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首页> 外文期刊>Journal of Neuroscience Methods >In Process Citation
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In Process Citation

机译：过程中引用

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摘要

Transglutaminases (TGs) posttranslationally modify proteins by transamidation of specific polypeptide bond glutamines. This reaction results in deamination, polyamine incorporation or the formation of isopeptide bonds. Transglutaminase activity in the brain is increased in several neurodegenerative diseases. Because insoluble inclusions occur in these neurodegenerative diseases, it has been hypothesized that transglutaminase contributes to the formation of the inclusions by catalyzing the formation of isopeptide bonds resulting in crosslinked, insoluble protein aggregates. To demonstrate a role for transglutaminase in the formation of these inclusions, the primary approach has been to show increased immunoreactivity with antibodies that recognize the isopeptide bonds. However, the specificity of these antibodies for isopeptide crosslinks within or between proteins has not been clearly established. In this report we demonstrate that the two most commonly used isopeptide antibodies do not specifically recognize the isopeptide bonds formed by transglutaminase when they are within or between proteins.
机译：转谷氨酰胺酶（TGs）通过特定多肽键谷氨酰胺的转酰胺基作用来翻译后修饰蛋白质。该反应导致脱氨基，多胺结合或异肽键的形成。在几种神经退行性疾病中，大脑中的转谷氨酰胺酶活性增加。由于在这些神经退行性疾病中会出现不溶性内含物，因此可以假设转谷氨酰胺酶通过催化异肽键的形成导致交联的不溶性蛋白质聚集体，从而促进了内含物的形成。为了证明转谷氨酰胺酶在这些内含物形成中的作用，主要方法是显示与识别异肽键的抗体的免疫反应性增加。但是，这些抗体对蛋白质内部或蛋白质之间的异肽交联的特异性尚未明确。在本报告中，我们证明了两种最常用的异肽抗体在蛋白质内部或蛋白质之间时，不能特异性识别由转谷氨酰胺酶形成的异肽键。

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