PuSH - Publikationsserver des Helmholtz Zentrums München

Eitelhuber, A.C. ; Vosyka, O.* ; Nagel, D. ; Bognar, M. ; Lenze, D.* ; Lammens, K.* ; Schlauderer, F.* ; Hlahla, D. ; Hopfner, K.P.* ; Lenz, G.* ; Hummel, M.* ; Verhelst, S.H.* ; Krappmann, D.

Activity-based probes for detection of active MALT1 paracaspase in immune cells and lymphomas.

Chem. Biol. 22, 129-138 (2014)
DOI PMC
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
MALT1 paracaspase is activated upon antigen receptor stimulation to promote lymphocyte activation. In addition, deregulated MALT1 protease activity drives survival of distinct lymphomas such as the activated B cell type of diffuse large B cell lymphoma (ABC-DLBCL). Here, we designed fluorophore or biotin-coupled activity based-probes (ABP) that covalently modify the active center of MALT1. MALT1-ABPs are exclusively labeling an active modified full length form of MALT1 upon T cell stimulation. Further, despite the CARMA1 requirement for initial MALT1 activation, the MALT1-ABPs show that protease activity is not confined to the high-molecular CARMA1-BCL10-MALT1 (CBM) complex. Using biotin-coupled ABPs, we developed a robust assay for sensitive and selective detection of active MALT1 in cell lines, primary lymphocytes, and DLBCL tumor biopsies. Taken together, MALT1-ABPs represent powerful chemical tools to measure cellular MALT1 activation, determine efficacy of small molecule inhibitors, and classify lymphomas based on MALT1 activity status.
Altmetric
Weitere Metriken?
[➜Einloggen]
Zusatzinfos bearbeiten [➜Einloggen]
Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter Nf-kappa-b; Protease Activity; Abc-dlbcl; T-cells; In-vivo; Activation; Cleavage; Phosphorylation; Identification; Inhibitors
ISSN (print) / ISBN 1074-5521
e-ISSN 1879-1301
Zeitschrift Chemistry and Biology
Quellenangaben Band: 22, Heft: 1, Seiten: 129-138 Artikelnummer: , Supplement: ,
Verlag Elsevier
Verlagsort Cambridge
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Research Unit Signaling and Translation (SAT)
Institute of Molecular Toxicology and Pharmacology (TOXI)