Hook Darren W A, Harding John J
Nuffield Laboratory of Ophthalmology, Oxford, UK.
Dev Ophthalmol. 2002;35:150-60. doi: 10.1159/000060819.
The major lenticular protein alpha-crystallin has chaperone activity. With increasing age this chaperone function is compromised. Diabetes and glucocorticoid therapy are risk factors for cataract and are associated with raised sugar and glucocorticoid levels, respectively. These molecules react with proteins. Long-lived lenticular proteins are particularly susceptible to such attack. To investigate this possibility we carried out incubations of alpha-crystallin with fructose 6-phosphate and prednisolone-21-hemisuccinate and investigated the effect of modification on chaperone ability. Fructose 6-phosphate and prednisolone-21-hemisuccinate compromised chaperone activity as measured by the beta L-crystallin thermal aggregation assay. Tryptophan fluorescence provided evidence that the structure of alpha-crystallin had been modified by both compounds.
主要的晶状体蛋白α-晶状体蛋白具有伴侣活性。随着年龄的增长，这种伴侣功能会受到损害。糖尿病和糖皮质激素治疗是白内障的危险因素，分别与血糖升高和糖皮质激素水平升高有关。这些分子会与蛋白质发生反应。寿命较长的晶状体蛋白尤其容易受到这种攻击。为了研究这种可能性，我们将α-晶状体蛋白与6-磷酸果糖和泼尼松龙-21-半琥珀酸进行孵育，并研究修饰对伴侣能力的影响。通过βL-晶状体蛋白热聚集测定法测量，6-磷酸果糖和泼尼松龙-21-半琥珀酸损害了伴侣活性。色氨酸荧光提供了证据，表明这两种化合物都改变了α-晶状体蛋白的结构。
