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Related Experiment Videos

Protease in normal human epidermal keratinocytes

P Ray1, S T Ali

  • 1Biology Department, Walter Reed Army Institute of Research, Washington, D. C. 20307-5100, USA.

Drug and Chemical Toxicology
|August 26, 1998
PubMed
Summary
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Mustard chemicals stimulate a membrane-bound protease in skin cells. This protease, dependent on calcium and protein synthesis, may be a diagnostic marker for chemical exposure and a target for new drug development.

Area of Science:

  • Toxicology
  • Biochemistry
  • Dermatology

Background:

  • Chemical warfare agents like sulfur mustard cause severe skin blistering.
  • The precise cellular mechanisms underlying mustard-induced toxicity are not fully understood.
  • Investigating cellular responses to mustards can reveal new therapeutic targets.

Purpose of the Study:

  • To characterize the protease stimulated by sulfur mustards in normal human epidermal keratinocytes (NHEK).
  • To elucidate the biochemical properties and dependencies of the mustard-induced protease.
  • To explore the potential diagnostic and therapeutic applications of this stimulated protease.

Main Methods:

  • In vitro study using normal human epidermal keratinocytes (NHEK) exposed to CEES, nitrogen mustard (HN2), and sulfur mustard (HD).

Related Experiment Videos

  • Protease activity assay using chromozym (TRY) peptide substrate.
  • Inhibition studies using calcium chelators (EGTA, BAPTA AM), a serine protease inhibitor (DFP), and a protein synthesis inhibitor (cycloheximide).
  • Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) to identify stimulated proteins.

    • Main Results:

    • Mustard exposure stimulated protease activity in NHEK cells, with optimal conditions identified (e.g., 200 microM CEES, 100 microM HN2/HD, 16 hours).
    • The stimulated protease was membrane-bound and its activity was inhibited by calcium chelators, DFP, and cycloheximide.
    • SDS-PAGE revealed a 70-80 KDa protein band associated with the protease activity, sensitive to the same inhibitors.
    • Results suggest a trypsin/chymotrypsin-like serine protease dependent on Ca2+ and new protein synthesis.

    Conclusions:

    • Mustard toxicity involves the stimulation of a calcium-dependent, serine protease requiring new protein synthesis.
    • This mustard-stimulated protease may serve as a biomarker for exposure.
    • The protease represents a potential target for developing drugs to counteract vesicant effects.