Investigative Ophthalmology & Visual Science Cover Image for Volume 65, Issue 7
June 2024
Volume 65, Issue 7
Open Access
ARVO Annual Meeting Abstract  |   June 2024
Mechanism of αB-Crystallin Elastin-like Polypeptide conjugates protection against tunicamycin-induced ER stress in ARPE-19 cells
Author Affiliations & Notes
  • Sara Aly Attia
    Department of Pharmacology and Pharmaceutical Sciences, University of Southern California, Los Angeles, California, United States
  • Parameswaran G Sreekumar
    Doheny Eye Institute, Los Angeles, California, United States
  • Ram Kannan
    Stein Eye Institute Geffen School of Medicine, University of California Los Angeles, Los Angeles, California, United States
    Doheny Eye Institute, Los Angeles, California, United States
  • J. Andrew MacKay
    Department of Pharmacology and Pharmaceutical Sciences, University of Southern California, Los Angeles, California, United States
    Department of Ophthalmology, University of Southern California Keck School of Medicine, Los Angeles, California, United States
  • Footnotes
    Commercial Relationships   Sara Attia None; Parameswaran Sreekumar None; Ram Kannan None; J. Andrew MacKay None
  • Footnotes
    Support  None
Investigative Ophthalmology & Visual Science June 2024, Vol.65, 5098. doi:
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      Sara Aly Attia, Parameswaran G Sreekumar, Ram Kannan, J. Andrew MacKay; Mechanism of αB-Crystallin Elastin-like Polypeptide conjugates protection against tunicamycin-induced ER stress in ARPE-19 cells. Invest. Ophthalmol. Vis. Sci. 2024;65(7):5098.

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

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Abstract

Purpose : Oxidative and endoplasmic reticulum (ER) stress-induced retinal degeneration is implicated in ocular pathologies including AMD. Our recent work revealed that a mini-peptide derived from αB-crystallin recombinantly fused with elastin like polypeptides (ELPs) protects RPE cells from stress-induced cell death. In the present study, we compared two ELP fusions and evaluated their potential against tunicamycin, which can induce ER stress responses.

Methods : Previously, our team fused (mini cry) peptide with multiple elastin-like polypeptide (ELP) motifs. These ELPs consist of pentapeptide sequence, encoded as: (VPGVG)n, at which (n) specifies molecular size and the guest residue ‘X’ determines polymeric hydrophobicity. ELPs phase separate above a tunable transition temperature, Tt, which may facilitate their therapeutic applications. In earlier work, we engineered an amphiphilic mini-cry di-block polymer onto a micelle-forming ELP called SI, encoded as: (VPGSG)48(VPGIG)48, which has two Tt. In contrast, we now have a simpler monoblock ELP, V96 encoded as (VPGVG)96, which displays a single Tt near 37 oC. Physiochemical properties of both constructs (SI and V96) were compared by dynamic light scattering, spectrophotometry, and contrast microscopy. Their comparative cellular release, uptake, and efficacy were tested by Retinal Pigment Epithelial (ARPE-19) cells using confocal microscopy and western blotting. Hydrogen peroxide (H2O2) and tunicamycin challenges were used as oxidative and ER stressors.

Results : Results indicated successful ELP fusion with sensitive assembly at physiological temperatures. Unlike controls, only cry-ELP-treated groups showed upregulation of BIP/GPR78 and PERK signals in vitro (Figure 1). While both mini cry-ELP conjugates had an increased cellular association under oxidative stress, cry-V96 showed less lysosomal colocalization and faster cellular entry in both normal and stressed cultures.

Conclusions : Compared to cry-SI, V96 ELP fusion promoted lysosomal release necessary to provide protection against an oxidative stressor; furthermore, in the tunicamycin-induced ER stress model, RPE cells revealed upregulation of protective ER stress markers. These results suggest additional preclinical PK/PD evaluation of these peptide therapeutics is warranted.

This abstract was presented at the 2024 ARVO Annual Meeting, held in Seattle, WA, May 5-9, 2024.

 

Figure 1. cry-ELPs upregulate BIP/GRP78 and PERK signals under endoplasmic reticulum stress.

Figure 1. cry-ELPs upregulate BIP/GRP78 and PERK signals under endoplasmic reticulum stress.

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