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

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.