Interaction of Cholera Toxin B Subunit with Rat Intestinal Epithelial Cells

被引:0
|
作者
E. V. Navolotskaya
V. B. Sadovnikov
D. V. Zinchenko
V. I. Vladimirov
Y. A. Zolotarev
机构
[1] Russian Academy of Sciences,Branch of Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry
[2] Pushchino State Natural Science Institute,Institute of Molecular Genetics
[3] Russian Academy of Sciences,undefined
来源
Russian Journal of Bioorganic Chemistry | 2018年 / 44卷
关键词
peptides; receptors; cholera toxin B subunit; thymosin-α; interferon-α;
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学科分类号
摘要
We prepared 125I-labeled cholera toxin B subunit (125I-labeled CT-B, specific activity 98 Ci/mmol) and found that its binding to rat IEC-6 intestinal epithelial cells was high-affinity (Kd 1.9 nM). The binding of labeled protein was completely inhibited by unlabeled thymosin-α1 (TM-α1), interferon-α2 (IFN-α2), and synthetic peptide LKEKK, which corresponds to residues 16–20 in TM-α1 and 131–135 in IFN-α2 (Ki 1.2, 0.9, and 1.6 nM, respectively), but was not inhibited by synthetic peptide KKEKL with inverted amino acid sequence (Ki > 10 μM). Thus, TM-α1, IFN-α2, and the LKEKK peptide bind with high affinity and specificity to CT-B receptor on rIEC-6 cells. It was found that CT-B and the LKEKK peptide at concentrations of 10–1000 nM increased nitric oxide production and soluble guanylate cyclase activity in the cells in a dose-dependent manner.
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页码:403 / 407
页数:4
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