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

Kazuho Ikeo, Kei Takahashi, Takashi Gojobori*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

16 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)146-148
Number of pages3
JournalFEBS Letters
Issue number1-2
StatePublished - Aug 5 1991
Externally publishedYes


  • Blood coagulation
  • Kringle
  • Molecular evolution
  • Serine proteasc

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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