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Rhodamine 110-linked amino acids and peptides as substrates to measure caspase activity upon apoptosis induction in intact cells
Universitäts-Kinderklinik Ulm, Prittwitzstrasse 43, D-89075 Ulm, Germany, Universität Münster, Röntgen-Strasse 21, D-48149 Münster, Germany, and Orpegen Pharma, Czerny-Ring 22, D-69115 Heidelberg, Germany .
Department of Immunology and Cell Biology, University of Münster, Münster, Germany.ORCID iD: 0000-0001-9518-1411
Orpegen Pharma, Czerny-Ring 22, D-69115 Heidelberg, Germany .
Universitäts-Kinderklinik Ulm, Prittwitzstrasse 43, D-89075 Ulm, Germany, Universität Münster, Röntgen-Strasse 21, D-48149 Münster, Germany.
1999 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 38, no 42, 13906-13911 p.Article in journal (Refereed) Published
Abstract [en]

Caspases (cysteine aspartate-specific proteases) are a structurally related group of cysteine proteases that cleave peptide bonds following specific recognition sequences. They play a central role in activating apoptosis of vertebrate cells. To measure apoptosis induced by various stimuli and at an early apoptotic stage, caspases are an ideal target. This is especially the case when apoptotic cells have to be analyzed ex vivo before phagocytes remove them. A new and sensitive caspase assay is based on a substrate that contains only aspartate residues linked to rhodamine 110. With this and similar substrates, we are able to detect intracellular caspase activation by flow cytometry after apoptosis induction in intact hematopoetic cell lines.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 1999. Vol. 38, no 42, 13906-13911 p.
Keyword [en]
activation, downstream, enzyme, flow cytometric determination, granzyme-b, protease
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:liu:diva-87024DOI: 10.1021/bi9913395ISI: 000083288400016PubMedID: 10529236OAI: oai:DiVA.org:liu-87024DiVA: diva2:584256
Available from: 2013-01-08 Created: 2013-01-08 Last updated: 2017-12-06

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Los, Marek Jan

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