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Rodent monophyly deduced from the unique gastric proteinase constitution and molecular phylogenetic analyses using pepsinogen-C cDNA sequences

机译:啮齿动物单系统推导出的独特的胃蛋白酶宪法和分子使用pepsinogen-C cDNA系统发育分析序列

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摘要

Pepsinogens are zymogens of pepsins, the gastric digestive proteinases. Although pepsinogen A is predominant in most mammalian species hitherto known, pepsinogen C is expressed exclusively and the lack of pepsinogen A is evidenced in the rat and guinea pig. Furthermore, in these two rodents, considerable amount of procathepsin E is also expressed in gastric mucosa although it is almost undetectable in other mammals. In this paper, in order to clarify whether such unique gastric proteinase constitution is common among rodents, we carried out purification and characterization of gastric proteinases, and molecular cloning of pepsinogen-C cDNAs from several rodent species including the degu and coypu. Pepsinogen C and procathepsin E were isolated but pepsinogen A was undetectable in the rodents, leading to the conclusion that that rodents commonly share the unique gastric proteinase constitution. This feature could be treated as a new "molecular synapomorphy", supporting strongly monophyly of the order Rodentia. From the molecular phylogenetic analyses of pepsinogen-C cDNA sequences, monophyly of the order Rodentia was also supported by the analyses with high statistic reliabilities. (c) 2006 Elsevier Inc. All rights reserved.
机译:胃蛋白酶原是胃蛋白酶的发酵菌,胃消化蛋白酶。主要在大多数哺乳动物物种迄今为止胃蛋白酶原C表达完全胃蛋白酶原的缺乏是证明老鼠和几内亚猪。啮齿动物,大量的组织蛋白原E在胃粘膜虽然也表示在其他哺乳动物几乎检测不到。纸,为了澄清是否这样独一无二的胃蛋白酶宪法中比较普遍啮齿动物,我们进行净化和胃蛋白酶的特性,分子克隆pepsinogen-C互补一些包括八齿鼠和啮齿动物物种河狸鼠。隔离但胃蛋白酶原是发现不了的啮齿动物,主要的结论啮齿动物一般分享独特的胃蛋白酶宪法。作为一个新的“分子共源性状”,强烈支持单系统的秩序啮齿目。pepsinogen-C cDNA序列的分析,单系统订单的啮齿目也支持与高统计分析的可靠性。保留。

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