Ito Yoichi, Sonobe Haruyuki
Institute of Intelligent Information and Communications Technology, Konan University, Kobe, Japan.
Ann N Y Acad Sci. 2009 Apr;1163:421-4. doi: 10.1111/j.1749-6632.2009.04465.x.
In the silkworm Bombyx mori, ecdysteroid 22-kinase (EcKinase) has been shown to catalyze the conversion of free ecdysteroids to physiologically inactive ecdysteroid 22-phosphates. First, a phylogenetic analysis of EcKinase showed that many proteins homologous to B. mori EcKinase are found mainly in Ecdysozoa, including insects and nematodes. Next, by RT-PCR analysis combined with laser microdissection and by immunohistochemistry, we demonstrated that free ecdysteroids in the B. mori ovary are synthesized in follicle cells and transferred into the oocyte where they are phosphorylated by EcKinase whose mRNA originates from nurse cells and the oocyte itself.
在家蚕中,蜕皮甾体22 -激酶(EcKinase)已被证明可催化游离蜕皮甾体转化为生理上无活性的蜕皮甾体22 -磷酸酯。首先,对EcKinase的系统发育分析表明,许多与家蚕EcKinase同源的蛋白质主要存在于蜕皮动物中,包括昆虫和线虫。其次,通过结合激光显微切割的RT - PCR分析和免疫组织化学,我们证明家蚕卵巢中的游离蜕皮甾体是在卵泡细胞中合成的,并转移到卵母细胞中,在那里它们被EcKinase磷酸化,EcKinase的mRNA来源于滋养细胞和卵母细胞自身。