Literature DB >> 6438625

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.   

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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Year:  1984        PMID: 6438625      PMCID: PMC392050          DOI: 10.1073/pnas.81.22.6934

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  14 in total

1.  Evidence for proteolytic fragments in commercial samples of human ceruloplasmin.

Authors:  L Rydén
Journal:  FEBS Lett       Date:  1971-11-01       Impact factor: 4.124

2.  A general method applicable to the search for similarities in the amino acid sequence of two proteins.

Authors:  S B Needleman; C D Wunsch
Journal:  J Mol Biol       Date:  1970-03       Impact factor: 5.469

3.  The subunit structure of thrombin-activated factor V. Isolation of activated factor V, separation of subunits, and reconstitution of biological activity.

Authors:  C T Esmon
Journal:  J Biol Chem       Date:  1979-02-10       Impact factor: 5.157

4.  Pattern recognition in nucleic acid sequences. I. A general method for finding local homologies and symmetries.

Authors:  W B Goad; M I Kanehisa
Journal:  Nucleic Acids Res       Date:  1982-01-11       Impact factor: 16.971

Review 5.  Factor V.

Authors:  M E Nesheim; J A Katzmann; P B Tracy; K G Mann
Journal:  Methods Enzymol       Date:  1981       Impact factor: 1.600

6.  Similar amino acid sequences: chance or common ancestry?

Authors:  R F Doolittle
Journal:  Science       Date:  1981-10-09       Impact factor: 47.728

7.  Internal triplication in the structure of human ceruloplasmin.

Authors:  N Takahashi; R A Bauman; T L Ortel; F E Dwulet; C C Wang; F W Putnam
Journal:  Proc Natl Acad Sci U S A       Date:  1983-01       Impact factor: 11.205

8.  Characterization of Factor V activation intermediates.

Authors:  M E Nesheim; W B Foster; R Hewick; K G Mann
Journal:  J Biol Chem       Date:  1984-03-10       Impact factor: 5.157

9.  Coordinate binding of factor Va and factor Xa to the unstimulated platelet.

Authors:  P B Tracy; M E Nesheim; K G Mann
Journal:  J Biol Chem       Date:  1981-01-25       Impact factor: 5.157

10.  Thrombin-catalyzed activation of human coagulation factor V.

Authors:  K Suzuki; B Dahlbäck; J Stenflo
Journal:  J Biol Chem       Date:  1982-06-10       Impact factor: 5.157

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  26 in total

1.  Identification of the prooxidant site of human ceruloplasmin: a model for oxidative damage by copper bound to protein surfaces.

Authors:  C K Mukhopadhyay; B Mazumder; P F Lindley; P L Fox
Journal:  Proc Natl Acad Sci U S A       Date:  1997-10-14       Impact factor: 11.205

2.  Contribution of A1 subunit residue Q316 in thrombin-activated factor VIII to A2 subunit dissociation.

Authors:  Ernest T Parker; Pete Lollar
Journal:  Biochemistry       Date:  2007-08-04       Impact factor: 3.162

3.  Simultaneous Cu-, Fe-, and Zn-specific detection of metalloproteins contained in rabbit plasma by size-exclusion chromatography-inductively coupled plasma atomic emission spectroscopy.

Authors:  Shawn A Manley; Simon Byrns; Andrew W Lyon; Peter Brown; Jürgen Gailer
Journal:  J Biol Inorg Chem       Date:  2008-09-10       Impact factor: 3.358

4.  Cloning of a cDNA coding for human factor V, a blood coagulation factor homologous to factor VIII and ceruloplasmin.

Authors:  W H Kane; E W Davie
Journal:  Proc Natl Acad Sci U S A       Date:  1986-09       Impact factor: 11.205

5.  Complete cDNA and derived amino acid sequence of human factor V.

Authors:  R J Jenny; D D Pittman; J J Toole; R W Kriz; R A Aldape; R M Hewick; R J Kaufman; K G Mann
Journal:  Proc Natl Acad Sci U S A       Date:  1987-07       Impact factor: 11.205

6.  Mass spectrometry-assisted study reveals that lysine residues 1967 and 1968 have opposite contribution to stability of activated factor VIII.

Authors:  Esther Bloem; Henriet Meems; Maartje van den Biggelaar; Carmen van der Zwaan; Koen Mertens; Alexander B Meijer
Journal:  J Biol Chem       Date:  2012-01-03       Impact factor: 5.157

7.  Internal duplication and sequence homology in factors V and VIII.

Authors:  D N Fass; R M Hewick; G J Knutson; M E Nesheim; K G Mann
Journal:  Proc Natl Acad Sci U S A       Date:  1985-03       Impact factor: 11.205

8.  Aceruloplasminemia: molecular characterization of this disorder of iron metabolism.

Authors:  Z L Harris; Y Takahashi; H Miyajima; M Serizawa; R T MacGillivray; J D Gitlin
Journal:  Proc Natl Acad Sci U S A       Date:  1995-03-28       Impact factor: 11.205

9.  Identification of four novel mutations in F5 associated with congenital factor V deficiency.

Authors:  Sachiko Kanaji; Taisuke Kanaji; Miho Honda; Sachie Nakazato; Kazuo Wakayama; Yoshitomi Tabata; Shoichiro Shibata; Hisashi Gondo; Ikuko Nakamura; Koichi Node; Masanori Miura; Masaharu Miyahara; Takashi Okamura; Fumio Nagumo; Shoichiro Ohta; Kenji Izuhara
Journal:  Int J Hematol       Date:  2008-12-04       Impact factor: 2.490

10.  Intact human ceruloplasmin oxidatively modifies low density lipoprotein.

Authors:  E Ehrenwald; G M Chisolm; P L Fox
Journal:  J Clin Invest       Date:  1994-04       Impact factor: 14.808

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