Kamei Akira, Takamura Shinsuke, Nagai Makoto, Takeuchi Noriko
Section of Biochemistry, Faculty of Pharmacy, Meijo University, Nagayo, Japan.
Biol Pharm Bull. 2004 Dec;27(12):1923-31. doi: 10.1248/bpb.27.1923.
We reported previously that C-terminal truncated alpha-crystallins were found in lenses of hereditary cataractous rat ICR/f. In this study, we examined the phosphorylation of the crystalline lens proteins, alphaB-crystallin and alphaA-crystallin, in cataractous and normal rats of different ages and have found an increase in the phosphorylation of serine residues of truncated alpha-crystallin in cataractous lens. Phosphorylation and C-terminal truncation of alpha-crystallins could, both, reduce their chaperone-like activity and lead to cataract formation.
我们之前报道过,在遗传性白内障大鼠ICR/f的晶状体中发现了C端截短的α-晶状体蛋白。在本研究中,我们检测了不同年龄的白内障大鼠和正常大鼠晶状体蛋白αB-晶状体蛋白和αA-晶状体蛋白的磷酸化情况,发现白内障晶状体中截短的α-晶状体蛋白丝氨酸残基的磷酸化增加。α-晶状体蛋白的磷酸化和C端截短都可能降低其伴侣样活性并导致白内障形成。