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The expression and function of cathepsin E in dendritic cells

Benjamin M Chain1, Paul Free, Patrick Medd

  • 1Department of Immunology and Molecular Pathology, University College London, London, United Kingdom. b.chain@ucl.ac.uk

Journal of Immunology (Baltimore, Md. : 1950)
|February 9, 2005
PubMed

Insights

Cathepsin E plays a crucial role in antigen processing within dendritic cells for the class II MHC pathway. This study demonstrates its nonredundant function in presenting antigens to T cells.

Area of Science:

  • Immunology
  • Cell Biology
  • Biochemistry

Background:

  • Cathepsin E is an aspartic proteinase involved in antigen (Ag) processing.
  • Dendritic cells are key antigen-presenting cells (APCs) in the immune system.
  • The precise role of Cathepsin E in dendritic cell Ag processing remained unclear.

Purpose of the Study:

  • To investigate the presence and function of Cathepsin E in human myeloid dendritic cells.
  • To elucidate the role of Cathepsin E in the class II Major Histocompatibility Complex (MHC) antigen processing pathway.

Main Methods:

  • Documented Cathepsin E expression (mRNA and protein) in human myeloid dendritic cells.
  • Utilized a novel pepstatin-based inhibitor to block Cathepsin D/E activity.
  • Assessed antigen presentation by dendritic cells using wild-type and cathepsin D-deficient mice.

Main Results:

  • Cathepsin E protein was localized to perinuclear and peripheral compartments in dendritic cells.
  • The synthesized inhibitor effectively blocked Cathepsin D/E activity in vitro and in cells.
  • Dendritic cells treated with the inhibitor failed to present intact ovalbumin (OVA) but could present an OVA-derived peptide.

Conclusions:

  • Cathepsin E is present and functional in dendritic cells.
  • Cathepsin E has a significant, nonredundant role in processing antigens for presentation via the class II MHC pathway.

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