Characterization of a ribonucleic acid transcript from the brook trout (Salvelinus fontinalis) ovary with structural similarities to mammalian adipsin complement factor D and tissue kallikrein, and the effects of kallikrein-like serine proteases on follicle contraction
Characterization of a ribonucleic acid transcript from the brook trout (Salvelinus fontinalis) ovary with structural similarities to mammalian adipsin complement factor D and tissue kallikrein, and the effects of kallikrein-like serine proteases on follicle contraction
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DOI：
10.1095/biolreprod58.4.887
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发表时间：
1998-04-01
影响因子：
3.6
通讯作者：
Sokal, N
中科院分区：
文献类型：
--
作者：
Hajnik, CA;Goetz, FW;Sokal, N
从鳟鱼排卵 cDNA 文库中分离出 2.4 千碱基 (kb) 克隆（激肽释放酶鳟鱼 #14；KT-14）。 KT-14 含有 768 个碱基对 (bp) 的开放阅读框 (ORF)，可能编码 255 个氨基酸的蛋白质。 KT-14 cDNA 还包含一个 711 bp 5' 非翻译区和一个位于 ORF 下游的 793 bp 区域，其中包括重复 12 次的 66 bp 序列。 KT-14 ORF 的氨基酸序列与猪补体因子 D 的氨基酸序列有 41% 相同，与猪胰激肽释放酶的氨基酸序列有 33% 相同。在卵巢组织的 Northern 印迹中，KT-14 与 1.8、2.4、2.9 和 3.2 kb 的四种转录物杂交。虽然 3.2-kb 和 2.4-kb 转录本在减数分裂成熟之前存在于卵巢中，但它们分别在排卵时和排卵后 12 小时显着上调。针对重组 KT-14 蛋白构建的抗体可识别卵巢组织和体液中的一种 30 kDa 免疫原性蛋白。这种免疫原性蛋白质在排卵时在组织中显着升高。通过卵泡减肥生物测定，我们提供了间接证据，证明哺乳动物激肽释放酶和相关丝氨酸蛋白酶可以刺激溪鳟鱼卵泡收缩。因此，KT-14 蛋白的一种可能的功能可能是调节排卵时卵母细胞的排出。
A 2.4-kilobase (kb) clone (kallikrein trout #14; KT-14) was isolated from a brook trout ovulatory cDNA library. KT-14 contains an open reading frame (ORF) of 768 base pairs (bp), presumably encoding a protein of 255 amino acids. The KT-14 cDNA also contains a 711-bp 5' untranslated region and a 793-bp region downstream of the ORF that includes a 66-bp sequence repeated 12 times. The amino acid sequence of the KT-14 ORF is 41% identical to that of porcine complement factor D and 33% identical to that of porcine pancreatic kallikrein. On Northern blots of ovarian tissue, KT-14 hybridized with four transcripts of 1.8, 2.4, 2.9, and 3.2 kb. While the 3.2- and 2.4-kb transcripts were present in the ovary prior to meiotic maturation, they were significantly up-regulated at ovulation and at 12 h postovulation, respectively. Antibodies constructed against the recombinant KT-14 protein recognized one 30-kDa immunogenic protein in ovarian tissue and fluid. This immunogenic protein was significantly elevated in the tissue by ovulation. Using a follicle weight loss bioassay, we provide indirect evidence that mammalian kallikrein and related serine proteases can stimulate brook trout follicle contraction. Thus, one possible function of the KT-14 protein may be the regulation of oocyte expulsion at ovulation.