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Denatured human α-defensin attenuates the bactericidal activity and the stability against enzymatic digestion

Tanabe, Hiroki ; Ayabe, Tokiyoshi ; Maemoto, Atsuo ; Ishikawa, Chisato ; Inaba, Yuhei ; Sato, Ryu ; Moriichi, Kentaro ; Okamoto, Kotaro ; Watari, Jiro ; Kono, Toru ; Ashida, Toshifumi ; Kohgo, Yutaka

Biochemical and biophysical research communications, 2007-06, Vol.358 (1), p.349-355 [Periódico revisado por pares]

United States: Elsevier Inc

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Denatured human α-defensin attenuates the bactericidal activity and the stability against enzymatic digestion
Autor: Tanabe, Hiroki ; Ayabe, Tokiyoshi ; Maemoto, Atsuo ; Ishikawa, Chisato ; Inaba, Yuhei ; Sato, Ryu ; Moriichi, Kentaro ; Okamoto, Kotaro ; Watari, Jiro ; Kono, Toru ; Ashida, Toshifumi ; Kohgo, Yutaka
Assuntos: alpha-Defensins - chemistry ; alpha-Defensins - pharmacology ; alpha-Defensins - physiology ; Amino Acid Sequence ; Anti-Bacterial Agents - chemistry ; Anti-Bacterial Agents - pharmacology ; Bacteria ; Crohn Disease - metabolism ; Disulfides - metabolism ; Enteric defensin ; Folding disorder ; Humans ; Ileum - metabolism ; Inflammatory bowel disease ; Molecular Sequence Data ; Paneth cells ; Peptides - chemistry ; Peptides - pharmacology ; Protein Denaturation ; Protein Precursors - chemistry ; Protein Precursors - pharmacology ; Protein Precursors - physiology ; Protein Processing, Post-Translational ; Salmonella typhimurium - drug effects ; Trypsin - metabolism
É parte de: Biochemical and biophysical research communications, 2007-06, Vol.358 (1), p.349-355
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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Descrição: α-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.
Editor: United States: Elsevier Inc
Idioma: Inglês

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Denatured human α-defensin attenuates the bactericidal activity and the stability against enzymatic digestion

Tanabe, Hiroki ; Ayabe, Tokiyoshi ; Maemoto, Atsuo ; Ishikawa, Chisato ; Inaba, Yuhei ; Sato, Ryu ; Moriichi, Kentaro ; Okamoto, Kotaro ; Watari, Jiro ; Kono, Toru ; Ashida, Toshifumi ; Kohgo, Yutaka

United States: Elsevier Inc

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