Regulation of M-phase progression in Chaetopterus oocytes by protein kinase C.
Regulation of M-phase progression in Chaetopterus oocytes by protein kinase C.
复制标题
蛋白激酶 C 调节毛鳍鱼卵母细胞的 M 期进程。
DOI：
10.1016/0012-1606(92)90294-q
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发表时间：
1992
影响因子：
2.7
通讯作者：
Palazzo,RE
中科院分区：
文献类型：
--
作者：
Eckberg,WR;Palazzo,RE
我们研究了蛋白激酶C在全色毛翅目鱼类卵母细胞中的存在及其在生发泡破裂(GVBD)发生中的作用。首先，我们证明了卵母细胞含有一种磷脂和钙依赖的蛋白激酶，即蛋白激酶C(PKC)。由于PKC是佛波醇酯的主要细胞内受体，我们测试了佛波醇12，13-二丁酸酯(PDBu)诱导GVBD的能力，并比较了PDBu诱导的GVBD与正常(海水)诱导的GVBD所涉及的几个关键事件和过程。海水和100-200nMPDBu在相似的时间过程中诱导染色体凝聚、纺锤体形成和纺锤体迁移。这两种处理都导致新合成蛋白质的SDS-PAGE图谱发生了类似的变化。约46 kDa和54 kDa的多肽合成明显增加。两种处理均能提高卵母细胞蛋白质的磷酸化水平，尤其是22、32、46、55、和84 kDa的蛋白质。这两种处理都导致M期特异性组蛋白H1激酶活性的激活，这表明成熟促进因子的出现。星形孢子素是一种有效的蛋白激酶C抑制剂，可阻断GVBD和M期特异性H1激酶的激活，而优先拮抗蛋白激酶A的HA1004则没有作用。这项研究的结果表明，蛋白激酶C可以激活GVBD中涉及的一系列必要的生化和形态过程。此外，这些研究表明，蛋白激酶C通过激活成熟促进因子而引起GVBD，并支持蛋白激酶C在该物种的卵母细胞成熟中起重要作用的假说。
We have examined the presence of protein kinase C in oocytes ofChaetopterus pergamentaceusand its role in the initiation of germinal vesicle breakdown (GVBD). First, we demonstrated that the oocytes contain a phospholipid- and calcium-dependent protein kinase, protein kinase C (PKC). Since PKC is the primary intracellular receptor for phorbol esters, we tested the ability of phorbol 12,13-dibutyrate (PDBu) to induce GVBD and compared several critical events and processes involved in GVBD induced by PDBu to those induced normally (by seawater). Seawater and 100–200 nMPDBu induced chromosome condensation, spindle formation, and spindle migration over a similar time course. Both treatments induced similar alterations in the SDS-PAGE pattern of newly synthesized proteins. The synthesis of polypeptides of approximately 46 and 54 kDa increased specifically. Both treatments increased oocyte protein phosphorylation, especially of proteins of 22, 32, 46, 55, 64, and 84 kDa. Both treatments resulted in the activation of an M-phase-specific histone H1 kinase activity, which demonstrates the appearance of maturation-promoting factor. Staurosporine, a potent protein kinase C inhibitor, blocked GVBD and the activation of M-phase-specific H1 kinase, whereas HA1004, which preferentially antagonizes protein kinase A, had no effect. The results of this study demonstrate that protein kinase C can activate a wide spectrum of essential biochemical and morphological processes involved in GVBD. Further, these studies suggest that protein kinase C elicits GVBD by activating maturation-promoting factor and support the hypothesis that protein kinase C plays an essential role in oocyte maturation in this species.