ESCRS - PO422 - Gsto1, Gsto2, Gpx1 And Sod2 Polymorphisms Modify Susceptibility Of Developing Primary Open Angle Glaucoma

Gsto1, Gsto2, Gpx1 And Sod2 Polymorphisms Modify Susceptibility Of Developing Primary Open Angle Glaucoma

Published 2022 - 40th Congress of the ESCRS

Reference: PO422 | Type: ESCRS 2022 - Posters | DOI: 10.82333/2rmx-kq84

Authors: Miroslav Radivoje Stamenkovic* 1 , Aleksandra Popovic 1 , Biljana Vukadinovic 1 , Zoran Zikic 1 , Milos Plavsic 1 , Tatjana Djukic 2 , Sanja Radojevic 3 , Svetlana Sukalo 1 , Ana Savic-Radojevic 1

1Eye Clinic University Medical Center Zvezdara,Eye Clinic University Medical Center Zvezdara,Belgrade,Serbia, 2Institute of Biochemistry,Medical Faculty University of Belgrade,Belgrade,Serbia, 3Eye Clinic University Medical Center Zvezdara,Belgrade,Serbia

Purpose

A contributing role of disrupted redox homeostasis in pathophysiology and progression of primary open angle glaucoma (POAG) has been suggested. We aimed to assess the association between polymorphisms in genes encoding enzymes involved in redox homeostasis, mitochondrial superoxide dismutase (SOD2), glutathione peroxidase (GPX1) and glutathione transferases (GSTs) with susceptibility to POAG.

Setting

Eye Clinic University Medical Center Zvezdara, Belgrade, 

 

 

Methods

Single nucleotide polymorphisms of GSTO1 (rs4925), GSTO2 (rs156697), GSTP1(rs1695), as well as GPX1 (rs1050450) and SOD2 (rs4880) were determined by quantitative polymerase chain reaction (qPCR) in 102 POAG patients and 302 respective controls.

Results

We found 8-fold increased risk for POAG development in carriers of both GSTO2*GG and GSTO1*AA variant genotypes (OR=8.21, p=0.002). Moreover, individuals who carried GPX1*TT and SOD2*CC genotypes had also an increased risk of POAG development (OR=6.66, p=0.005).

Conclusions

The present study supports the hypothesis that in combination, GSTO1/GSTO2, modulate the risk of primary open angle glaucoma.

 

 Keywords: primary open angle glaucoma, glutathione transferases, glutathione peroxidase, superoxide dismutase