Curtin University Homepage
  • Library
  • Help
    • Admin

    espace - Curtin’s institutional repository

    JavaScript is disabled for your browser. Some features of this site may not work without it.
    View Item 
    • espace Home
    • espace
    • Curtin Research Publications
    • View Item
    • espace Home
    • espace
    • Curtin Research Publications
    • View Item

    Characterization of porcine factor VII, X and comparison with human factor VII, X

    Access Status
    Fulltext not available
    Authors
    Chen, Younan
    Qiao, J.
    Tan, W.
    Lu, Y.
    Qin, S.
    Zhang, J.
    Li, S.
    Bu, H.
    Cheng, J.
    Date
    2009
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Chen, Y. and Qiao, J. and Tan, W. and Lu, Y. and Qin, S. and Zhang, J. and Li, S. et al. 2009. Characterization of porcine factor VII, X and comparison with human factor VII, X. Blood Cells, Molecules, and Diseases. 43 (1): pp. 111-118.
    Source Title
    Blood Cells, Molecules, and Diseases
    DOI
    10.1016/j.bcmd.2009.02.004
    ISSN
    1079-9796
    School
    School of Biomedical Sciences
    URI
    http://hdl.handle.net/20.500.11937/20838
    Collection
    • Curtin Research Publications
    Abstract

    Objective: Factor VII (FVII) and factor X (FX) are two predominant molecules of coagulation cascade. Whether porcine FVII and FX could efficiently work in human circulation is important for successful pig to human liver transplantation. We compared the genetic characterizations and coagulation activities of porcine and human FVII and FX to shed insight into the further investigation of potential inter-species molecular incompatibility between porcine FVII, FX and human derived procoagulants and anticoagulants in xenotransplantation. Methods: Multiple rounds of PCR were used to screen the positive clones from a porcine liver tissue cDNA library. 5' RACE and 3' RACE were conducted to get the full-length cDNA. The three-dimensional structure of protein was modeled by Swiss-Model program. Prothrombin Time (PT) of porcine and human plasma was determined by coagulation autoanalyzer. Activities of porcine FVII and FX were detected by adding the porcine plasma into FVII or FX-deficient human plasma. Results: We cloned the full-length cDNA of porcine FVII and FX, which contained 1416 bp and 1856 bp, coding 445 and 479 amino acids, respectively. Porcine FVII and FX shared 74.08% and 73.1% amino acid identities with human FVII and FX. Sequence alignments showed that porcine FVII might have additional ?-carboxyglutamic acid in Gla domain, and one important variation of Lys62-Glu in light chain. No significant difference was observed in TF binding region of heavy chain, while 4 variations were identified in the important functional residues responsible for proteolysis activity, as Gln217-Glu, Thr151-Lys, Glu154-Val and Gln40-Leu. However, no apparent change was displayed in the 3-D model of the heavy chain of porcine FVII. When porcine FX was analyzed, great variations have been found at active peptide (Ser143 to Arg194) with only 11.6% identity. Some important variations at ?-carboxyglutamic acids and Ca2+ binding sites were identified, while high conservations were discovered at other functional sites. Comparisons on 3-D protein models demonstrated that the protein backbones of porcine and human FX were highly conserved, and little difference was shown at the molecular surface of anticoagulant binding sites S2 and S3. PT detection of porcine and human plasma showed similar results, while coagulation activities of porcine FVII and FX were remarkably higher than that of human. Conclusion: Porcine FVII and FX showed relatively high homology with human FVII and FX in nucleotide, amino acid sequences and three-dimensional structure. However, the different affinities to important macromolecules caused by genetic differences might contribute to the molecular incompatibilities in liver xenotransplantation. © 2009 Elsevier Inc. All rights reserved.

    Related items

    Showing items related by title, author, creator and subject.

    • Cloning of porcine platelet glycoprotein Iba and comparison with the human homolog
      Shi, M.; Qiao, J.; Shen, Y.; Lu, Y.; Chen, Younan; Cheng, J. (2012)
      Glycoprotein Ib-IX-V (GPIb-IX-V) is a platelet adhesion receptor complex that initiates platelet aggregation. Glycoprotein Iba (GPIba) is the central component of the GPIb-IX-V complex, anchoring the complex to the ...
    • cDNA Cloning, Protein Structure Modeling of Rhesus Monkey (Macaca mulatta) Prothrombin
      Qin, S.; Tan, W.; Chen, Younan; Lu, Y.; Lu, X.; Li, Y.; Li, H.; Wang, L.; Cheng, J. (2008)
      Objective: Hemorrhagic diseases have been considered to be one of the main causes of xenotransplantation failure. To explore the role of the rhesus monkey (Macaca mulatta) coagulation system in a pig-to-human xenotransplantation ...
    • Size exclusion chromatography as a tool for natural organic matter characterisation in drinking water treatment
      Allpike, Bradley (2008)
      Natural organic matter (NOM), ubiquitous in natural water sources, is generated by biogeochemical processes in both the water body and in the surrounding watershed, as well as from the contribution of organic compounds ...
    Advanced search

    Browse

    Communities & CollectionsIssue DateAuthorTitleSubjectDocument TypeThis CollectionIssue DateAuthorTitleSubjectDocument Type

    My Account

    Admin

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    Follow Curtin

    • 
    • 
    • 
    • 
    • 

    CRICOS Provider Code: 00301JABN: 99 143 842 569TEQSA: PRV12158

    Copyright | Disclaimer | Privacy statement | Accessibility

    Curtin would like to pay respect to the Aboriginal and Torres Strait Islander members of our community by acknowledging the traditional owners of the land on which the Perth campus is located, the Whadjuk people of the Nyungar Nation; and on our Kalgoorlie campus, the Wongutha people of the North-Eastern Goldfields.