April 2011
Volume 52, Issue 14
Free
ARVO Annual Meeting Abstract  |   April 2011
EMILIN-1 (Elastin Microfibril Interface Located Protein) is Present in Lens Capsule-Associated Pseudoexfoliation Material
Author Affiliations & Notes
  • Mary L. Tapia
    Ophthalmology, Bascom Palmer Eye Institute, Miami, Florida
  • Miguel Risco
    Ophthalmology, Bascom Palmer Eye Institute, Miami, Florida
  • XiangMei Kong
    Ophthalmology, Bascom Palmer Eye Institute, Miami, Florida
  • Gustavo Munguba
    Ophthalmology, Bascom Palmer Eye Institute, Miami, Florida
  • James T. Banta
    Ophthalmology, Bascom Palmer Eye Institute, Miami, Florida
  • Sander Dubovy
    Ophthalmology, Bascom Palmer Eye Institute, Miami, Florida
  • Sanjoy Bhattacharya
    Ophthalmology, Bascom Palmer Eye Institute, Miami, Florida
  • Richard Lee
    Ophthalmology, Bascom Palmer Eye Institute, Miami, Florida
  • Footnotes
    Commercial Relationships  Mary L. Tapia, None; Miguel Risco, None; XiangMei Kong, None; Gustavo Munguba, None; James T. Banta, None; Sander Dubovy, None; Sanjoy Bhattacharya, None; Richard Lee, None
  • Footnotes
    Support  RKL is supported by NIH and the Bascom Palmer Eye Insitute is supported by NIH and an unrestricted grant from RPB.
Investigative Ophthalmology & Visual Science April 2011, Vol.52, 4594. doi:
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      Mary L. Tapia, Miguel Risco, XiangMei Kong, Gustavo Munguba, James T. Banta, Sander Dubovy, Sanjoy Bhattacharya, Richard Lee; EMILIN-1 (Elastin Microfibril Interface Located Protein) is Present in Lens Capsule-Associated Pseudoexfoliation Material. Invest. Ophthalmol. Vis. Sci. 2011;52(14):4594.

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

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Abstract

Purpose: : EMILIN-1 is an extracellular matrix protein that is known to interact with elastin, a known component of pseudoexfoliation material (PXFM). We demonstrate the presence of EMILIN-1 in lens capsule-bound pseudoexfoliation material (PXFM).

Methods: : Lens Capsules (LC) and aqueous humor (AH) were obtained from normal and pseudoexfoliation (PXF) patient eyes during cataract extraction surgery through avascular cornea and without contamination by hemorrhage. Proteomic analysis of aqueous humor and lens capsule was performed using electrospray tandem mass spectrometry. Immunofluorescence (IF) was conducted on lens capsules taken from normal and PXF patients. Western blotting for EMILIN-1 was performed on pooled solubilized LC (minimum 7 specimens/sample) and AH (minimum 2 specimens/sample) from normal and PXF eyes. GeneGo protein interaction software was used to map out interactions with EMILIN-1 with other proteins that we have idnetified as being associated with PXF material.

Results: : Proteomic analysis of LC and AH differentially identified the presence of EMILIN-1 in the AH of PXF eyes. Immunofluorescence localized EMILIN-1 to PXF material bound to lens capsule epithelium. Western blot analysis demonstrated a ~70 kDa EMILIN-1 protein band in both normal and PXF AH of comparable size. In silico, EMILIN-1 is closely associated with LOXL1, TGF-beta1, Elastin and other known PXF material components.

Conclusions: : EMILIN-1 was identified in PXFM found on lens capsule epithelium and in AH. This finding contributes to the growing body of knowledge of PXFM constituents. EMILIN-1 is an extracellular matrix protein that interacts with Elastin. We believe EMILIN-1 from the AH precipitates in association with elastin form PXF material. Further study is warranted to map the entire list of PXFM component proteins.

Keywords: anterior chamber • proteomics • microscopy: light/fluorescence/immunohistochemistry 
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