June 2015
Volume 56, Issue 7
Free
ARVO Annual Meeting Abstract  |   June 2015
Understanding the molecular mechanism of RPE pathology in Smith-Lemli-Opitz Syndrome
Author Affiliations & Notes
  • Sriganesh Ramachandra Rao
    Ophthalmology and Biochemistry, SUNY at Buffalo and SUNY Eye Institute, Buffalo, NY
    Research Service, VA Western NY Healthcare System, Buffalo, NY
  • Bruce A Pfeffer
    Ophthalmology and Biochemistry, SUNY at Buffalo and SUNY Eye Institute, Buffalo, NY
    Research Service, VA Western NY Healthcare System, Buffalo, NY
  • Meerim Choi
    Ophthalmology and Biochemistry, SUNY at Buffalo and SUNY Eye Institute, Buffalo, NY
    Research Service, VA Western NY Healthcare System, Buffalo, NY
  • Kevin Francis
    PDEGEN, NIH/NICHD, Bethesda, MD
  • Forbes D Porter
    PDEGEN, NIH/NICHD, Bethesda, MD
  • Steven J Fliesler
    Ophthalmology and Biochemistry, SUNY at Buffalo and SUNY Eye Institute, Buffalo, NY
    Research Service, VA Western NY Healthcare System, Buffalo, NY
  • Footnotes
    Commercial Relationships Sriganesh Ramachandra Rao, None; Bruce Pfeffer, None; Meerim Choi, None; Kevin Francis, None; Forbes Porter, None; Steven Fliesler, None
  • Footnotes
    Support None
Investigative Ophthalmology & Visual Science June 2015, Vol.56, 2389. doi:
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      Sriganesh Ramachandra Rao, Bruce A Pfeffer, Meerim Choi, Kevin Francis, Forbes D Porter, Steven J Fliesler; Understanding the molecular mechanism of RPE pathology in Smith-Lemli-Opitz Syndrome. Invest. Ophthalmol. Vis. Sci. 2015;56(7 ):2389.

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

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Abstract

Purpose: We previously showed that the retinal pigmented epithelium (RPE) in the AY9944 rat model of Smith-Lemli-Opitz syndrome (SLOS) exhibits marked accumulation of phagosomes, lipofuscin and bis-retinoids compared to age-matched controls. Lysosomal pH and function are sensitive to altered cholesterol homeostasis and oxysterol levels. We tested the hypothesis that SLOS patient-derived RPE cells in vitro would exhibit dysfunctional lysosomal molecular signatures, and also would have decreased autophagic flux and an elevated ubiquitinated protein load due to hindered autophagic clearance.

Methods: Inducible pluripotent stem cells (iPSCs) derived from SLOS patient skin fibroblasts were reprogrammed to RPE cells (SLOS RPE) (Neural Stem Cell Institute, Rensselaer, NY); control human embryonic stem cell-derived RPE (nhRPE) cells were used as controls. Sterols (cholesterol (Chol), 7-dehydrocholesterol (7DHC)) were quantified by RP-HPLC (N=3 ea.). Protein levels of lysosomal markers (mature Cathepsin-D, LAMP2), upstream (Beclin1) and downstream (p62 and LC3-I/II) markers of autophagy, and ubiquitinated protein levels were assessed by Western blot/densitometry (N=3 ea.), normalized to GAPDH levels. Mean/S.D. values were statistically compared using Student’s t-test (significance criterion, p ≤ 0.05).

Results: SLOS RPE and nhRPE cells were validated by morphological criteria (hexagonal, melanized, polarized epithelial monolayers) and RPE protein markers (cRAlBP, cytokeratin-8, ZO-1). SLOS RPE cells exhibited 20-fold higher 7DHC/Chol mole ratios [0.697 ± 0.064] than nhRPE [0.035 ± 0.009] (p<0.01). Protein levels of lysosome and autophagic markers in SLOS RPE (expressed as % change compared to normal RPE) were as follows (p < 0.02): LAMP2, -42%; mature Cathepsin-D, -98%; Beclin-1, 388%; p62, >+1500%; LC3II, -71%; ubiquitinated proteins, +440%.

Conclusions: These findings are indicative of marked lysosomal dysfunction and compromised autophagic flux in SLOS RPE compared to control cells (nhRPE), consistent with the RPE pathology observed in the AY9944 rat model of SLOS. These changes may be due to the increased 7DHC levels (or oxysterols derived therefrom) in SLOS RPE cells, which may perturb lysosomal membrane structure and function.

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