| iGLuc: a luciferase-based inflammasome and protease activity reporter. | |
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MedLine Citation:
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PMID: 23291722 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Measurement of protease activity in living cells or organisms remains a challenging task. We here present a transgene-encoded biosensor that reports the proteolytic activity of caspase-1 in the course of inflammasome activation and that of other proteases in a highly sensitive and specific manner. This protease reporter is based on the biological activity of a pro-interleukin (IL)-1β-Gaussia luciferase (iGLuc) fusion construct, in which pro-IL-1β-dependent formation of protein aggregates renders GLuc enzyme inactive. Cleavage leads to monomerization of this biosensor protein, resulting in a strong gain in luciferase activity. Exchange of the canonical caspase-1 cleavage site in this reporter construct allows the generation of protease biosensors with additional specificities. The high sensitivity, signal-to-background ratio and specificity of the iGLuc system renders it a useful tool to study proteolytic events in mouse and human cells at high throughput and to monitor protease activity in mice in vivo. |
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Authors:
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Eva Bartok; Franz Bauernfeind; Maria G Khaminets; Christopher Jakobs; Brian Monks; Katherine A Fitzgerald; Eicke Latz; Veit Hornung |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2013-1-06 |
Journal Detail:
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Title: Nature methods Volume: - ISSN: 1548-7105 ISO Abbreviation: Nat. Methods Publication Date: 2013 Jan |
Date Detail:
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Created Date: 2013-1-7 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101215604 Medline TA: Nat Methods Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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1] Institute for Clinical Chemistry and Clinical Pharmacology, Unit for Clinical Biochemistry, University Hospital, University of Bonn, Bonn, Germany. [2]. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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