The cornified envelope of terminally differentiated human epidermal keratinocytes consists of cross-linked protein

Robert H. Rice, Howard Green

Research output: Contribution to journalArticle

358 Scopus citations

Abstract

A small proportion of the protein of stratum corneum of human epidermal callus is insoluble even when boiled in solutions containing sodium dodecylsulfate and a reducing agent. This protein is present in the cornified envelope, a structure located beneath the plasma membrane. When cornified envelopes were dissolved by exhaustive proteolytic digestion and the products analyzed by chromatography, approximately 18% of the total lysine residues were found as the cross-linking dipeptide ε{lunate}-(γ-glutamyl) lysine. Labeled cornified envelope protein was synthesized by human epidermal keratinocytes allowed to differentiate terminally in culture. The extent of cross-linking, determined from the proportion of radioactive lysine in ε{lunate}-(γ-glutamyl) lysine after exhaustive proteolysis, was similar to that in stratum corneum. The properties of the cornified envelopes (insolubility in detergent and reducing agents, and solubility following proteolytic digestion) are readily explained by a structure consisting of a cross-linked protein lattice.

Original languageEnglish (US)
Pages (from-to)417-422
Number of pages6
JournalCell
Volume11
Issue number2
DOIs
StatePublished - 1977
Externally publishedYes

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Medicine(all)

Fingerprint Dive into the research topics of 'The cornified envelope of terminally differentiated human epidermal keratinocytes consists of cross-linked protein'. Together they form a unique fingerprint.

  • Cite this