May 2007
Volume 48, Issue 13
ARVO Annual Meeting Abstract  |   May 2007
Proteomic Identification of Lens Capsule Proteins in Pseudoexfoliation
Author Affiliations & Notes
  • E. R. Anderson
    College of Medicine, University of Nebraska Medical Center, Omaha, Nebraska
    Ophthalmology, Bascom Palmer Eye Inst, University of Miami, Miami, Florida
  • T. Lee
    Ophthalmology, Bascom Palmer Eye Inst, University of Miami, Miami, Florida
  • S. K. Battacharya
    Ophthalmology, Bascom Palmer Eye Inst, University of Miami, Miami, Florida
  • R. K. Lee
    Ophthalmology, Bascom Palmer Eye Inst, University of Miami, Miami, Florida
  • Footnotes
    Commercial Relationships E.R. Anderson, None; T. Lee, None; S.K. Battacharya, None; R.K. Lee, None.
  • Footnotes
    Support Supported by NIH center grant P30 EY01480, EY016775 (to RKL), AHAF (to RKL), EY015266 (to SKB) and by an unrestricted grant to the University of Miami from Research to Prevent Blindness.
Investigative Ophthalmology & Visual Science May 2007, Vol.48, 5615. doi:
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    • Get Citation

      E. R. Anderson, T. Lee, S. K. Battacharya, R. K. Lee; Proteomic Identification of Lens Capsule Proteins in Pseudoexfoliation. Invest. Ophthalmol. Vis. Sci. 2007;48(13):5615.

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      © ARVO (1962-2015); The Authors (2016-present)

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Purpose:: Pseudoexfoliation (PXF) is a systemic disorder that manifests in ocular disease as glaucoma. The clinical hallmark of PXF is the deposition of fibrillar material in the anterior chamber of the eye, typically observed on the lens capsule. The molecular components of the PXF deposits are yet to be identified. Liquid chromatography tandem mass spectrometry analyses identified several proteins in lens capsules (LC) derived from patients with PXF. This study reports the histological distribution of these structural proteins in human lens capsules.

Methods:: Human LCs from normal and PXF patients were bloodlessly obtained during routine cataract extraction surgery and flash frozen, homogenized and used in western blot analysis or placed in fixative and sectioned for immunohistological analysis. Frozen LC sections (PXF=6, controls=6) were immunostained using CY-5 conjugated antibodies and nuclear DAPI staining for immunofluoresence as well as HRP-DAB for immunohistochemistry. Western blot analysis (PXF=10, controls=10) confirmed the expression of these proteins in human lens capsules.

Results:: The presence of structural proteins in the anterior lens capsule of patients with PXF was determined by immunostaining and by earlier proteomic analysis. The distribution of these proteins was localized to the lens capsule, the epithelium, or both. In particular, HNK-1 and RBC-associated proteins and epitopes were found to be differentially expressed and localized in PXF compared to normal LC. Western blot protein analysis correlated with these results and those from prior LCQ LC MS/MS mass spectrometry.

Conclusions:: This study highlights the molecular composition and histopathological distribution of differentially expressed proteins associated with the anterior LC in eyes with PXF. Confirming the presence of these proteins within the human lens capsule, and establishing the protein composition of LC tissue is important in understanding the pathophysiology of PXF and PXF-associated proteins. HNK-1 epitopes were present in PXF material deposits. Further exploration of these histological correlations with clinical disease may aid in the identification and understanding of pathological processes underlying PXF.

Keywords: proteomics • microscopy: light/fluorescence/immunohistochemistry • pathology: human 

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