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    Immunopharmacology. 1996 Sep;34(2-3):113-23.

    Thymosin alpha 1 interacts with the VIP receptor-effector system in rat and mouse immunocompetent cells.

    Pozo D, Guerrero JM, Segura JJ, Calvo JR.

    Department of Medical Biochemistry and Molecular Biology, University of Seville School of Medicine, Spain.

    Thymic peptide thymosin alpha 1 (10(-11) to 10(-6) M) is shown to interact with the VIP receptor-effector system in rat and mouse peritoneal macrophages, and both rat peripheral blood lymphocytes and spleen lymphocytes. In all models, thymosin alpha 1 inhibits 125I-VIP binding with a potency that is in a range 1000-1700 times lower than that of the native VIP. Interaction of thymosin alpha 1 with VIP receptors is compared with that of some structurally VIP-related peptides such as helodermin, PHI, secretin, and glucagon. The order of potency in inhibiting 125I-VIP binding was VIP > helodermin > PHI > secretin > thymosin alpha 1. Thymosin alpha 1 (10(-10) to 10(-6) M) was weak in stimulating adenylyl cyclase activity. Its efficacy is in a range 900-1800 times lower than that of native VIP in all cell types studied. The analysis of the sequence of both complete and N-terminal portion of thymosin alpha 1 reveals close structural and physicochemical similarities with the members of the so-called VIP family of polypeptides. Taken together, experimental data support that thymosin alpha 1 must be included like the lowest partial agonist of the VIP family of polypeptides and it is a VIP receptor antagonist with weak intrinsic activity.

    PMID: 8886855 [PubMed - indexed for MEDLINE]

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