title: Does post-translational modification influence chaperone-like activity of alpha-crystallin? I. Study on phosphorylation.
abstract: It is difficult to isolate derivatives of alpha-crystallin with only one type of post-translational modification, because this protein is subjected to several different types of modification. In the present study using bovine lens proteins, we isolated mono-phosphorylated alphaB-crystallin with no other post-translational modifications. Using this material, we demonstrated that mono-phosphorylation reduced the activity of alphaB-crystallin by approximately 30%. Our results confirmed that investigation of the correlation between chaperone-like activities of alpha-crystallin and post-translational modification is important to understand the mechanism of cataract formation.
authors.affiliation: Department of Biochemistry, Faculty of Pharmaceutical Sciences, Meijo University, Aichi, Japan. kamei@meijo-u.ac.jp
authors.forename: A
authors.initials: A
authors.lastname: Kamei
authors.forename: T
authors.initials: T
authors.lastname: Hamaguchi
authors.forename: N
authors.initials: N
authors.lastname: Matsuura
authors.forename: K
authors.initials: K
authors.lastname: Masuda
mesh_terms: D000818:Animals; D002417:Cattle; D018833:Chaperonins / Q000378:metabolism*; D003459:Crystallins / Q000378:metabolism*; D013058:Mass Spectrometry / Q000379:methods; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational
chemical_list: D003459:Crystallins; D018833:Chaperonins