Purification and Analysis of the Interactions of Caspase-1 and ASC for Assembly of the Inflammasome

Title
Purification and Analysis of the Interactions of Caspase-1 and ASC for Assembly of the Inflammasome
Author(s)
박현호베드리칸난
Keywords
SPECK-LIKE PROTEIN; NALP3 INFLAMMASOME; PROCASPASE-1 ACTIVATION; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; PYD DOMAIN; CARD; APOPTOSIS; RECRUITMENT; IMMUNITY
Issue Date
201503
Publisher
HUMANA PRESS INC
Citation
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, v.175, no.6, pp.2883 - 2894
Abstract
Inflammasomes are intracellular macromolecular complexes assembled to activate inflammatory caspases such as caspase-1 and caspase-5, which perform critical roles during innate immune response. The NALP3 inflammasome comprises three protein components, NALP3, ASC, and caspase-1. ASC, which contains both a pyrin domain (PYD) and a caspase recruitment domain (CARD), acts as a bridge to recruit NALP3 using the PYD/PYD interaction and to recruit caspase-1 via the CARD/CARD interaction. In this study, we successfully purified and characterized ASC CARD and caspase-1 CARD. The results showed that ASC CARD was unable to interact with caspase-1 CARD in vitro; therefore, we proposed an interaction mode between ASC CARD and caspase-1 CARD from a structural based modeling study.
URI
http://hdl.handle.net/YU.REPOSITORY/33069http://dx.doi.org/10.1007/s12010-014-1471-4
ISSN
0273-2289
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공과대학 > 화학공학부 > Articles
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