TY - JOUR
T1 - Expression of Bcl-xs in Xenopus oocytes induces BH3-dependent and caspase-dependent cytochrome c release and apoptosis
AU - Braun, Tali
AU - Dar, Shachar
AU - Vorobiov, Dmitry
AU - Lindenboim, Liora
AU - Dascal, Nathan
AU - Stein, Reuven
PY - 2003/1/1
Y1 - 2003/1/1
N2 - The mechanism of action of pro-apoptotic proteins is difficult to study in vivo because of their death effect, which makes it problematic to obtain sufficient homogeneous experimental material for biochemical analysis. We show here that pro-apoptotic genes expressed in Xenopus oocytes constitute a useful in vivo system for studying their mechanism of action. In the present study, we used this system to study the death effects of Bcl-xs, a pro-apoptotic member of the Bcl-2 family. The results showed that expression of Bcl-xs in oocytes induces oocyte death by a caspase-dependent mechanism, which includes BH3-dependent cytochrome c release and is inhibited by co-expression of the antiapoptotic proteins Bcl-2 and Bcl-XL. The release of cytochrome c was found to be dependent on caspase activity. Bcl-xs was localized mainly in the mitochondria, and Bcl-xs transmembrane and BH3 domains were required for its apoptotic effect. These findings suggest that Bcl-xs induces apoptosis in Xenopus oocytes mainly by its presence in the mitochondria, where it induces BH3- and caspase-dependent release of cytochrome c, which leads to oocyte death.
AB - The mechanism of action of pro-apoptotic proteins is difficult to study in vivo because of their death effect, which makes it problematic to obtain sufficient homogeneous experimental material for biochemical analysis. We show here that pro-apoptotic genes expressed in Xenopus oocytes constitute a useful in vivo system for studying their mechanism of action. In the present study, we used this system to study the death effects of Bcl-xs, a pro-apoptotic member of the Bcl-2 family. The results showed that expression of Bcl-xs in oocytes induces oocyte death by a caspase-dependent mechanism, which includes BH3-dependent cytochrome c release and is inhibited by co-expression of the antiapoptotic proteins Bcl-2 and Bcl-XL. The release of cytochrome c was found to be dependent on caspase activity. Bcl-xs was localized mainly in the mitochondria, and Bcl-xs transmembrane and BH3 domains were required for its apoptotic effect. These findings suggest that Bcl-xs induces apoptosis in Xenopus oocytes mainly by its presence in the mitochondria, where it induces BH3- and caspase-dependent release of cytochrome c, which leads to oocyte death.
UR - http://www.scopus.com/inward/record.url?scp=0037226618&partnerID=8YFLogxK
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AN - SCOPUS:0037226618
SN - 1541-7786
VL - 1
SP - 186
EP - 194
JO - Molecular Cancer Research
JF - Molecular Cancer Research
IS - 3
ER -