Yonsei Med J.  2004 Feb;45(1):73-80. 10.3349/ymj.2004.45.1.73.

Accumulation and Aberrant Modifications of alpha-Crystallins in Anterior Polar Cataracts

Affiliations
  • 1Laboratory of Ophthalmol. and Visual Sci., Korea Eye Tissue and Gene Bank. ckjoo@cmc.cuk.ac.kr
  • 2Department of Ophthalmol., College of Med., The Catholic Univ. of Korea, Seoul, Korea.
  • 3Graduate School of East-West Med. Sci., Kyung Hee Univ., Seoul, Korea.
  • 4Department of Life Science, The University of Seoul, Korea.
  • 5Department of Ophthalmol., Inje Univ., Ilsan Paik Hospital, Korea.
  • 6Department of Ophthalmol., Yonsei Univ. College of Med., Seoul, Korea.

Abstract

Crystallins are the major proteins found in the lens, and the localization of specific crystallins is well known. Overexpression and accumulation of alphaB-crystallin has been observed in response to stress conditions or in certain diseases, such as brain tumors and neurodegenerative diseases. The purpose of this study was to examine whether alpha-crystallins are modified during pathological myofibroblastic changes in lens epithelial cells. Lens epithelial cells attached to the anterior capsules of patients with nuclear or anterior polar cataracts were analyzed quantitatively for alpha-crystallin proteins and mRNAs using Western blot and RT-PCR analysis., respectively. The degree of modification of alpha-crystallins was determined by 2-dimensional gel electrophoresis followed by Western blotting. Higher molecular weight protein bands that were immunoreactive to anti-alphaA- and anti-alphaB-crystallin antibodies around 45 kDa accumulated more in the anterior polar cataract samples than in those with the nuclear type of cataracts. Also monomeric alphaB-crystallins accumulated more in lens epithelial cells of patients with anterior polar cataracts. By comparison, no significant changes were found in the levels of the mRNAs encoding alphaA- and alphaB-crystallins in the different types of cataracts. Both alphaA- and alphaB-crystallin proteins seemed to undergo more extensive modification in anterior polar cataracts. Conclusion. In addition to fibrotic changes, which accompany increased levels of extracellular matrix molecules, accumulation and abnormal modification of alpha-crystallins might be implicated in the pathogenic mechanism of this type of cataract.

Keyword

Alpha-crystallins; cataract; lens epithelium; modification; two-dimensional gel electrophoresis

MeSH Terms

Adult
Cataract/*genetics/metabolism
Epithelial Cells/metabolism
Female
Human
Lens, Crystalline/metabolism
Male
Middle Aged
RNA, Messenger/analysis
Reverse Transcriptase Polymerase Chain Reaction
Support, Non-U.S. Gov't
alpha-Crystallin A Chain/*genetics/metabolism
alpha-Crystallin B Chain/*genetics/metabolism
Full Text Links
  • YMJ
Actions
Cited
CITED
export Copy
Close
Share
  • Twitter
  • Facebook
Similar articles
Copyright © 2024 by Korean Association of Medical Journal Editors. All rights reserved.     E-mail: koreamed@kamje.or.kr