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

Cell. 1985 Mar;40(3):685-95. doi: 10.1016/0092-8674(85)90217-x.

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 gel-filtration chromatography. Monoclonal antibodies raised to the particulate enzyme cross-react with one of two transglutaminases 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 anti-transglutaminase 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.

Publication types

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

MeSH terms

  • Acyltransferases / immunology
  • Acyltransferases / isolation & purification
  • Acyltransferases / metabolism*
  • Animals
  • Antibodies, Monoclonal / immunology
  • Cell Differentiation
  • Cell Line
  • Cell Membrane / enzymology
  • Cell Membrane / ultrastructure
  • Chromatography
  • Cytosol / enzymology
  • Epidermis / enzymology*
  • Epidermis / ultrastructure
  • Epitopes / immunology
  • Female
  • Histocytochemistry
  • Humans
  • Hybridomas / immunology
  • Keratins / metabolism*
  • Kinetics
  • Mice
  • Mice, Inbred BALB C
  • Transglutaminases

Substances

  • Antibodies, Monoclonal
  • Epitopes
  • Keratins
  • Acyltransferases
  • Transglutaminases