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. 1984 Nov;81(22):6934–6937. doi: 10.1073/pnas.81.22.6934

Coagulation factors V and VIII and ceruloplasmin constitute a family of structurally related proteins.

W R Church, R L Jernigan, J Toole, R M Hewick, J Knopf, G J Knutson, M E Nesheim, K G Mann, D N Fass
PMCID: PMC392050  PMID: 6438625

Abstract

Computer searches of the National Biomedical Research Foundation protein and nucleic acid sequence data bases using the NH2 terminus of the bovine factor Va 94-kilodalton heavy chain, the NH2 terminus of the 74-kilodalton factor Va light chain, and an internal 98-residue segment of porcine factor VIII revealed that both bovine factor V and porcine factor VIII are statistically homologous to human ceruloplasmin. The NH2-terminal segment of bovine factor Va heavy chain is homologous to three segments of ceruloplasmin sequence starting at residues 1, 351, and 713; the NH2-terminal sequence of bovine factor Va light chain is homologous to the same human ceruloplasmin sequence segments beginning at residues 1, 349, and 711. The longer porcine factor VIII sequence is homologous to three segments of human ceruloplasmin, residues 1-77, 400-433, and 683-791. These data indicate that factor V, factor VIII, and ceruloplasmin comprise a group of evolutionarily linked protein structures that possibly resulted from multiplication of ancestral precursor genes.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Doolittle R. F. Similar amino acid sequences: chance or common ancestry? Science. 1981 Oct 9;214(4517):149–159. doi: 10.1126/science.7280687. [DOI] [PubMed] [Google Scholar]
  2. Esmon C. T. The subunit structure of thrombin-activated factor V. Isolation of activated factor V, separation of subunits, and reconstitution of biological activity. J Biol Chem. 1979 Feb 10;254(3):964–973. [PubMed] [Google Scholar]
  3. Fass D. N., Knutson G. J., Katzmann J. A. Monoclonal antibodies to porcine factor VIII coagulant and their use in the isolation of active coagulant protein. Blood. 1982 Mar;59(3):594–600. [PubMed] [Google Scholar]
  4. Goad W. B., Kanehisa M. I. Pattern recognition in nucleic acid sequences. I. A general method for finding local homologies and symmetries. Nucleic Acids Res. 1982 Jan 11;10(1):247–263. doi: 10.1093/nar/10.1.247. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Kane W. H., Lindhout M. J., Jackson C. M., Majerus P. W. Factor Va-dependent binding of factor Xa to human platelets. J Biol Chem. 1980 Feb 10;255(3):1170–1174. [PubMed] [Google Scholar]
  6. Moshkov K. A., Lakatos S., Hajdu J., Závodsky P., Neifakh S. A. Proteolysis of human ceruloplasmin. Some peptide bonds are particularly susceptible to proteolytic attack. Eur J Biochem. 1979 Feb 15;94(1):127–134. doi: 10.1111/j.1432-1033.1979.tb12879.x. [DOI] [PubMed] [Google Scholar]
  7. Needleman S. B., Wunsch C. D. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J Mol Biol. 1970 Mar;48(3):443–453. doi: 10.1016/0022-2836(70)90057-4. [DOI] [PubMed] [Google Scholar]
  8. Nesheim M. E., Foster W. B., Hewick R., Mann K. G. Characterization of Factor V activation intermediates. J Biol Chem. 1984 Mar 10;259(5):3187–3196. [PubMed] [Google Scholar]
  9. Nesheim M. E., Foster W. B., Hewick R., Mann K. G. Characterization of Factor V activation intermediates. J Biol Chem. 1984 Mar 10;259(5):3187–3196. [PubMed] [Google Scholar]
  10. Nesheim M. E., Katzmann J. A., Tracy P. B., Mann K. G. Factor V. Methods Enzymol. 1981;80(Pt 100):249–274. doi: 10.1016/s0076-6879(81)80023-7. [DOI] [PubMed] [Google Scholar]
  11. Rydén L. Evidence for proteolytic fragments in commercial samples of human ceruloplasmin. FEBS Lett. 1971 Nov 1;18(2):321–325. doi: 10.1016/0014-5793(71)80477-5. [DOI] [PubMed] [Google Scholar]
  12. Suzuki K., Dahlbäck B., Stenflo J. Thrombin-catalyzed activation of human coagulation factor V. J Biol Chem. 1982 Jun 10;257(11):6556–6564. [PubMed] [Google Scholar]
  13. Takahashi N., Bauman R. A., Ortel T. L., Dwulet F. E., Wang C. C., Putnam F. W. Internal triplication in the structure of human ceruloplasmin. Proc Natl Acad Sci U S A. 1983 Jan;80(1):115–119. doi: 10.1073/pnas.80.1.115. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Tracy P. B., Nesheim M. E., Mann K. G. Coordinate binding of factor Va and factor Xa to the unstimulated platelet. J Biol Chem. 1981 Jan 25;256(2):743–751. [PubMed] [Google Scholar]
  15. Wolf P. L. Ceruloplasmin: methods and clinical use. Crit Rev Clin Lab Sci. 1982;17(3):229–245. doi: 10.3109/10408368209107037. [DOI] [PubMed] [Google Scholar]

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