Evolutionary origin of numerous kringles in human and simian apolipoprotein(a)

FEBS Letters

Ikeo, Kazuho¹  Takahashi, Kei²  Gojobori, Takashi¹ 

[1] DNA Research Center, National Institute of Genetics, Mishima 411, Japan;Department of Physiology, Shimane Medical University, Izumo 693, Japan

关键词: Molecular evolution;    Kringle;    Blood coagulation;    Serine proteasc;   

DOI  :  10.1016/0014-5793(91)80036-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Human apolipoprotein(a) has a great size heterogeneity and consists of 38 kringle domains in the amino terminal and a serine proteasc domain in the carboxyl terminal. All but one kringle of apolipoprotein(a) are homologous to the fourth kringle of plasminogen. However, the 38th kringle resembles the fifth kringle of plasminogen and it seems to have been deleted in simian species. The phylogenetic trees suggest that an ancestral apolipoprotein(a) may have started with a duplicate of a plasminogen type protein. It also implies that deletion of the three kringles in the amino terminus followed, and that one of the remaining two kringles was duplicated in both human and simian species and the other was processed by a deletion in simian species after species separation. Thus, the number of kringles in other mammals not yet studied may vary considerably from species to species.

【 授权许可】

Unknown