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 journalArticle

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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.

Original languageEnglish
Pages (from-to)143-7
Number of pages5
JournalImmunology Letters
Volume128
Issue number2
DOIs
Publication statusPublished - Feb 16 2010

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Cathepsin A
Antigen-Presenting Cells
Cathepsins
Peptides
B-Lymphocyte Subsets
T-Lymphocyte Epitopes
Antigen Presentation
Serine Proteases
Myeloid Cells
Major Histocompatibility Complex
Proline
Dendritic Cells
Peptide Hydrolases
Amino Acids

Keywords

  • 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

Cite this

Cathepsin A is expressed in primary human antigen-presenting cells. / Reich, Michael; Spindler, Klaus-Dieter; Burret, Michael; Kalbacher, Hubert; Boehm, Bernhard O; Burster, Timo.

In: Immunology Letters, Vol. 128, No. 2, 16.02.2010, p. 143-7.

Research output: Contribution to journalArticle

Reich, M, Spindler, K-D, Burret, M, Kalbacher, H, Boehm, BO & Burster, T 2010, 'Cathepsin A is expressed in primary human antigen-presenting cells', Immunology Letters, vol. 128, no. 2, pp. 143-7. https://doi.org/10.1016/j.imlet.2009.11.010
Reich, Michael ; Spindler, Klaus-Dieter ; Burret, Michael ; Kalbacher, Hubert ; Boehm, Bernhard O ; Burster, Timo. / Cathepsin A is expressed in primary human antigen-presenting cells. In: Immunology Letters. 2010 ; Vol. 128, No. 2. pp. 143-7.
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AU - Reich, Michael

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AU - Burret, Michael

AU - Kalbacher, Hubert

AU - Boehm, Bernhard O

AU - Burster, Timo

N1 - Copyright (c) 2009 Elsevier B.V. All rights reserved.

PY - 2010/2/16

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N2 - 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.

AB - 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.

KW - Amino Acid Sequence

KW - Antigen-Presenting Cells

KW - Antigens

KW - B-Lymphocytes

KW - Cathepsin A

KW - Dendritic Cells

KW - Humans

KW - Immunohistochemistry

KW - Molecular Sequence Data

KW - Peptides

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

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JO - Immunology Letters

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