Suppression of oxidative stress-induced XXXX by calpain antisense.

@entity5427 @entity99 @entity66 @entity63 @entity14410 @entity880 @entity141 @entity2469 @entity1673 @entity130
BACKGROUND: Calpain, a cytosolic @entity141 -dependent proteinase, plays a pivotal role in cell injury. In this study, we investigated the effect of calpain-mu antisense oligonucleotide on oxidative stress induced- @entity130 . MATERIALS AND METHODS: Hemagglutinating virus of Japan liposome complex with one of three types of antisense oligonucleotide ( @entity1673 , @entity5427 , @entity14410 ) or scramble oligonucleotide was added to the culture medium of HuH7 cells and incubated for 6 days. The expression of calpain-mu protein was examined by Western blotting. After the addition of @entity2469 , bleb formation was examined by phase contrast microscopy, and cell viability was assessed by the release of @entity880 dehydrogenase. RESULTS: Incubation of HuH7 cells with @entity5427 resulted in a decrease in the amount of calpain on day 4 and a further decrease to almost undetectable levels on day 6, whereas scramble oligonucleotide had no effect. Bleb formation was observed 120 min after the addition of @entity2469 in scramble oligonucleotide-treated cells as in untreated cells. In contrast, it was rarely observed in @entity5427 -treated cells. @entity880 dehydrogenase release was significantly suppressed in @entity5427 -treated cells, compared with that in scramble oligonucleotide treated-cells. CONCLUSIONS: Our findings suggest that calpain activation is involved in the pathogenesis of @entity66 and that transfection of calpain antisense may potentially protect against @entity63 /reperfusion @entity99 .
