Cell-mediated reduction of human β-defensin 1: a major role for mucosal thioredoxin
Abstract
Human β-defensin 1 (hBD-1) is an antimicrobial peptide expressed by epithelia and hematopoietic cells. We demonstrated recently that hBD-1 shows activity against enteric commensals and Candida species only after its disulfide bonds have been reduced by thioredoxin (TRX) or a reducing environment. Here we show that besides TRX, glutaredoxin (GRX) is also able to reduce hBD-1, although with far less efficacy. Moreover, living intestinal and lymphoid cells can effectively catalyze reduction of extracellular hBD-1. By chemical inhibition of the TRX system or specific knockdown of TRX, we demonstrate that cell-mediated reduction is largely dependent on TRX. Quantitative PCR in intestinal tissues of healthy controls and inflammatory bowel disease patients revealed altered expression of some, although not all, redox enzymes, especially in ulcerative colitis. Reduced hBD-1 and TRX localize to extracellular colonic mucus, suggesting that secreted or membrane-bound TRX converts hBD-1 to a potent antimicrobial peptide in vivo.
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BibTeX
@article{jaeger2026cellmediated,
title = {{Cell-mediated reduction of human β-defensin 1: a major role for mucosal thioredoxin}},
author = {S Jaeger and B Schroeder and U Meyer-Hoffert and L Courth and S Fehr and M Gersemann and E Stange and J Wehkamp},
journal = {Mucosal Immunology},
year = {2026},
month = sep,
doi = {10.1038/mi.2013.17},
url = {https://hal.science/hal-05772276v1},
note = {CC BY-NC-ND},
}
RIS
TY - JOUR
TI - Cell-mediated reduction of human β-defensin 1: a major role for mucosal thioredoxin
AU - S Jaeger
AU - B Schroeder
AU - U Meyer-Hoffert
AU - L Courth
AU - S Fehr
AU - M Gersemann
AU - E Stange
AU - J Wehkamp
PY - 2026
DA - 2026/09/30
JO - Mucosal Immunology
DO - 10.1038/mi.2013.17
UR - https://hal.science/hal-05772276v1
AB - Human β-defensin 1 (hBD-1) is an antimicrobial peptide expressed by epithelia and hematopoietic cells. We demonstrated recently that hBD-1 shows activity against enteric commensals and Candida species only after its disulfide bonds have been reduced by thioredoxin (TRX) or a reducing environment. Here we show that besides TRX, glutaredoxin (GRX) is also able to reduce hBD-1, although with far less efficacy. Moreover, living intestinal and lymphoid cells can effectively catalyze reduction of extracellular hBD-1. By chemical inhibition of the TRX system or specific knockdown of TRX, we demonstrate that cell-mediated reduction is largely dependent on TRX. Quantitative PCR in intestinal tissues of healthy controls and inflammatory bowel disease patients revealed altered expression of some, although not all, redox enzymes, especially in ulcerative colitis. Reduced hBD-1 and TRX localize to extracellular colonic mucus, suggesting that secreted or membrane-bound TRX converts hBD-1 to a potent antimicrobial peptide in vivo.
SN - 1933-0219
SN - 1935-3456
ER -