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首页> 外文OA文献 >Identification of a second transmembrane protein tyrosine phosphatase, IA-2beta, as an autoantigen in insulin-dependent diabetes mellitus: precursor of the 37-kDa tryptic fragment.
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Identification of a second transmembrane protein tyrosine phosphatase, IA-2beta, as an autoantigen in insulin-dependent diabetes mellitus: precursor of the 37-kDa tryptic fragment.

机译：鉴定第二个跨膜蛋白酪氨酸磷酸酶IA-2beta作为胰岛素依赖性糖尿病中的自身抗原：37 kDa胰蛋白酶片段的前体。

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A novel cDNA, IA-2beta, was isolated from a mouse neonatal brain library. The predicted protein sequence revealed an extracellular domain, a transmembrane region, and an intracellular domain. The intracellular domain is 376 amino acids long and 74% identical to the intracellular domain of IA-2, a major autoantigen in insulin-dependent diabetes mellitus (IDDM). A partial sequence of the extracellular domain of IA-2beta indicates that it differs substantially (only 26% identical) from that of IA-2. Both molecules are expressed in islets and brain tissue. Forty-six percent (23 of 50) of the IDDM sera but none of the sera from normal controls (0 of 50) immunoprecipitated the intracellular domain of IA-2beta. Competitive inhibition experiments showed that IDDM sera have autoantibodies that recognize both common and distinct determinants on IA-2 and IA-2beta. Many IDDM sera are known to immunoprecipitate 37-kDa and 40-kDa tryptic fragments from islet cells, but the identity of the precursor protein(s) has remained elusive. The current study shows that treatment of recombinant IA-2beta and IA-2 with trypsin yields a 37-kDa fragment and a 40-kDa fragment, respectively, and that these fragments can be immunoprecipitated with diabetic sera. Absorption of diabetic sera with unlabeled recombinant IA-2 or IA-2beta, prior to incubation with radiolabeled 37-kDa and 40-kDa tryptic fragments derived from insulinoma or glucagonoma cells, blocks the immunoprecipitation of both of these radiolabeled tryptic fragments. We conclude that IA-2beta and IA-2 are the precursors of the 37-kDa and 40-kDa islet cell autoantigens, respectively, and that both IA-2 and IA-2beta are major autoantigens in IDDM.
机译：从小鼠新生脑文库中分离出一种新的IA-1beta cDNA。预测的蛋白质序列揭示了细胞外结构域，跨膜区和细胞内结构域。细胞内结构域长376个氨基酸，与IA-2（胰岛素依赖型糖尿病（IDDM）中的主要自身抗原）的细胞内结构域74％相同。 IA-2beta胞外域的部分序列表明，它与IA-2实质上不同（仅26％相同）。两种分子均在胰岛和脑组织中表达。 IDDM血清中有46％（50个中的23个），但正常对照（50个中的0个）的血清中没有一个免疫沉淀IA-2beta的细胞内结构域。竞争性抑制实验表明，IDDM血清具有识别IA-2和IA-2beta上共同决定簇和不同决定簇的自身抗体。已知许多IDDM血清会从胰岛细胞中免疫沉淀出37 kDa和40 kDa的胰蛋白酶片段，但前体蛋白的身份仍然难以捉摸。当前的研究表明，用胰蛋白酶处理重组IA-2beta和IA-2分别产生一个37 kDa的片段和一个40 kDa的片段，并且这些片段可以用糖尿病血清免疫沉淀。在与源自胰岛素瘤或胰高血糖素细胞的放射性标记的37-kDa和40-kDa胰蛋白酶消化片段孵育之前，用未标记的重组IA-2或IA-2beta吸收糖尿病血清，会阻止这两个放射性标记的胰蛋白酶消化片段的免疫沉淀。我们得出的结论是，IA-2beta和IA-2分别是37 kDa和40 kDa胰岛细胞自身抗原的前体，并且IA-2和IA-2beta都是IDDM中的主要自身抗原。

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