کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2050983 1074187 2007 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Tight junction modulation and biochemical characterisation of the zonula occludens toxin C-and N-termini
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
Tight junction modulation and biochemical characterisation of the zonula occludens toxin C-and N-termini
چکیده انگلیسی

The ZOT N-terminal domain was expressed and refolded, yielding a soluble protein with defined secondary structure. Although distantly related to protein I of filamentous phages, no evidence of ATPase activity was found. It is therefore unlikely that the ZOT N-terminal domain is involved in cholera toxin phage packaging in Vibrio cholerae. The ZOT C-terminal domain caused delocalisation of occludin and ZO-1 from Caco-2 cell–cell contacts, irrespective of disulfide bridge formation in its putative binding domain. However, the C-terminal domain did not cause actin reorganisation and this may explain the absence of a concomitant reduction in the transepithelial electrical resistance across cell monolayers.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 581, Issue 16, 26 June 2007, Pages 2974–2980
نویسندگان
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