Differential analysis of D-beta-Asp-containing proteins found in normal and infrared irradiated rabbit lens.
Although proteins are generally composed of l-alpha-amino acids, d-beta-aspartic acid (Asp)-containing proteins have been reported in various elderly tissues. Our previous study detected several d-beta-Asp-containing proteins in a rabbit lens derived from epithelial cell line by Western blot analysis of a 2D-gel using a polyclonal antibody that is highly specific for d-beta-Asp-containing proteins. The identity of each spot was subsequently determined by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and the Ms-Fit online database searching algorithm. In this study, we discovered novel d-beta-Asp-containing proteins from rabbit lens. The results indicate that beta-crystallin A3, beta-crystallin A4, beta-crystallin B1, beta-crystallin B2, beta-crystallin B3, gamma-crystallin C, gamma-crystallin D, and lambda-crystallin in rabbit lens contain d-beta-Asp residues. Furthermore, the occurrence of d-beta-Asp residues increases with infrared ray (IR) irradiation. Additionally, some d-beta-Asp-containing proteins only appear after IR irradiation. One such protein is the alpha-enolase, which shows homology to tau-crystallin.
Takata
Takumi
T
Research Reactor Institute, Kyoto University, Kumatori-cho, Sennan, Osaka 590-0494, Japan.
Shimo-Oka
Tadashi
T
Kojima
Masami
M
Miki
Kunio
K
Fujii
Noriko
N
D000818:Animals; D015180:Electrophoresis, Gel, Two-Dimensional; D007259:Infrared Rays; D026581:Isoaspartic Acid / Q000032:analysis*; D007908:Lens, Crystalline / Q000737:chemistry* / Q000528:radiation effects*; D011817:Rabbits; D012995:Solubility; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D038204:beta-Crystallins / Q000737:chemistry*
D026581:Isoaspartic Acid; D038204:beta-Crystallins