Keratinocyte-specific transglutaminase of cultured human epidermal cells: Relation to cross-linked envelope formation and terminal differentiation

Scott M. Thacher, Robert H. Rice

Research output: Contribution to journalArticlepeer-review

344 Scopus citations

Abstract

The predominant form of the cross-linking enzyme, transglutaminase, in cultured normal human epidermal keratinocytes, is found in cell particulate material and can be solubilized by nonionic detergent. It elutes as a single peak upon either anion-exchange or gelfiltration chromatography. Monoclonal antibodies raised to the particulate enzyme cross-react with one of two transglutaminase, in the cell cytosol. The second cytosolic transglutaminase, which has distinct kinetic and physical properties from the first, does not cross-react and is not essential for formation of the keratinocyte cross-linked envelope in vitro. The antitransglutaminase antibodies stain the more differentiated layers of epidermis in a pattern similar to that given by anti-involucrin antiserum. These observations support the hypothesis that the transglutaminase so identified is involved in cross-linked envelope formation in vivo.

Original languageEnglish (US)
Pages (from-to)685-695
Number of pages11
JournalCell
Volume40
Issue number3
DOIs
StatePublished - 1985
Externally publishedYes

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Medicine(all)

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