Document Detail


iGLuc: a luciferase-based inflammasome and protease activity reporter.
MedLine Citation:
PMID:  23291722     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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.
Authors:
Eva Bartok; Franz Bauernfeind; Maria G Khaminets; Christopher Jakobs; Brian Monks; Katherine A Fitzgerald; Eicke Latz; Veit Hornung
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-06
Journal Detail:
Title:  Nature methods     Volume:  -     ISSN:  1548-7105     ISO Abbreviation:  Nat. Methods     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-7     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101215604     Medline TA:  Nat Methods     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
1] Institute for Clinical Chemistry and Clinical Pharmacology, Unit for Clinical Biochemistry, University Hospital, University of Bonn, Bonn, Germany. [2].
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