Amino Acids

, Volume 30, Issue 4, pp 369–389

Eye lens proteomics

  • W. Hoehenwarter
  • J. Klose
  • P. R. Jungblut
Review Article

DOI: 10.1007/s00726-005-0283-9

Cite this article as:
Hoehenwarter, W., Klose, J. & Jungblut, P. Amino Acids (2006) 30: 369. doi:10.1007/s00726-005-0283-9

Summary.

The eye lens is a fascinating organ as it is in essence living transparent matter. Lenticular transparency is achieved through the peculiarities of lens morphology, a semi-apoptotic process where cells elongate and loose their organelles and the precise molecular arrangement of the bulk of soluble lenticular proteins, the crystallins. The 16 crystallins ubiquitous in mammals and their modifications have been extensively characterized by 2-DE, liquid chromatography, mass spectrometry and other protein analysis techniques. The various solubility dependant fractions as well as subproteomes of lenticular morphological sections have also been explored in detail. Extensive post translational modification of the crystallins is encountered throughout the lens as a result of ageing and disease resulting in a vast number of protein species. Proteomics methodology is therefore ideal to further comprehensive understanding of this organ and the factors involved in cataractogenesis.

Keywords: Eye lens – Proteomics – Crystallins – 2-DE – Liquid chromatography – Mass spectrometry 

Copyright information

© Springer-Verlag 2006

Authors and Affiliations

  • W. Hoehenwarter
    • 1
  • J. Klose
    • 2
  • P. R. Jungblut
    • 1
  1. 1.Max Planck Institute for Infection Biology, Core Facility Protein AnalysisBerlinGermany
  2. 2.Institute for Human Genetics, CharitéBerlinGermany

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