, Newborn
  • Intermediate Filament Proteins / genetics
  • Keratinocytes / physiology*
  • Male
  • Membrane Proteins / genetics
  • Middle Aged
  • Proteins / genetics
  • Skin Aging / genetics*
  • Skin Ulcer / genetics
  • Transcriptome*
  • Young Adult

Substances

  • CRCT1 protein, human
  • Calgranulin B
  • Cornified Envelope Proline-Rich Proteins
  • FLG protein, human
  • Filaggrin Proteins
  • Intermediate Filament Proteins
  • LELP1 protein, human
  • Membrane Proteins
  • Proteins
  • loricrin
  • Calcium