| First Author | Andley UP | Year | 2013 |
| Journal | Biochemistry | Volume | 52 |
| Issue | 17 | Pages | 2933-48 |
| PubMed ID | 23590631 | Mgi Jnum | J:201930 |
| Mgi Id | MGI:5516174 | Doi | 10.1021/bi400180d |
| Citation | Andley UP, et al. (2013) Comparative proteomic analysis identifies age-dependent increases in the abundance of specific proteins after deletion of the small heat shock proteins alphaA- and alphaB-crystallin. Biochemistry 52(17):2933-48 |
| abstractText | Mice with deletion of genes for small heat shock proteins alphaA- and alphaB-crystallin (alphaA/alphaB(-/-)) develop cataracts. We used proteomic analysis to identify lens proteins that change in abundance after deletion of these alpha-crystallin genes. Wild-type (WT) and alphaA/alphaB(-/-) knockout (DKO) mice were compared using two-dimensional difference gel electrophoresis and mass spectrometric analysis, and protein identifications were validated by Mascot proteomic software. The abundance of histones H2A, H4, and H2B fragment, and a low molecular weight beta1-catenin increased 2-3-fold in postnatal day 2 lenses of DKO lenses compared with WT lenses. Additional major increases were observed in abundance of betaB2-crystallin and vimentin in 30-day-old lenses of DKO animals compared with WT animals. Lenses of DKO mice were comprised of nine protein spots containing betaB2-crystallin at 10-40-fold higher abundance and three protein spots containing vimentin at >/=2-fold higher abundance than in WT lenses. Gel permeation chromatography identified a unique 328 kDa protein in DKO lenses, containing beta-crystallin, demonstrating aggregation of beta-crystallin in the absence of alpha-crystallins. Together, these changes provide biochemical evidence for possible functions of specific cell adhesion proteins, cytoskeletal proteins, and crystallins in lens opacities caused by the absence of the major chaperones, alphaA- and alphaB-crystallins. |
