Influence of microcystin-YR and nodularin on the activity of some proteolytic enzymes in mouse liver.
The activity of cathepsins D and L, arginine aminopeptidase, dipeptidase II and dipeptidase IV was determined in the lysosomal, microsomal, cytoplasmatic fractions and in the complete homogenate of the mouse hepatocytes following injection of microcystin-YR and nodularin. The effect of both toxins depended on the time of action and on the fraction of cell cytoplasm. Microcystin-YR inhibited the synthesis of the studied proteases and caused a labialization of lysosomal membranes, whereas nodularin induced the synthesis of the enzymes and destabilized the reticulum endoplasmatic membranes.
Lankoff
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Department of Radiobiology and Immunology, Pedagogical University, Kielce, Swietokrzyska, Poland. alankoff@pu.kielce.pl
Kolataj
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D000704:Analysis of Variance; D000818:Animals; D002403:Cathepsins / Q000378:metabolism; D000458:Cyanobacteria; D004150:Dipeptidases / Q000378:metabolism*; D005260:Female; D008099:Liver / Q000187:drug effects* / Q000201:enzymology*; D008387:Marine Toxins / Q000494:pharmacology*; D051379:Mice; D052998:Microcystins; D010456:Peptides, Cyclic / Q000494:pharmacology*
D008387:Marine Toxins; D052998:Microcystins; D010456:Peptides, Cyclic; C063998:nodularin; C065685:microcystin YR; D002403:Cathepsins; D004150:Dipeptidases