Interaction of Cholera Toxin B-subunit with Human T-lymphocytes.
Biochemistry (Mosc)
; 82(9): 1036-1041, 2017 Sep.
Article
em En
| MEDLINE
| ID: mdl-28988532
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 (Kd = 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 (Ki 0.8, 1.2, and 1.6 nM, respectively), but was not inhibited by the unlabeled synthetic peptide KKEKL with inverted sequence (Ki > 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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Timosina
/
Linfócitos T
/
Toxina da Cólera
/
Interferon-alfa
/
Guanilil Ciclase Solúvel
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article