title: The effect of modification of alpha-crystallin by prednisolone-21-hemisuccinate and fructose 6-phosphate on chaperone activity.
abstract: 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.
authors.affiliation: Nuffield Laboratory of Ophthalmology, Oxford, UK.
authors.forename: Darren W A
authors.initials: DW
authors.lastname: Hook
authors.forename: John J
authors.initials: JJ
authors.lastname: Harding
mesh_terms: D000818:Animals; D002417:Cattle; D005636:Fructosephosphates / Q000494:pharmacology*; D007908:Lens, Crystalline / Q000737:chemistry; D018832:Molecular Chaperones / Q000378:metabolism*; D011239:Prednisolone / Q000031:analogs & derivatives* / Q000494:pharmacology*; D013050:Spectrometry, Fluorescence; D038201:alpha-Crystallins / Q000187:drug effects* / Q000302:isolation & purification / Q000378:metabolism
chemical_list: D005636:Fructosephosphates; D018832:Molecular Chaperones; D038201:alpha-Crystallins; C027618:fructose-6-phosphate; D011239:Prednisolone; C021322:prednisolone hemisuccinate