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Thymosin alpha 1 modulates the expression of high affinity interleukin-2 receptors on normal human lymphocytes.

作者信息

Leichtling K D, Serrate S A, Sztein M B

机构信息

Department of Medicine, George Washington University School of Medicine, Washington, DC 20037.

出版信息

Int J Immunopharmacol. 1990;12(1):19-29. doi: 10.1016/0192-0561(90)90064-t.

DOI:10.1016/0192-0561(90)90064-t
PMID:2303316
Abstract

In this report we demonstrate that thymosin alpha 1 (T alpha 1), a synthetic peptide composed of 28 amino acid residues, and thymosin fraction 5 (TF5) enhance the number of high affinity interleukin 2 receptors (IL-2R) expressed by human peripheral blood lymphocytes in response to in vitro stimulation with phytohemagglutinin (PHA). Thymosins did not, however, alter the affinity of the IL-2R for its ligand. Dose-response studies using a wide range of concentrations indicated a bimodal distribution of responsiveness to T alpha 1. In most experiments the high and low concentration peaks of activity were observed at 10(-8) M and 10(-12) M, respectively, although peak responses were observed at different T alpha 1 concentrations in different donors. No effects were elicited by thymosins in the absence of mitogenic stimulation. Thymosin enhancement of PHA-induced high affinity IL-2R expression directly correlated with increased levels of Tac antigen expression, as determined by flow cytometry, and enhanced interleukin 2 (IL-2) production. Since the biological effects of IL-2 are associated with the occupancy of high affinity IL-2R, the findings presented in this report strongly suggest that thymosins play a significant role in the regulation of immune responses through the modulation of high affinity IL-2R expression.

摘要

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