مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Persian Verion

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

video

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

sound

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Persian Version

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

View:

730
مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Download:

0
مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Cites:

Information Journal Paper

Title

THE EFFICIENCY OF SECRETION AND γ-CARBOXYLATION OF RECOMBINANT HUMAN FACTOR IX IN STABLE DROSOPHILA CELLS

Pages

  233-242

Abstract

 Background and Objectives: Human factor IX (hFIX) during maturation in the liver requires carboxylation of glutamic amino acids in the Gla domain, which is involved in its secretion and activity. Due to the deficiency of mammalian expression systems in the secretion and fully g_carboxylation of recombinant coagulation factors and higher activity of g_carboxylase enzyme in Drosophila S2 system, the present study was performed to evaluate ability of this system in g_carboxylation, secretion and activity of recombinant hFIX.Materials and Methods: In this study, following transfection of S2 cells with pMT-hFIX vector, the ELISA and aPTT tests were used to evaluate the expression and activity of recombinant hFIX. In addition, g_carboxylation of factor IX was approved by barium citrate precipitation. The samples were analyzed on three consecutive days and being repeated three times.Results The coagulation results showed the secretion of active recombinant hFIX by stable S2 cells. Quantitative assessment of recombinant hFIX in medium and cell lysis with ELISA showed 94% secretion efficiency. The results of ELISA on precipitated FIX with barium citrate also indicated that about 45% of secreted recombinant hFIX from S2cells are fully carboxylated.Conclusions: Activity and barium citrate precipitation of recombinant hFIX confirmed the ability of S2 cells, unlike other insect cells, in the g_carboxylation of factor IX. So, our results provide convincing evidence that Drosophila g_carboxylase perform necessary g_carboxylation required for secretion and coagulation activity of recombinant hFIX.

Cites

  • No record.
  • References

    Cite

    APA: Copy

    KHALILZADEH, S., & VATANDOOST, J.. (2016). THE EFFICIENCY OF SECRETION AND γ-CARBOXYLATION OF RECOMBINANT HUMAN FACTOR IX IN STABLE DROSOPHILA CELLS. THE SCIENTIFIC JOURNAL OF IRANIAN BLOOD TRANSFUSION ORGANIZATION (KHOON), 13(3), 233-242. SID. https://sid.ir/paper/78432/en

    Vancouver: Copy

    KHALILZADEH S., VATANDOOST J.. THE EFFICIENCY OF SECRETION AND γ-CARBOXYLATION OF RECOMBINANT HUMAN FACTOR IX IN STABLE DROSOPHILA CELLS. THE SCIENTIFIC JOURNAL OF IRANIAN BLOOD TRANSFUSION ORGANIZATION (KHOON)[Internet]. 2016;13(3):233-242. Available from: https://sid.ir/paper/78432/en

    IEEE: Copy

    S. KHALILZADEH, and J. VATANDOOST, “THE EFFICIENCY OF SECRETION AND γ-CARBOXYLATION OF RECOMBINANT HUMAN FACTOR IX IN STABLE DROSOPHILA CELLS,” THE SCIENTIFIC JOURNAL OF IRANIAN BLOOD TRANSFUSION ORGANIZATION (KHOON), vol. 13, no. 3, pp. 233–242, 2016, [Online]. Available: https://sid.ir/paper/78432/en

    Related Journal Papers

    Related Seminar Papers

  • No record.
  • Related Plans

  • No record.
  • Recommended Workshops






    Move to top
    telegram sharing button
    whatsapp sharing button
    linkedin sharing button
    twitter sharing button
    email sharing button
    email sharing button
    email sharing button
    sharethis sharing button