Biol Reprod
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Roberts, K. P.
Right arrow Articles by Hamilton, D. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Roberts, K. P.
Right arrow Articles by Hamilton, D. W.
Agricola
Right arrow Articles by Roberts, K. P.
Right arrow Articles by Hamilton, D. W.
Biology of Reproduction 67, 525-533 (2002)
© 2002 Society for the Study of Reproduction, Inc.


Regular Article

A Comparative Analysis of Expression and Processing of the Rat Epididymal Fluid and Sperm-Bound Forms of Proteins D and E1

Kenneth P. Robertsb, Kathy M. Ensruda, and David W. Hamilton2,,a

a Department of Genetics, Cell Biology, and Development and the b Department of Urologic Surgery, University of Minnesota, Minneapolis, Minnesota 55455

The mammalian epididymis secretes numerous proteins important for sperm maturation. Among these are proteins D and E, which belong to the CRISP family (cysteine-rich secretory proteins) and are the product of the Crisp-1 gene. These proteins have been the focus of a number of studies and have been implicated in sperm/egg fusion. Protein D and protein E have been purified to apparent homogeneity in several laboratories. Polyclonal antibodies raised against each protein typically cross-reacted with both proteins, suggesting that they were immunologically similar, if not identical. Our laboratory has previously reported the generation of a monoclonal antibody (mAb 4E9) that recognizes only protein E. Using mAb 4E9, the localization of protein E was shown to be domain specific on the sperm surface and there is processing of the protein in the fluid, with only the lowest molecular weight form associating with sperm. Subsequent purification and amino acid sequencing of protein D confirmed that proteins D and E are nearly identical and differ only by presence of the 4E9 epitope on protein E. Here we report the generation of antibodies to regions of amino acid sequence identity in proteins D and E. Using these antibodies, we demonstrate that protein D associates with the sperm head and that a portion of this protein may be proteolytically processed. In addition, we demonstrate that the proteolytic processing of protein E occurs in the carboxy terminal region of this protein. The data also suggest that a portion of protein D may also undergo processing, similar to that of protein E. Finally, we use these antibodies to demonstrate that proteins D and E are differentially expressed by the epididymal epithelium. Taken together, these data suggest that proteins D and E may have individual roles in sperm function.

First decision: 29 January 2002.

1 Supported by National Institutes of Health grant HD-11962.

2 Correspondence: David W. Hamilton, Department of Genetics, Cell Biology, and Development, University of Minnesota, 6-160 Jackson Hall, 321 Church Street S.E., Minneapolis, MN 55455. FAX: 612 626 7431; dwh{at}umn.edu




This article has been cited by other articles:


Home page
ReproductionHome page
D. Jamsai, D. M Bianco, S. J Smith, D. J Merriner, J. D Ly-Huynh, A. Herlihy, B. Niranjan, G. M Gibbs, and M. K O'Bryan
Characterization of gametogenetin 1 (GGN1) and its potential role in male fertility through the interaction with the ion channel regulator, cysteine-rich secretory protein 2 (CRISP2) in the sperm tail
Reproduction, June 1, 2008; 135(6): 751 - 759.
[Abstract] [Full Text] [PDF]


Home page
Biol. Reprod.Home page
M. A. Nolan, L. Wu, H. J. Bang, S. A. Jelinsky, K. P. Roberts, T. T. Turner, G. S. Kopf, and D. S. Johnston
Identification of Rat Cysteine-Rich Secretory Protein 4 (Crisp4) as the Ortholog to Human CRISP1 and Mouse Crisp4
Biol Reprod, May 1, 2006; 74(5): 984 - 991.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. Guo, M. Teng, L. Niu, Q. Liu, Q. Huang, and Q. Hao
Crystal Structure of the Cysteine-rich Secretory Protein Stecrisp Reveals That the Cysteine-rich Domain Has a K+ Channel Inhibitor-like Fold
J. Biol. Chem., April 1, 2005; 280(13): 12405 - 12412.
[Abstract] [Full Text] [PDF]


Home page
Biol. Reprod.Home page
K. P. Roberts, J. A. Wamstad, K. M. Ensrud, and D. W. Hamilton
Inhibition of Capacitation-Associated Tyrosine Phosphorylation Signaling in Rat Sperm by Epididymal Protein Crisp-1
Biol Reprod, August 1, 2003; 69(2): 572 - 581.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2002 by the Society for the Study of Reproduction.