Characterization of a cDNA Encoding Murine Coagulation Factor VII

SummaryThe cDNA encoding murine coagulation factor VII (mfVII) was isolated and reconstructed from a Λ Zap cDNA library generated from murine liver mRNA. The cDNA contains 1903 nucleotides spanning 15 bases upstream of the 5’-translation initiation codon, an open reading frame of 1338 nucleotides, 550 nucleotides downstream of the first stop codon and a 3’ poly(A) tail. The translation product is composed of a 41-amino acid signal/propeptide region followed by a 405-residue mature protein. The latter is highly homologous to that of human, rabbit, bovine, Rhesus monkey, and canine fVII. All protein domains of hfVII are strictly conserved in mfVII.

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Cloning and Characterization of a cDNA Encoding Murine Coagulation Factor X

Thrombosis and Haemostasis ◽

10.1055/s-0037-1615144 ◽

1998 ◽

Vol 80 (07) ◽

pp. 87-91 ◽

Cited By ~ 2

Author(s):

Zhong Liang ◽

Adrian Cooper ◽

Melanie DeFord ◽

Peter Carmeliet ◽

Desire Collen ◽

...

Keyword(s):

Stop Codon ◽

Coagulation Factor ◽

Factor X ◽

Human Embryonic Kidney ◽

Reading Frame ◽

293 Cells ◽

Murine Liver ◽

Translation Initiation Codon ◽

Amino Acid Signal

SummaryThe cDNA encoding murine coagulation factor X (fX) was isolated and reconstructed from a λZap cDNA library generated from murine liver mRNA. The cDNA contains 1486 bases starting at the 5’-translation initiation codon. It includes an open reading frame of 1443 nucleotides, followed by an 18 residue 3’ nontranslated sequence downstream of the first stop codon, and a 3’ poly(A) tail. The translation product is composed of a 40-amino acid signal/propeptide region followed by a 441-residue mature protein. The latter is highly homologous to that of human and rat fX. All protein domains of human and rat fX are strictly conserved in mouse fX. The cDNA coding for mouse fX has been expressed in human embryonic kidney 293 cells and generates fX activity measured in a clotting assay using human fX-deficient plasma.

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Characterization of Transcriptional Regulatory Elements in the Promoter Region of the Murine Blood Coagulation Factor VII Gene

Journal of Biological Chemistry ◽

10.1074/jbc.273.4.2277 ◽

1998 ◽

Vol 273 (4) ◽

pp. 2277-2287 ◽

Cited By ~ 16

Author(s):

Daniel R. Stauffer ◽

Beatrice N. Chukwumezie ◽

Julie A. Wilberding ◽

Elliot D. Rosen ◽

Francis J. Castellino

Keyword(s):

Blood Coagulation ◽

Promoter Region ◽

Coagulation Factor ◽

Regulatory Elements ◽

Factor Vii ◽

Transcriptional Regulatory Elements ◽

Coagulation Factor Vii ◽

Transcriptional Regulatory

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Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII

Glycoconjugate Journal ◽

10.1007/s10719-008-9143-7 ◽

2008 ◽

Vol 25 (9) ◽

pp. 827-842 ◽

Cited By ~ 20

Author(s):

François Fenaille ◽

Catherine Groseil ◽

Christine Ramon ◽

Sandrine Riandé ◽

Laurent Siret ◽

...

Keyword(s):

Coagulation Factor ◽

Mass Spectrometric ◽

Factor Vii ◽

Coagulation Factor Vii

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Characterization of canine coagulation factor VII and its complex formation with tissue factor: canine-human cross-species compatibility

Journal of Thrombosis and Haemostasis ◽

10.1111/j.1538-7836.2010.03931.x ◽

2010 ◽

Vol 8 (8) ◽

pp. 1763-1772 ◽

Cited By ~ 11

Author(s):

T. KNUDSEN ◽

A. T. KRISTENSEN ◽

B. B. SØRENSEN ◽

O. H. OLSEN ◽

H. R. STENNICKE ◽

...

Keyword(s):

Complex Formation ◽

Tissue Factor ◽

Coagulation Factor ◽

Factor Vii ◽

Coagulation Factor Vii

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Cloning and Characterization of a Nonhemolytic Phospholipase C Gene from Burkholderia pseudomallei

Journal of Clinical Microbiology ◽

10.1128/jcm.37.11.3742-3745.1999 ◽

1999 ◽

Vol 37 (11) ◽

pp. 3742-3745 ◽

Cited By ~ 13

Author(s):

Sunee Korbsrisate ◽

Nuttiga Suwanasai ◽

Amornrut Leelaporn ◽

Takayuki Ezaki ◽

Yoshiaki Kawamura ◽

...

Keyword(s):

Amino Acid ◽

Phospholipase C ◽

Burkholderia Pseudomallei ◽

Immunoglobulin M ◽

Mature Protein ◽

Reading Frame ◽

Heat Stable ◽

Amino Acid Signal Peptide ◽

Amino Acid Signal

We cloned and characterized a phosphatidylcholine-hydrolyzing phospholipase C (PC-PLC) gene from Burkholderia pseudomallei. DNA sequence analysis of the gene indicated an open reading frame coding for 700 amino acids with a 34-amino-acid signal peptide. When cleaved, this yields a secreted 73-kDa mature protein. The deduced amino acid sequence exhibited 48% similarity to that of a nonhemolytic PLC from Pseudomonas aeruginosa. The expressed PC-PLC was heat stable, nonhemolytic for sheep erythrocytes, and active between pH 2 and 8. Western blot analysis with sera from melioidosis patients indicated that they produced immunoglobulin M antibodies against this PC-PLC protein.

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Cloning of Guinea Pig Tissue Factor cDNA: Comparison of Primary Structure among Six Mammalian Species

Thrombosis and Haemostasis ◽

10.1055/s-0037-1613836 ◽

2000 ◽

Vol 83 (03) ◽

pp. 455-461 ◽

Cited By ~ 3

Author(s):

Rui-Jin Shi ◽

Wen-Zhou Li ◽

Victor Marder ◽

Lee Sporn

Keyword(s):

Guinea Pig ◽

Tissue Factor ◽

Catalytic Domain ◽

Mammalian Species ◽

Coagulation Factor ◽

Apparent Molecular Weight ◽

Procoagulant Activity ◽

Factor Vii ◽

Reading Frame ◽

Coagulation Factor Vii

SummaryTissue factor (TF) is a transmembrane glycoprotein that serves as an essential cofactor for plasma coagulation factor VII. TF procoagulant activity exhibits varying species specificity. In particular, guinea pig (GP) TF is unable to activate clotting in heterologous plasma systems, but the molecular basis for this phenomenon is not yet understood. The full-length GP TF cDNA was cloned and sequenced. The open reading frame encoded a predicted precursor protein of 289 amino acids (aa) which was expressed in a reticulocyte lysate system as a protein of apparent molecular weight of 34 kD. The identity of the predicted aa sequence of mature GP TF with rabbit, human, bovine, rat and mouse TF was 66.4, 64.4, 60.6, 53.2 and 52.2%, respectively. With a focus on sites of potential functional significance, we compared sequences within the known binding regions. The eleven residues at the interface region between the TF1 and TF2 modules, which bind to the EGF domain of VIIa, were perfectly conserved among the six species, with the exception of an isoleucine replacing a lysine in the guinea pig sequence. However, only four of the eleven binding residues in the TF1 module, known to interact with the catalytic domain of factor VII, and three of the five residues in the TF2 module, involved in binding the factor VII Gla domain, were conserved among species. We hypothesize that divergence at these regions contributes to the specificity and non-reciprocity of TF procoagulant activity between species.

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Nucleotide Structure and Characterization of the Murine Blood Coagulation Factor VII Gene

Thrombosis and Haemostasis ◽

10.1055/s-0038-1650692 ◽

1996 ◽

Vol 76 (06) ◽

pp. 0957-0964 ◽

Cited By ~ 6

Author(s):

Esohe Idusogie ◽

Elliot D Rosen ◽

Peter Carmeliet ◽

Desire Collen ◽

Francis J Castellino

Keyword(s):

Consensus Sequence ◽

Protein A ◽

Coagulation Factor ◽

Factor Vii ◽

Gene Encoding ◽

Coagulation Factor Vii ◽

Splice Junctions ◽

Extension Analysis ◽

Major Domain

SummaryThe gene encoding murine coagulation factor VII (fVII) has been cloned. Seven introns and eight exons are present, with the introns positioned as splice junctions between the major domain units of the protein. A total of 11,748 bp of the gene was sequenced, and included 1,077 bp of a 5’-flanking region, in which several high probability binding sites for liver transcription factors were present, as well as a CCAAT sequence and possible GC boxes. Primer extension analysis revealed that the major transcription start site was positioned only 9 residues upstream of the ATG initiation codon, thus providing a very short 5’-untranslated region of the gene. The sequence of the CAP site in the murine fVII gene matched exactly the consensus eukaryotic sequence. A total of 1,484 bp of 3’-flanking nucleotides included a probable polyadenylation site (ATTAAA) and an appropriately positioned downstream consensus sequence (AGTGTTTC) for the efficient formation of a 3’ terminus of mRNA. These results indicate that all elements are present for liver-based transcription of the gene for murine factor VII. The sequence and restriction endonuclease map of this gene will facilitate construction of fVII deficient mice and mice containing mutant fVII genes.

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