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关于人类D-阿斯巴酸氧化酶的调节

Valentina Rabattoni¹, Zoraide Motta¹, Matteo Miceli¹

¹"The Protein Factory 2.0", Dipartimento di Biotecnologie e Scienze della Vita, Università degli studi dell'Insubria, Varese, Italy.

Protein science : a publication of the Protein Society

|October 8, 2023

概括

人类的酵素D-酸氧化酶 (hDASPO) 是通过化法调节的,并与pLG72相互作用,使其失活并降低其细胞水平. 这种相互作用可能会防止D-阿斯巴酸毒性.

科学领域:

神经科学是一个神经科学.
生物化学生物化学
酶学是一种酶学.

背景情况:

人类的酵素D-阿斯巴达酸氧化酶 (hDASPO) 调节大脑的D-阿斯巴达酸水平,影响NMDA,AMPA和mGlu5受体.
通过hDASPO降解D-阿斯巴酸对于预防与年龄相关的认知衰退至关重要,并且与精神分裂症和自闭症等精神疾病有关.

研究的目的:

研究调节hDASPO活性和稳定性的翻译后修饰和蛋白相互作用.
阐明pLG72.72规定的hDASPO规则的功能后果.

主要方法:

在体外化,硫化和化试验.
同免疫沉和表面等离子体共振用于研究蛋白质相互作用.
细胞表达研究评估hDASPO半衰期和复杂形成.

主要成果:

hDASPO经过体外化,对其活性有轻微影响;没有检测到硫化和化.
hDASPO与灵长类动物特异性蛋白质pLG72形成复合体,其解离常数在微分子范围内,导致酶失活.
pLG72和hDASPO的细胞共同表达导致细胞复合体,而pLG72减少了hDASPO的半衰期.

结论:

结合pLG72会使hDASPO失活,并降低其细胞稳定性,这表明存在一个调节机制.
这种相互作用可以作为一种保护措施,防止D-酸盐降解产生的过氧化产生的潜在细胞毒性.

关键词:

D-阿斯巴酸盐的使用方法亚味氧化酶的使用方法神经传递的神经传递在 pLG72 里面.后翻译修改后的修改蛋白质与蛋白质的相互作用

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