E. Benhur et al., INHIBITION OF PHTHALOCYANINE-SENSITIZED PHOTOHEMOLYSIS OF HUMAN ERYTHROCYTES BY QUERCETIN, Photochemistry and photobiology, 57(6), 1993, pp. 984-988
Photohemolysis of erythrocytes in the presence of aluminum phthalocyan
ine tetrasulfonate as a sensitizer is inhibited by quercetin. D2O (98.
5%) stimulated photohemolysis regardless of quercetin presence, sugges
ting the participation of singlet oxygen in the process. Since it has
been shown that this flavonoid reacts with singlet oxygen, the protect
ive effect might be attributed, at least partially, to its competitive
reaction with singlet oxygen. At the molecular level, the alterations
of membrane proteins that escort the process of photohemolysis, such
as cross-linking of spectrin monomers and of other membrane proteins,
were selectively inhibited by quercetin. This effect was qualitatively
similar to that induced by NaF, suggesting that quercetin may, like N
aF, also inhibit type I photooxidations, which contribute to hemolysis
. The lipophilicity of quercetin seems to be an essential factor in th
e inhibition process; rutin, a water-soluble 3-rutinoside of quercetin
, had only a negligible protective effect on photohemolysis.