Binding of cholera toxin B subunit to intestinal epithelial cells
| Autor: | V. B. Sadovnikov, Elena V. Navolotskaya, Vladimir P. Zav'yalov, Valery M. Lipkin |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Cholera Toxin Protein subunit Peptide Receptors Cell Surface G(M1) Ganglioside Toxicology medicine.disease_cause Ligands Nitric Oxide Binding Competitive Cell Line Iodine Radioisotopes 03 medical and health sciences medicine Animals Humans Intestinal Mucosa Receptor Peptide sequence ta116 chemistry.chemical_classification Binding Sites 030102 biochemistry & molecular biology Toxin Guanylate cyclase activity Cholera toxin Anti-Inflammatory Agents Non-Steroidal Interferon-alpha General Medicine medicine.disease Cholera Molecular biology Peptide Fragments Rats Thymosin Kinetics 030104 developmental biology chemistry Guanylate Cyclase Caco-2 Cells Oligopeptides |
| Zdroj: | Toxicology in vitro : an international journal published in association with BIBRA. 47 |
| ISSN: | 1879-3177 |
| Popis: | We have prepared 125I-labeled cholera toxin B subunit (125I-labeled CT-B, a specific activity of 98 Ci/mmol) and found that it binds to rat IEC-6 and human Caco-2 intestinal epithelial cells with high affinity (Kd 3.6 and 3.7 nM, respectively). 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, but was not inhibited by the synthetic peptide KKEKL with inverted amino acid sequence (Ki > 10 μM). Thus, TM-α1, IFN-α2, and the peptide: LKEKK bind with high affinity and specificity to the cholera toxin receptor on IEC-6 and Caco-2 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 IEC-6 and Caco-2 cells. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect