Interaction of cholera toxin B-subunit with human T-lymphocytes |
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Authors: | E V Navolotskaya V B Sadovnikov D V Zinchenko Y A Zolotarev V M Lipkin V P Zav’yalov |
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Institution: | 1.Branch of Shemyakin?Ovchinnikov Institute of Bioorganic Chemistry,Russian Academy of Sciences,Pushchino, Moscow Region,Russia;2.Institute of Molecular Genetics,Russian Academy of Sciences,Moscow,Russia;3.Shemyakin?Ovchinnikov Institute of Bioorganic Chemistry,Russian Academy of Sciences,Moscow,Russia;4.University of Turku,Turku,Finland |
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Abstract: | In this work, 125I-labeled cholera toxin B-subunit (CT-B) (specific activity 98 Ci/mmol) was prepared, and its high-affinity binding to human blood T-lymphocytes (K d = 3.3 nM) was determined. The binding of the 125I-labeled CT-B was inhibited by unlabeled interferon-α2 (IFN-α2), thymosin-α1 (TM-α1), and by the synthetic peptide LKEKK, which corresponds to sequences 16-20 of human TM-α1 and 131-135 of IFN-α2 (K i 0.8, 1.2, and 1.6 nM, respectively), but was not inhibited by the unlabeled synthetic peptide KKEKL with inverted sequence (K i > 1 μM). In the concentration range of 10-1000 nM, both CT-B and peptide LKEKK dose-dependently increased the activity of soluble guanylate cyclase (sGC) but did not affect the activity of membrane-bound guanylate cyclase. The KKEKL peptide tested in parallel did not affect sGC activity. Thus, the CT-B and peptide LKEKK binding to a common receptor on the surface of T-lymphocytes leads to an increase in sGC activity. |
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