April 2014
Volume 55, Issue 13
Free
ARVO Annual Meeting Abstract  |   April 2014
AGE-modifications in human lens capsule: Implications for posterior capsule opacification
Author Affiliations & Notes
  • Cibin T Raghavan
    Ophthalmology and Visual Sciences, Case Western Reserve University, Cleveland, OH
  • Mareen Smuda
    Institute of Chemistry, Martin-Luther-University Halle-Wittenberg, Halle/Saale, Germany
  • Marcus Glomb
    Institute of Chemistry, Martin-Luther-University Halle-Wittenberg, Halle/Saale, Germany
  • Annapurna Singh
    Ophthalmology and Visual Sciences, University Hospitals of Cleveland, Cleveland, OH
  • Pankaj Gupta
    Ophthalmology and Visual Sciences, University Hospitals of Cleveland, Cleveland, OH
  • Ram H Nagaraj
    Ophthalmology and Visual Sciences, Case Western Reserve University, Cleveland, OH
  • Footnotes
    Commercial Relationships Cibin Raghavan, None; Mareen Smuda, None; Marcus Glomb, None; Annapurna Singh, None; Pankaj Gupta, None; Ram Nagaraj, None
  • Footnotes
    Support None
Investigative Ophthalmology & Visual Science April 2014, Vol.55, 5722. doi:
  • Views
  • Share
  • Tools
    • Alerts
      ×
      This feature is available to authenticated users only.
      Sign In or Create an Account ×
    • Get Citation

      Cibin T Raghavan, Mareen Smuda, Marcus Glomb, Annapurna Singh, Pankaj Gupta, Ram H Nagaraj; AGE-modifications in human lens capsule: Implications for posterior capsule opacification. Invest. Ophthalmol. Vis. Sci. 2014;55(13):5722.

      Download citation file:


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

      ×
  • Supplements
Abstract

Purpose: Proteins in basement membrane are long-lived and accumulate chemical modifications during aging. The reaction of carbonyl compounds that results in the formation of advanced glycation end products (AGEs) is a major chemical modification in basement membrane proteins. Human lens capsule is a basement membrane secreted by lens epithelial cells. In this study we have investigated the effect of age and cataract on AGE modification in human lens capsules. The overall objective is to determine the effects of capsule AGEs on secondary cataract formation.

Methods: Lens capsules from normal lenses were isolated from donor lenses. Anterior capsule from cataractous lenses were collected from the capsulorhexis procedure during cataract surgery. AGE estimations were done using fluorescence HPLC and LC/MS. Human lens epithelial cells isolated from a 48-year donor lens was cultured on glycated or non-glycated Type IV collagen or basement membrane extract (BME). Glycation of the culture plates coated Type IV collagen or BME was carried out by incubating with one of the following two glycating mixtures: 1) low glycating mixture (LG): 2 mM ascorbate, 5 mM glucose and 100 μM methylglyoxal and 2) high glycating mixture (HG): 2 mM ascorbate, 25 mM glucose and 250 μM methylglyoxal for one week. Cell adhesion, proliferation and migration of lens epithelial cells on AGE-modified or control matrices were assessed by standard procedures.

Results: Fluorescent AGEs pentosidine and argpyrimidine were present in significantly higher amounts in the capsules of cataractous lenses when compared to those of age-matched normal lenses. The levels of these two AGEs were higher in the capsules of diabetic cataracts relative to those in senile cataracts. A number of other AGEs were identified by the LC/MS method, which are being quantified. Lens epithelial cell adhesion was significantly reduced in cells cultured on both LG and HG glycated collagen or BME relative to cells cultured on unmodified cell matrix. Similarly, cell proliferation and migration were significantly reduced in cells cultured on glycated matrices relative to those on non-glycated matrices.

Conclusions: Higher AGE content in the capsules of cataractous lenses could promote lens epithelial cell transformation into mesenchymal phenotype by negatively affecting cell proliferation and migration.

Keywords: 652 posterior capsular opacification (PCO) • 567 intraocular lens • 512 EMT (epithelial mesenchymal transition)  
×
×

This PDF is available to Subscribers Only

Sign in or purchase a subscription to access this content. ×

You must be signed into an individual account to use this feature.

×