Journal
IMMUNOLOGY LETTERS
Volume 128, Issue 2, Pages 143-147Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.imlet.2009.11.010
Keywords
Antigen presentation/processing; Cathepsin A
Categories
Funding
- Deutsche Forschungsgemeinschaft [SFB 518-A4, GRK 1041-2]
- Department of Internal Medicine
Ask authors/readers for more resources
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 11 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. (C) 2009 Elsevier BLV. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available