AN EXTRAOVARIAN PROTEIN ACCUMULATED IN MOSQUITO OOCYTES IS A CARBOXYPEPTIDASE ACTIVATED IN EMBRYOS
AN EXTRAOVARIAN PROTEIN ACCUMULATED IN MOSQUITO OOCYTES IS A CARBOXYPEPTIDASE ACTIVATED IN EMBRYOS
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DOI：
10.1073/pnas.88.23.10821
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发表时间：
1991-12-01
影响因子：
11.1
通讯作者：
RAIKHEL, AS
中科院分区：
文献类型：
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作者：
CHO, WL;DEITSCH, KW;RAIKHEL, AS
我们报告了一个现象，以前未知的卵生动物，在埃及伊蚊的丝氨酸羧肽酶合成卵巢外，然后内化的卵母细胞。克隆了蚊卵黄生成羧肽酶（VCP）的cDNA并进行了序列测定。VCP cDNA与仅存在于卵黄发生雌性的脂肪体中的1.5-脱氢酶mRNA杂交。推导的氨基酸序列与丝氨酸羧肽酶家族的成员具有显著的同源性。使用丝氨酸蛋白酶抑制剂，[H-3]二异丙基氟磷酸盐的结合试验表明，VCP在胚胎发育开始时在鸡蛋中被激活。VCP的激活与其大小从53 kDa（无活性的酶原）减少到48 kDa（活性酶）有关。VCP的活性，48-kDa，形式是最大的存在于胚胎发育的中期，并在结束时消失。
We report a phenomenon previously unknown for oviparous animals; in Aedes aegypti mosquitoes a serine carboxypeptidase is synthesized extraovarially and then internalized by oocytes. The cDNA encoding mosquito vitellogenic carboxypeptidase (VCP) was cloned and sequenced. The VCP cDNA hybridizes to a 1.5-kilobase mRNA present only in the fat body of vitellogenic females. The deduced amino acid sequence of VCP shares significant homology with members of the serine carboxypeptidase family. Binding assays using a serine protease inhibitor, [H-3]diisopropyl fluorophosphate, showed that VCP is activated in eggs at the onset of embryonic development. Activation of VCP is associated with the reduction in its size from 53 kDa (inactive proenzyme) to 48 kDa (active enzyme). The active, 48-kDa, form of VCP is maximally present at the middle of embryonic development and disappears by the end.