Denatured human alpha-defensin attenuates the bactericidal activity and the stability against enzymatic digestion |
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Authors: | Tanabe Hiroki Ayabe Tokiyoshi Maemoto Atsuo Ishikawa Chisato Inaba Yuhei Sato Ryu Moriichi Kentaro Okamoto Kotaro Watari Jiro Kono Toru Ashida Toshifumi Kohgo Yutaka |
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Institution: | Division of Gastroenterology and Hematology/Oncology, Department of Medicine, Asahikawa Medical College, Japan. tant@asahikawa-med.ac.jp |
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Abstract: | alpha-Defensin is an antimicrobial peptide which plays an important role in innate immunity. Human defensin (HD)-5 is stored in the Paneth cells of the small intestine as a pro-form and is cleaved by trypsin, which is co-secreted from the Paneth cell granules. The mature HD-5 is protected from further digestion by the proteolysis enzyme. We generated both recombinant HD-5 and proHD-5, and the reduced form of each peptide in order to determine their physiological roles of the disulfide bonds. The reduced proHD-5 attenuated the bactericidal activity and the stability against the trypsin digestion. Human defensin was protected from the enzymatic degradation by disulfide bridges. We further purified the HD-5 with a disulfide variation in the small intestine of Crohn's disease patients. The HD-5 was sensitive to the trypsin treatment. These observations evidently predict that a defensin deficiency may be caused by a disulfide disorder in the disease. |
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Keywords: | Enteric defensin Paneth cells Inflammatory bowel disease Folding disorder |
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