MOLECULAR INTERACTIONS OF CRYSTALLINS IN THE EYE

眼睛中晶状体蛋白的分子相互作用

• 批准号: 7953940
• 负责人: Jonathan Mark Petrash
• 金额: $ 0.58万
• 依托单位: WASHINGTON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-02-01 至 2010-01-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7953940
• 关键词: Applications Grants; Binding; Cataract; Cell membrane; Computer Retrieval of Information on Scientific Projects Database; Crystallins; Development; Eye; Funding; Grant; Human; Institution; Lipids; Mass Spectrum Analysis; Membrane; Membrane Proteins; Mouse Strains; Post-Translational Protein Processing; Property; Proteins; Research; Research Personnel; Resources; Role; Source; Specificity; Transgenic Mice; United States National Institutes of Health; alpha-Crystallins; biomedical resource; experience; insight; lens; mutant

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. This grant proposal is from a highly experienced investigator to examine whether a mutant form of alphaA-crystallin (R116 C), associated with autosomal dominant cataract in human, has altered property of elevated plasma membrane binding and therefore, causes cataract. Preliminary results shows a change in the property of the mutant alpha-crystallin compared wild type alpha, and according to the P.I., this may be a causative factor in the human autosomal dominant cataract. To investigate this causative factor in the autosomal dominant cataract, three specific aims are proposed. These will determine the specificities of lens membrane proteins and lipids during binding with alpha-crystallin, the effect of post-translational modifications of alpha-crystallin on its membrane-binding capability and finally the role of the mutant protein in cataract development by producing a transgenic mouse strain for lens expression of R116C mutant form of alphaA-crystallin. Together, the studies will provide insight regarding the role of alphaA R116C mutant in potential mechanism of the human autosomal dominant cataract.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 该赠款提案来自经验丰富的研究者，以检查与人类中与常染色体显性白内障相关的α-晶状体突变形式（R116 C）是否改变了质膜结合升高的性质，因此导致白内障。初步结果表明，突变体α-晶状体的特性发生了变化，比较了野生型α，根据P.I.，这可能是人类常染色体显性白内障的病原因素。为了研究常染色体显性白内障中的这种病因，提出了三个特定目标。这些将确定与α-晶状体蛋白结合过程中晶状体膜蛋白和脂质的特异性，这是α-晶状体的翻译后修饰对膜结合能力的作用，最后突变体蛋白在caparact发育中的作用，通过产生转移小鼠菌株对Rens semprant sepress for Rens semplyant ry116c-cranda cranda cy116c-cranda a and Allafe seprance。总之，这些研究将提供有关αAR116C突变体在人常染色体显性白内障潜在机制中的作用的见解。