EVOLUTIONARY ORIGIN OF NUMEROUS KRINGLES IN HUMAN AND SIMIAN APOLIPOPROTEIN(A)

被引：19

作者：

IKEO, K

TAKAHASHI, K

GOJOBORI, T

机构：

[1] NATL INST GENET,DNA RES CTR,MISHIMA,SHIZUOKA 411,JAPAN

[2] GRAD UNIV ADV STUDIES,MISHIMA 411,JAPAN

[3] SHIMANE MED UNIV,DEPT PHYSIOL,IZUMO,SHIMANE 693,JAPAN

来源：

FEBS LETTERS | 1991年 / 287卷 / 1-2期

关键词：

MOLECULAR EVOLUTION; KRINGLE; BLOOD COAGULATION; SERINE PROTEASE;

D O I：

10.1016/0014-5793(91)80036-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Human apolipoprotein(a) has a great size heterogeneity and consists of 38 kringle domains in the amino terminal and a serine protease 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.

引用

页码：146 / 148

页数：3

共 22 条

[21] IDENTIFICATION AND PRIMARY SEQUENCE OF AN UNSPLICED HUMAN UROKINASE POLY(A)+ RNA [J].