IOVS
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Weinreb, O.
Right arrow Articles by Bloemendal, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Weinreb, O.
Right arrow Articles by Bloemendal, H.
(Investigative Ophthalmology and Visual Science. 2000;41:191-198.)
© 2000 by The Association for Research in Vision and Ophthalmology, Inc.

Effect of UV-A Light on the Chaperone-like Properties of Young and Old Lens {alpha}-Crystallin

Orly Weinreb1, Martinus Adrianus Maria van Boekel1, Ahuva Dovrat2 and Hans Bloemendal1

1 From the Department of Biochemistry, University of Nijmegen, the Netherlands; and the 2 B. Rappaport Faculty of Medicine, Technion–Israel Institute of Technology, Haifa, Israel.

PURPOSE. To study the damaging effect of UV-A irradiation on the chaperone-like properties of {alpha}-crystallin and the subsequent recovery process of young and old bovine lenses.

METHODS. Young and old bovine lenses were kept in organ culture. After 24 hours of incubation they were irradiated with UV-A at 365 nm, and optical quality measurements were performed during the experiments (192 hours). {alpha}-Crystallin and {alpha}A1-, {alpha}A2-, {alpha}B1-, and {alpha}B2-crystallin subunits were analyzed, separated by gel filtration and cation exchange chromatography, respectively, after different culture times. Protein patterns were obtained after two-dimensional (2-D) gel electrophoresis. Chaperone-like activity was determined on the basis of insulin B-chain and ßL-crystallin aggregation assays. Aggregation of {alpha}-crystallin was analyzed, tryptophan fluorescence measurements were performed, and {alpha}-crystallin mRNA levels were determined.

RESULTS. The water-soluble {alpha}-crystallin obtained from old lenses compared with young lenses after UV irradiation had decreased chaperone activity, a higher molecular weight, and increased loss of tryptophan fluorescence. Moreover, {alpha}-crystallin mRNA virtually disappeared, whereas extra spots on the 2-D protein pattern appeared, possibly because of deamidation.

CONCLUSIONS. {alpha}-Crystallin obtained from old lenses is more affected by irradiation than {alpha}-crystallin derived from young lenses. Moreover, it appeared that {alpha}B-crystallin from UV-treated old lenses compared with control lenses was less susceptible to UV-A than {alpha}A-crystallin. It may well be that {alpha}B-crystallin protects {alpha}A-crystallin in vivo.




This article has been cited by other articles:


Home page
 IOVSHome page
G. Thiagarajan, J. Lakshmanan, M. Chalasani, and D. Balasubramanian
Peroxynitrite Reaction with Eye Lens Proteins: {alpha}-Crystallin Retains Its Activity Despite Modification
Invest. Ophthalmol. Vis. Sci., July 1, 2004; 45(7): 2115 - 2121.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2000 by the Association for Research in Vision and Ophthalmology