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

被引：2
|
作者：
Pozo, D
Guerrero, JM
Segura, JJ
Calvo, JR
机构：
[1] UNIV SEVILLE, SCH MED, DEPT MED BIOCHEM & MOL BIOL, SEVILLE 41009, SPAIN
[2] VIRGEN MACARENA HOSP, SEVILLE 41009, SPAIN
来源：
IMMUNOPHARMACOLOGY | 1996年 / 34卷 / 2-3期
关键词：
vasoactive intestinal peptide (VIP); thymic hormones; thymosin alpha 1; VIP receptors; immunocompetent cells; cyclic AMP production; porcine peptide histidine isoleucine (PHI); helodermin; secretin;
D O I：
10.1016/0162-3109(96)00131-2
中图分类号：
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号：
100102 ;
摘要：
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 al inhibits I-125-VIP binding with a potency that is in a range 1000-1700 times lower than that of the native VLP. 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 I-125-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 al reveals close structural and physicochemical similarities with the members of the so-called VIP family of polypeptides. Taken together, experimental data support that thymosin al 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.
引用
收藏
页码：113 / 123
页数：11
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