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INVESTIGATIONS ON THE MECHANISM OF CHLORPROMAZINE PHOTOTOXICITY: EFFECTS ON LYSOSOMES OF CULTURED HUMAN FIBROBLASTS
Author(s) -
Hasei Kazuyoshi,
Ichihashi Masamitsu,
Mojamdar Manoj
Publication year - 1984
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1984.tb04586.x
Subject(s) - acid phosphatase , phototoxicity , chemistry , chlorpromazine , enzyme , microbiology and biotechnology , mechanism of action , biochemistry , pharmacology , in vitro , biology
The effect of chlorpromazine (CPZ) and UVA on lysosomes of cultured normal human fibroblasts has been investigated. Acid phosphatase (ACPase) activity in 12 000 g pellet of cells treated with CPZ (10 μg/m l ) and UVA (6 × 10 4 J/m 2 ) was found to be decreased as compared with non‐treated, CPZ or UVA treated control cells. This decrease, however, was not accompanied by a concomitant increase in ACPase activity in the 12 000 g supernatant. The addition of Triton X‐100 to cells pretreated with CPZ + UVA resulted in only a moderate increase in ACPase activity of the 12 000 g supernatant. ACPase activity of the cells incubated in media containing preirradiated CPZ was also found to he decreased. These results indicate that CPZ + UVA directly inactivate lysosomal enzymes, possibly without affecting the membrane.