Published in

Springer Nature [academic journals on nature.com], Mucosal Immunology, 5(6), p. 960-971, 2013

DOI: 10.1038/mi.2012.134

Links

Tools

Export citation

Search in Google Scholar

Inhibition of N-terminal ATPase on HSP90 attenuates colitis through enhanced Treg function

Journal article published in 2013 by Colm B. Collins, Carol M. Aherne, Alyson Yeckes, Kayla Pound, Holger K. Eltzschig, Paul Jedlicka, Edwin F. de Zoeten ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

Full text: Download

Green circle
Preprint: archiving allowed
Upload
Orange circle
Postprint: archiving restricted
Upload
Red circle
Published version: archiving forbidden
Policy details
Data provided by SHERPA/RoMEO

Abstract

Inflammatory Bowel Disease (IBD) is a chronic inflammatory condition thought to reflect a failure of the enteral immune system to adequately regulate itself. Inflammatory stress drives up-regulation of heat-shock proteins (HSP) including the pro-inflammatory chaperone, HSP90. This protein sequesters the transcription factor, heat-shock factor 1 (HSF1) in the cytoplasm preventing transcription of a number of anti-inflammatory proteins. We hypothesized that inhibition of HSP90 would exert an anti-inflammatory effect and thereby attenuate intestinal inflammation in murine models of IBD.