Cathepsin A is expressed in primary human antigen-presenting cells

Michael Reich, Klaus-Dieter Spindler, Michael Burret, Hubert Kalbacher, Bernhard O Boehm, Timo Burster

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)


Cathepsins are expressed in antigen-presenting cells (APC). These cathepsins are known to regulate antigen processing and degradation of the invariant chain (Ii) into the class II-associated Ii peptide (CLIP), which occupies the peptide-binding groove of the major histocompatibility complex (MHC) class II molecule. Previous studies have identified the serine carboxypeptidase cathepsin A (CatA) in various tissues and cells; however, it is not clear whether CatA is also expressed in primary human APC. We demonstrate the expression of CatA in B lymphoblastoid cells (BLC), primary human B cells, both subsets of myeloid dendritic cells (mDC1 and mDC2), as well as in plasmacytoid DC. PMSF or lactacystin-mediated inhibition of serine proteases in BLC-derived lysosomal proteases resulted in the inhibition of amino acid release from the C-terminal end of two model peptides. This inhibition did not occur by using a proline rich peptide. Our data suggest that CatA is involved in the C-terminal fine-tuning of antigenic T cell epitopes in human APC.

Original languageEnglish
Pages (from-to)143-7
Number of pages5
JournalImmunology Letters
Issue number2
Publication statusPublished - Feb 16 2010


  • Amino Acid Sequence
  • Antigen-Presenting Cells
  • Antigens
  • B-Lymphocytes
  • Cathepsin A
  • Dendritic Cells
  • Humans
  • Immunohistochemistry
  • Molecular Sequence Data
  • Peptides
  • Journal Article
  • Research Support, Non-U.S. Gov't

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