Open AccessReduced glutathione level and gsh-dependent enzyme activities in corticonuclear blocks of lenses in patients with senile cataract
Author(s) -
Bojana Kisić,
Dijana Mirić,
Lepša Žorić,
Ilić Aleksandra,
Ilija Dragojević
Publication year - 2012
Publication title -
srpski arhiv za celokupno lekarstvo
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.135
H-Index - 17
eISSN - 2406-0895
pISSN - 0370-8179
DOI - 10.2298/sarh1210563k
Subject(s) - glutathione , cumene hydroperoxide , thiol , antioxidant , glutathione peroxidase , medicine , lens (geology) , enzyme , senile cataract , biochemistry , chemistry , ophthalmology , biology , paleontology , catalysis
Reduced compound glutathione (GSH) in the lens has the function to protect the thiol group of lens proteins, and as a substrate of glutathione peroxidase (GPx) and glutathione S-transferase (GST). Protein containing thiol groups is significant for the normal function of lens epithelium, i.e. enzymes Na-K-ATP-ase, thus influencing cell permeability. The relationship GSH/GSSG (oxidized glutathione) is normally high in the lens and other ocular tissue owing to the glutathione-redox cycle, which is localized in the lens epithelium and cortex surface.