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一种源自人促甲状腺激素受体序列的合成寡肽可与格雷夫斯病免疫球蛋白结合,并抑制促甲状腺素抗体活性,但与促甲状腺激素无相互作用。

A synthetic oligopeptide derived from human thyrotropin receptor sequence binds to Graves' immunoglobulin and inhibits thyroid stimulating antibody activity but lacks interactions with TSH.

作者信息

Mori T, Sugawa H, Piraphatdist T, Inoue D, Enomoto T, Imura H

机构信息

Department of Laboratory Medicine, Kyoto University School of Medicine, Japan.

出版信息

Biochem Biophys Res Commun. 1991 Jul 15;178(1):165-72. doi: 10.1016/0006-291x(91)91794-d.

Abstract

An 11-residue oligopeptide, P-195, was synthesized to match human thyrotropin (TSH) receptor structure from No. 333 to 343 of amino acid sequence. Preincubation of 5 Graves' IgGs with P-195 up to 10 micrograms resulted in dose-dependent reductions of thyroid stimulating antibody (TSAb) activity. [125I] labeled P-195 was found to bind Graves' IgG. The bound radioactivity correlated significantly with their TSAb activity (N = 25, r = 0.587, p less than 0.01). A peptide having a completely reverse sequence as P-195 did not show such biological activity. The peptide did not affect TSH and thyrotropin binding inhibitor immunoglobulin (TBII) on their receptor binding nor biological activities. P-195 was concluded to have a part of TSAb binding sites.

摘要

合成了一种由11个残基组成的寡肽P-195,其氨基酸序列与人类促甲状腺激素(TSH)受体结构的第333至343位相匹配。将5种格雷夫斯病(Graves')免疫球蛋白(IgG)与高达10微克的P-195预孵育,导致甲状腺刺激抗体(TSAb)活性呈剂量依赖性降低。发现[125I]标记的P-195能与格雷夫斯病IgG结合。结合的放射性与它们的TSAb活性显著相关(N = 25,r = 0.587,p < 0.01)。一种氨基酸序列与P-195完全相反的肽不具有这种生物学活性。该肽对TSH及其受体结合以及促甲状腺素结合抑制免疫球蛋白(TBII)的生物学活性均无影响。得出结论,P-195具有TSAb结合位点的一部分。

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