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The Serine Protease CD26/DPP4 in Non-Transformed and Malignant T Cells
SIMPLE SUMMARY: The transmembrane serine protease CD26/Dipeptidylpeptidase 4 modulates T-cell activation, proliferation, and effector function. Due to their remarkable tumoricidal properties CD26-positive T cells are considered promising candidates for T cell-based immunotherapies while in cutaneous...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8657226/ https://www.ncbi.nlm.nih.gov/pubmed/34885056 http://dx.doi.org/10.3390/cancers13235947 |
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author | Chitadze, Guranda Wehkamp, Ulrike Janssen, Ottmar Brüggemann, Monika Lettau, Marcus |
author_facet | Chitadze, Guranda Wehkamp, Ulrike Janssen, Ottmar Brüggemann, Monika Lettau, Marcus |
author_sort | Chitadze, Guranda |
collection | PubMed |
description | SIMPLE SUMMARY: The transmembrane serine protease CD26/Dipeptidylpeptidase 4 modulates T-cell activation, proliferation, and effector function. Due to their remarkable tumoricidal properties CD26-positive T cells are considered promising candidates for T cell-based immunotherapies while in cutaneous T cell lymphoma CD26/DPP4 expression patterns are established markers for diagnosis and possibly prognosis. With a focus on T cells, we review current knowledge on the regulation of CD26/DPP4 expression and release, its implication in T-cell effector function and the suitability CD26/DPP4 as a diagnostic and/or prognostic factor in T-cell malignancies. ABSTRACT: CD26/Dipeptidylpeptidase 4 is a transmembrane serine protease that cleaves off N-terminal dipeptides. CD26/DPP4 is expressed on several immune cell types including T and NK cells, dendritic cells, and activated B cells. A catalytically active soluble form of CD26/DPP4 can be released from the plasma membrane. Given its wide array of substrates and interaction partners CD26/DPP4 has been implicated in numerous biological processes and effects can be dependent or independent of its enzymatic activity and are exerted by the transmembrane protein and/or the soluble form. CD26/DPP4 has been implicated in the modulation of T-cell activation and proliferation and CD26/DPP4-positive T cells are characterized by remarkable anti-tumor properties rendering them interesting candidates for T cell-based immunotherapies. Moreover, especially in cutaneous T-cell lymphoma CD26/DPP4 expression patterns emerged as an established marker for diagnosis and treatment monitoring. Surprisingly, besides a profound knowledge on substrates, interaction partners, and associated signal transduction pathways, the precise role of CD26/DPP4 for T cell-based immune responses is only partially understood. |
format | Online Article Text |
id | pubmed-8657226 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-86572262021-12-10 The Serine Protease CD26/DPP4 in Non-Transformed and Malignant T Cells Chitadze, Guranda Wehkamp, Ulrike Janssen, Ottmar Brüggemann, Monika Lettau, Marcus Cancers (Basel) Review SIMPLE SUMMARY: The transmembrane serine protease CD26/Dipeptidylpeptidase 4 modulates T-cell activation, proliferation, and effector function. Due to their remarkable tumoricidal properties CD26-positive T cells are considered promising candidates for T cell-based immunotherapies while in cutaneous T cell lymphoma CD26/DPP4 expression patterns are established markers for diagnosis and possibly prognosis. With a focus on T cells, we review current knowledge on the regulation of CD26/DPP4 expression and release, its implication in T-cell effector function and the suitability CD26/DPP4 as a diagnostic and/or prognostic factor in T-cell malignancies. ABSTRACT: CD26/Dipeptidylpeptidase 4 is a transmembrane serine protease that cleaves off N-terminal dipeptides. CD26/DPP4 is expressed on several immune cell types including T and NK cells, dendritic cells, and activated B cells. A catalytically active soluble form of CD26/DPP4 can be released from the plasma membrane. Given its wide array of substrates and interaction partners CD26/DPP4 has been implicated in numerous biological processes and effects can be dependent or independent of its enzymatic activity and are exerted by the transmembrane protein and/or the soluble form. CD26/DPP4 has been implicated in the modulation of T-cell activation and proliferation and CD26/DPP4-positive T cells are characterized by remarkable anti-tumor properties rendering them interesting candidates for T cell-based immunotherapies. Moreover, especially in cutaneous T-cell lymphoma CD26/DPP4 expression patterns emerged as an established marker for diagnosis and treatment monitoring. Surprisingly, besides a profound knowledge on substrates, interaction partners, and associated signal transduction pathways, the precise role of CD26/DPP4 for T cell-based immune responses is only partially understood. MDPI 2021-11-26 /pmc/articles/PMC8657226/ /pubmed/34885056 http://dx.doi.org/10.3390/cancers13235947 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Chitadze, Guranda Wehkamp, Ulrike Janssen, Ottmar Brüggemann, Monika Lettau, Marcus The Serine Protease CD26/DPP4 in Non-Transformed and Malignant T Cells |
title | The Serine Protease CD26/DPP4 in Non-Transformed and Malignant T Cells |
title_full | The Serine Protease CD26/DPP4 in Non-Transformed and Malignant T Cells |
title_fullStr | The Serine Protease CD26/DPP4 in Non-Transformed and Malignant T Cells |
title_full_unstemmed | The Serine Protease CD26/DPP4 in Non-Transformed and Malignant T Cells |
title_short | The Serine Protease CD26/DPP4 in Non-Transformed and Malignant T Cells |
title_sort | serine protease cd26/dpp4 in non-transformed and malignant t cells |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8657226/ https://www.ncbi.nlm.nih.gov/pubmed/34885056 http://dx.doi.org/10.3390/cancers13235947 |
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