The influence of some post-translational modifications on the chaperone-like activity of alpha-crystallin.
We investigated the influence of phosphorylation, glycation, carbamylation and oxidative modification on the capacity of alpha-crystallin to protect beta-crystallins against heat denaturation. Simple modification of lysine residues by early glycation or carbamylation had no effect. However, late (cross-linking) glycation products and oxidative modifications decreased the chaperone-like activity of alpha-crystallin. Homopolymers of alpha A-crystallin had a higher protecting capacity compared with those of alpha B-crystallin. The in vivo phosphorylated forms of especially alpha A- but also alpha B-crystallin revealed a somewhat better protecting ability than the respective non-phosphorylated forms.
van Boekel
M A
MA
Department of Biochemistry, University of Nijmegen, The Netherlands.
Hoogakker
S E
SE
Harding
J J
JJ
de Jong
W W
WW
D000818:Animals; D002417:Cattle; D003459:Crystallins / Q000737:chemistry* / Q000378:metabolism; D005632:Fructose / Q000737:chemistry; D005954:Glucosephosphate Dehydrogenase / Q000737:chemistry; D006358:Hot Temperature; D007526:Isoelectric Point; D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism; D008970:Molecular Weight; D010084:Oxidation-Reduction; D010750:Phosphoproteins / Q000737:chemistry; D011489:Protein Denaturation; D013329:Structure-Activity Relationship
D003459:Crystallins; D018832:Molecular Chaperones; D010750:Phosphoproteins; D005632:Fructose; D005954:Glucosephosphate Dehydrogenase