Caspases come together over LPS

Christina Smith; Xiaohui Wang; Hang Yin

doi:10.1016/j.it.2014.12.007

Caspases come together over LPS

Trends Immunol. 2015 Feb;36(2):59-61. doi: 10.1016/j.it.2014.12.007. Epub 2015 Jan 5.

Authors

Christina Smith¹, Xiaohui Wang², Hang Yin³

Affiliations

¹ Department of Chemistry & Biochemistry and the BioFrontiers Institute, University of Colorado Boulder, 596 UCB, Boulder, CO 80309-0596, USA.
² Department of Chemistry & Biochemistry and the BioFrontiers Institute, University of Colorado Boulder, 596 UCB, Boulder, CO 80309-0596, USA; Chemical Biology Laboratory, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin, 130022, China.
³ Department of Chemistry & Biochemistry and the BioFrontiers Institute, University of Colorado Boulder, 596 UCB, Boulder, CO 80309-0596, USA; Center of Basic Molecular Science and Department of Chemistry, Tsinghua University, Beijing, 100082, China. Electronic address: [email protected].

Abstract

Caspases are cellular executors, initiating cell death. In a recent study, Shi et al. report that caspases 4/5/11 are cytosolic LPS receptors, becoming activated through oligomerization upon interaction with LPS. These findings shed new light on the mechanisms underlying caspase-mediated pyroptosis, and have implications for the development of effective drugs to treat sepsis.

Publication types

Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Comment

MeSH terms

Animals
Caspases / metabolism*
Caspases, Initiator / metabolism*
Humans
Immunity, Innate*
Lipopolysaccharides / metabolism*

Substances

Lipopolysaccharides
Caspases
Caspases, Initiator

Abstract

Publication types

MeSH terms

Substances

Grants and funding