کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1937337 1050714 2007 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
An anti-endotoxin peptide that generates from the amino-terminal domain of complement regulatory protein C1 inhibitor
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
An anti-endotoxin peptide that generates from the amino-terminal domain of complement regulatory protein C1 inhibitor
چکیده انگلیسی

C1 inhibitor (C1INH), a complement regulatory protein, prevents endotoxin shock via a direct interaction of the amino-terminal domain with gram-negative bacterial lipopolysaccharide (LPS). Importantly, the cleaved, inactive C1INH still is an anti-endotoxin effector indicating the anti-endotoxin peptide that generates from the amino-terminal domain of C1INH. In this study, we first identified that a cleaved fragment within the major part of the amino-terminal domain in in vitro proteolytic analysis of C1INH had an ability to bind to LPS. We synthesized several peptides overlapping the C1INH cleaved fragment. Among these synthetic peptides, a 13-mer derivative peptide at position from 18 to 30, named N2(18–30), exhibited the most powerful anti-endotoxin activity in vitro, enlightening that it was most strong at binding to LPS, inhibiting the interaction of LPS with LPS-binding protein (LBP), blocking LPS binding to CD14+ cells, and suppressing production of tumor necrosis factor (TNF)-α by murine macrophages, RAW 264.7. In the murine endotoxin shock model, the peptide N2(18–30) protected mice from LPS-induced lethal septic shock by inhibiting macrophage activation. These data indicate that the peptide N2(18–30) derived from the amino-terminal region of C1INH is anti-endotoxin.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 359, Issue 2, 27 July 2007, Pages 285–291
نویسندگان
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