Institute for Evolutionary Biology, WWU Münster, Münster, Germany.
Max Planck-Institute for Biology Tuebingen, Tübingen, Germany.
J Mol Evol. 2022 Dec;90(6):418-428. doi: 10.1007/s00239-022-10071-3. Epub 2022 Oct 1.
Vertebrate blood coagulation is controlled by a cascade containing more than 20 proteins. The cascade proteins are found in the blood in their zymogen forms and when the cascade is triggered by tissue damage, zymogens are activated and in turn activate their downstream proteins by serine protease activity. In this study, we examined proteomes of 21 chordates, of which 18 are vertebrates, to reveal the modular evolution of the blood coagulation cascade. Additionally, two Arthropoda species were used to compare domain arrangements of the proteins belonging to the hemolymph clotting and the blood coagulation cascades. Within the vertebrate coagulation protein set, almost half of the studied proteins are shared with jawless vertebrates. Domain similarity analyses revealed that there are multiple possible evolutionary trajectories for each coagulation protein. During the evolution of higher vertebrate clades, gene and genome duplications led to the formation of other coagulation cascade proteins.
脊椎动物的血液凝固是由一个包含 20 多种蛋白质的级联反应控制的。级联反应中的蛋白质以酶原形式存在于血液中,当级联反应被组织损伤触发时,酶原被激活,并通过丝氨酸蛋白酶活性依次激活其下游蛋白质。在这项研究中,我们研究了 21 种脊索动物的蛋白质组,其中 18 种是脊椎动物,以揭示血液凝固级联反应的模块化进化。此外,还使用了两种节肢动物物种来比较属于血淋巴凝结和血液凝固级联的蛋白质的结构域排列。在脊椎动物凝血蛋白组中,近一半的研究蛋白与无颌脊椎动物共有。结构域相似性分析表明,每个凝血蛋白都有多种可能的进化轨迹。在高等脊椎动物进化过程中,基因和基因组的加倍导致了其他凝血级联蛋白的形成。