α1-Thymosin, α2-interferon, and the LKEKK syntetic peptide inhibit the binding of the B subunit of the cholera toxin to intestinal epithelial cell membranes
| Autor: | V. I. Vladimirov, Yury A. Zolotarev, V. B. Sadovnikov, Elena V. Navolotskaya, Dmitry V. Zinchenko |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification 030102 biochemistry & molecular biology Protein subunit Organic Chemistry Cholera toxin Thymosin Peptide medicine.disease_cause Biochemistry Molecular biology 03 medical and health sciences 030104 developmental biology Membrane chemistry Interferon medicine Receptor Intracellular medicine.drug |
| Zdroj: | Russian Journal of Bioorganic Chemistry. 43:673-677 |
| ISSN: | 1608-330X 1068-1620 |
| Popis: | The 125I-labeled B-subunit of the cholera toxin ([125I]CT-B, specific activity of 98 Ci/mmol) was prepared. This subunit was shown to be bound to the membranes which were isolated from epithelial cells of a mucous tunic of the rat thin intestine with high affinity (Kd = 3.7 nM). The binding of the labeled protein was inhibited by the unlabeled α2-interferon (IFN-α2), α1-thymosin, (TM-α1), and the LKEKK synthetic peptide corresponding to the 16–20 sequence of TM-α1 and the 131–135 sequence of human IFN-α2 (Ki 1.0, 1.5, and 2.0 nM, respectively), whereas the KKEKL unlabeled synthetic peptide did not inhibit the binding (Ki > 100 μМ). The LKEKK peptide and CT-B were shown to dose-dependently increase an activity of the soluble guanylate cyclase (sGC) in the concentration range from 10 to 1000 nM. Thus, the binding of TM- α1, IFN-α2, and the LKEKK peptide to the CT-B receptor on a surface of the epithelial cells of the mucous tunic of the rat thin intestine resulted in an increase in the intracellular level of cGMP. |
| Databáze: | OpenAIRE |
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