Reduced Human α-defensin 6 in Noninflamed Jejunal Tissue of Patients with Crohn's Disease.

Inflammatory Bowel Diseases
Ryohei HayashiMamoru Watanabe

Abstract

Mucosal barrier dysfunction is considered a critical component of Crohn's disease (CD) pathogenesis after the identification of susceptibility genes. However, the precise mechanism underlying mucosal barrier dysfunction has not yet been elucidated. We therefore aimed to elucidate the molecular mechanism underlying the expression of human α-defensin 6 (HD6) in patients with CD. HD6 expression was induced by the transfection of an atonal homolog 1 (Atoh1) transgene and was assessed by reverse transcription polymerase chain reaction. The HD6 promoter region targeted by Atoh1 and β-catenin was determined by reporter analysis and chromatin immunoprecipitation assay. HD5/HD6/Atoh1/β-catenin expression in noninflamed jejunal samples collected by balloon endoscopy from 15 patients with CD and 9 non-inflammatory bowel disease patients were assessed by immunofluorescence. Both promoter activity and gene expression of HD6 was significantly upregulated by the Atoh1 transgene in human colonic cancer cell line. We identified a TCF4 binding site and an E-box site, critical for the regulation of HD6 transcriptional activity by directly binding of Atoh1 in the 200-bp HD6 promoter region. The treatment with β-catenin inhibitor also decreases HD6...Continue Reading

References

Jul 10, 2002·Gastroenterology·Nagamu InoueToshifumi Hibi
Jan 30, 2004·Cancer Cell·Maina LepourceletRamesh A Shivdasani
Dec 24, 2004·Antimicrobial Agents and Chemotherapy·Bryan EricksenRobert I Lehrer
Mar 22, 2005·Nature Cell Biology·Johan H van EsHans Clevers
Dec 7, 2005·Proceedings of the National Academy of Sciences of the United States of America·Jan WehkampCharles L Bevins
Aug 22, 2007·The Journal of Immunology : Official Journal of the American Association of Immunologists·Jan WehkampEduard F Stange
Nov 22, 2008·American Journal of Physiology. Gastrointestinal and Liver Physiology·Ryuichi OkamotoMamoru Watanabe
Mar 3, 2010·Annual Review of Immunology·Arthur KaserRichard S Blumberg
Jun 17, 2011·Nature·Kevin J Maloy, Fiona Powrie
Nov 20, 2012·Langenbeck's Archives of Surgery·Simon JägerJan Wehkamp
Jan 22, 2013·Biochemical and Biophysical Research Communications·Yoshihito KanoMamoru Watanabe
Feb 13, 2013·Annual Review of Physiology·Hans C Clevers, Charles L Bevins
Oct 30, 2014·Mucosal Immunology·B O SchroederJ Wehkamp
Dec 3, 2014·Biochemical and Biophysical Research Communications·Nobukatsu HoritaMamoru Watanabe

❮ Previous
Next ❯

Citations

Sep 6, 2017·Clinical and Experimental Immunology·S KusakaA Andoh
May 1, 2020·Frontiers in Immunology·Jan Wehkamp, Eduard F Stange
Sep 5, 2020·Clinical Otolaryngology : Official Journal of ENT-UK ; Official Journal of Netherlands Society for Oto-Rhino-Laryngology & Cervico-Facial Surgery·Yu-Hsuan LinChia-Hung Kao
Feb 18, 2021·Journal of Crohn's & Colitis·Sho WatanabeKiichiro Tsuchiya

❮ Previous
Next ❯

Related Concepts

Related Feeds

Adherens Junctions

An adherens junction is defined as a cell junction whose cytoplasmic face is linked to the actin cytoskeleton. They can appear as bands encircling the cell (zonula adherens) or as spots of attachment to the extracellular matrix (adhesion plaques). Adherens junctions uniquely disassemble in uterine epithelial cells to allow the blastocyst to penetrate between epithelial cells. Discover the latest research on adherens junctions here.

Cadherins and Catenins

Cadherins (named for "calcium-dependent adhesion") are a type of cell adhesion molecule (CAM) that is important in the formation of adherens junctions to bind cells with each other. Catenins are a family of proteins found in complexes with cadherin cell adhesion molecules of animal cells: alpha-catenin can bind to β-catenin and can also bind actin. β-catenin binds the cytoplasmic domain of some cadherins. Discover the latest research on cadherins and catenins here.