Phosphoproteome analysis of hereditary cataractous rat lens alpha-crystallin.
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.
Kamei
Akira
A
Section of Biochemistry, Faculty of Pharmacy, Meijo University, Nagayo, Japan.
Takamura
Shinsuke
S
Nagai
Makoto
M
Takeuchi
Noriko
N
D000818:Animals; D002386:Cataract / Q000235:genetics* / Q000378:metabolism*; D007908:Lens, Crystalline / Q000737:chemistry* / Q000378:metabolism; D010766:Phosphorylation; D020543:Proteome / Q000032:analysis* / Q000235:genetics / Q000378:metabolism; D051381:Rats; D038201:alpha-Crystallins / Q000032:analysis* / Q000235:genetics / Q000378:metabolism
D020543:Proteome; D038201:alpha-Crystallins