Cathepsin A is expressed in primary human antigen-presenting cells

Abstract 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...

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Bibliographic Details
Published in:Immunology letters 2010-02, Vol.128 (2), p.143-147
Main Authors: Reich, Michael, Spindler, Klaus-Dieter, Burret, Michael, Kalbacher, Hubert, Boehm, Bernhard O, Burster, Timo
Format: Article
Language:English
Subjects:
Allergy and Immunology
Amino Acid Sequence
Antigen presentation/processing
Antigen-Presenting Cells - immunology
Antigen-Presenting Cells - metabolism
Antigens - chemistry
Antigens - immunology
B-Lymphocytes - immunology
B-Lymphocytes - metabolism
Cathepsin A
Cathepsin A - metabolism
Dendritic Cells - immunology
Dendritic Cells - metabolism
Humans
Immunohistochemistry
Molecular Sequence Data
Peptides - chemistry
Peptides - immunology
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Summary:Abstract 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.
ISSN:0165-2478
1879-0542
DOI:10.1016/j.imlet.2009.11.010