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
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