Characterization of glutathione S-transferase in cultured human keratinocytes

Kerry L. Blacker, Eric Olson, Donald A. Vessey, Thomas D. Boyer

Research output: Contribution to journalArticle

29 Scopus citations

Abstract

The glutathione S-transferase activity and isozymic composition of cultured human keratinocytes were characterized. Keratinocytes were grown in culture and harvested at different stages of differentiation. Glutathione S-transferase activity was found in the soluble cell fraction but not in the microsomal cell fraction. The glutathione S-transferase specific activity of the soluble cell fraction was found to increase as the keratinocytes differentiated in culture. All of the enzymatic activity was found to reside with a single isozymic form that was concluded to be the pi form of the enzyme based on substrate specificity, sensitivity to inhibitors, molecular weight, and reactivity towards antibodies raised to alpha, mu, and pi forms of the enzyme. It is concluded that all of the isozymic forms of glutathione S-transferase noted in whole skin, with the exception of pi, are of extra-keratinocyte origin.

Original languageEnglish (US)
Pages (from-to)442-446
Number of pages5
JournalJournal of Investigative Dermatology
Volume97
Issue number3
DOIs
StatePublished - Sep 1991

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Dermatology
  • Cell Biology

Fingerprint Dive into the research topics of 'Characterization of glutathione S-transferase in cultured human keratinocytes'. Together they form a unique fingerprint.

  • Cite this