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Modulation of erythrocyte photohemolysis rate by glutathione reductase inactivating alkylating agents
Author(s) -
Kersene Regina,
Maroziene Audrone,
Kliukiene Regina,
Anusevicius Zilvinas,
DidZiapctriene Janina,
Cenas Narimantas
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800203112
Subject(s) - chemistry , singlet oxygen , glutathione , phenylalanine , glutathione reductase , quenching (fluorescence) , reductase , amino acid , medicinal chemistry , biochemistry , oxygen , enzyme , organic chemistry , glutathione peroxidase , physics , quantum mechanics , fluorescence
In order to determine the rote of glutathione reductase (GR) in protection against AI‐phtalocyanine tetrasulfonate‐sensitized human erythrocyte photolysis, we have studied the effects of antitumour alkylating agents that inactivate GR, on photohemolysis rate. The rates of inactivation of reduced GR decreased in order BCNU > pharanox (N‐p‐[bis‐(2‐chloroethyl)‐amino]‐phe‐nylacetic acid N‐oxide) > phenalol (N‐p‐[bis‐(2‐chloroethyl)‐amino]‐phenylacetyl‐L‐phenylalanine) > o‐F‐ and p‐F‐lophenal (o‐ and p‐isomers of N‐p‐[bis‐(2‐chloroethyl)‐amino]‐phenylacetyl‐D,L‐fluorophenylalanine) > D,L‐melphalan. As supposed, erythrocyte photolysis was accelerated by BCNU and pharanox, however, it was slowed down by phenylalanine mustards. The latter effect was explained by singlet oxygen quenching and/or photooxidation reactions of these compounds. This points out to a possibility of certain phenylalanine derivatives to neutralize the side‐effects of photodynamic therapy.