Specific racemization and isomerization of the aspartyl residue of alphaA-crystallin due to UV-B irradiation.

Abstract:

:We have reported that the aspartyl (Asp)-151 residue in alphaA-crystallin in human eye lens was inverted to the D-isomer and isomerized to beta-Asp residue with age. We report here that ultraviolet (UV)-B irradiation induces the racemization and isomerization of the Asp-151 residue of alphaA-crystallin from lenses of 6-week-old rats to form D-isomer and beta-Asp residue. Simultaneous racemization and isomerization of the specific Asp residue indicate that the reaction proceeds via formation of a succinimide intermediate. This modification was not observed in UV-A irradiated and normal lenses. UV-B irradiation induced the racemization of only the Asp-151 residue and did not affect the other Asp residues in alphaA-crystallin. On the other hand, the high molecular weight fraction of the lens protein increased upon UV-B irradiation. Modification of the Asp residue would affect the three-dimensional packing array of the lens protein.

journal_name

Exp Eye Res

authors

Fujii N,Momose Y,Ishibashi Y,Uemura T,Takita M,Takehana M

doi

10.1006/exer.1997.0315

subject

Has Abstract

pub_date

1997-07-01 00:00:00

pages

99-104

issue

1

eissn

0014-4835

issn

1096-0007

pii

S0014-4835(97)90315-8

journal_volume

65

pub_type

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