Home  |   Archive  |   Online Submission  |   News & Events  |   Subscribe  |   APFA  |   Society  |   Contact Us  |   中文版
Search   
 
Journal

-Ahead of print
-Authors' Accepted
    Manuscripts
new!
-Current Issue
-Archive
-Acknowledgments
-Special Issues
-Browse by Category

Manuscript Submission

-Online Submission
-Online Review
-Instruction for Authors
-Instruction for Reviewers
-English Corner new!

About AJA

-About AJA
-Editorial Board
-Contact Us
-News

Resources & Services

-Advertisement
-Subscription
-Email alert
-Proceedings
-Reprints

Download area

-Copyright licence
-EndNote style file
-Manuscript word template
-Guidance for AJA figures
    preparation (in English)

-Guidance for AJA figures
    preparation (in Chinese)

-Proof-reading for the
    authors

-AJA Club (in English)
-AJA Club (in Chinese)

 
Abstract

Volume 6, Issue 1 (March 2004) 6, 3–13;

Recombinant human zona pellucida proteins ZP1, ZP2 and ZP3 co-expressed in a human cell line

M. Martic, E.K. Moses, T. E. Adams, D. Y. Liu, D. A. Gook, C. Garrett, M. E. Dunlop, G. H.W. Baker

Department of Obstetrics and Gynaecology, 2Department of Medicine, University of Melbourne, 3Pregnancy Research Center Royal Women's Hospital, 4Reproductive Services, Royal Women's Hospital and Melbourne IVF, 5CSIRO Division of Health Science and Nutrition, Melbourne, Australia
    

Advance online publication 1 March 2004

Abstract

Aim: To produce biologically active recombinant human (rh) ZP proteins in a human cell for use in sperm function tests. Methods: The human embryonic kidney cell line 293T was employed to produce rhZP1, rhZP2 and rhZP3 proteins individually and together by co-expression. Presence of these proteins in the culture medium and cell lysate was assessed by Western blotting analysis. The effect of the recombinant proteins on the human AR was assessed. Results: RhZP2 and rhZP3 were secreted into the culture medium, whereas rhZP1 was found only in the cell lysate. Interestingly, when all zona pellucida proteins were co-expressed in the same cells, rhZP1 was also secreted into the culture medium. However, despite the presence of all three ZP proteins in sufficient concentration and evidence of heavy glycosylation on gel electrophoresis, biological activity to induce the AR was not observed. Conclusion: RhZP1, rhZP2 and rhZP3 were successfully expressed in the human embryonic kidney cell line 293T. It appears that an interaction amongst these proteins may be required for release of rhZP1 from the cell. Although this approach is not satisfactory for producing active human ZP proteins, it makes a significant contribution to the understanding of the structural and functional characteristics of the ZP proteins.
    
    

Full Text |

 
Browse:  3552
 
Asian Journal of Andrology CN 31-1795/R ISSN 1008-682X  Copyright © 2023  Shanghai Materia Medica, Chinese Academy of Sciences.  All rights reserved.