Interaction of Cholera Toxin B Subunit with Intestinal Epithelial Cells
Journal Title: Journal of Endocrinology and Diabetes - Year 2017, Vol 4, Issue 3
Abstract
We have prepared 125I-labeled cholera toxin B subunit (125I-labeled CT-B, a specific activity of 98 Ci/mmol), and found that its binding to rat IEC-6 intestinal epithelial cells was high-affinity (Kd 3.7 nm). The binding of labeled protein was completely inhibited by unlabeled thymosin-α1 (TM-α1), interferon-α2 (IFN- α2), and the synthetic peptide LKEKK that corresponds to residues 16-20 in TM-α1 and 131-135 in IFN-α2 (Ki 1.5, 1.0 and 2.0 HM, respectively), but was not inhibited by the synthetic peptide KKEKL with inverted amino acid sequence (Ki > 10 mm). Thus, TM-α1, IFN-α2, and the peptide: LKEKK bind with high affinity and specificity to CT-B receptor on riec-6 cells. It was found that CT-B and the peptide: LKEKK at concentrations of 10 - 1000 nm increased in a dose-dependent manner the nitric oxide production and the soluble guanylate cyclase activity in the cells.
Authors and Affiliations
Elena V. Navolotskaya, Vladimir B. Sadovnikov, Valery M. Lipkin, Vladimir P. Zav’yalov
Keywords
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- EP ID EP333789
- DOI 10.15226/2374-6890/4/3/00178
- Views 117
- Downloads 0
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