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BOR - Papers in Press, published online ahead of print January 16, 2008.
Biol Reprod 2008, 10.1095/biolreprod.107.065524
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BIOLOGY OF REPRODUCTION 78, 910–920 (2008)
DOI: 10.1095/biolreprod.107.065524
© 2008 by the Society for the Study of Reproduction, Inc.

research-article

Molecular and Functional Characterization of the Rabbit Epididymal Secretory Protein 52, REP521

Brett Nixon 2 3, Russell C. Jones 3, and Michael K. Holland 4

School of Environmental and Life Sciences,3 Discipline of Biological Sciences, University of Newcastle, Callaghan, New South Wales 2308, Australia Centre for Early Human Development,4 Monash Institute of Reproduction and Development, Clayton, Victoria 3168, Australia

ABSTRACT

As part of a systematic study of rabbit epididymal proteins involved in sperm maturation, we have identified and characterized a novel glycoprotein (rabbit epididymal secretory protein 52 [REP52]) of 52 kDa. REP52 is synthesized and secreted in a tissue-specific manner by the mid (region 6) and distal (region 7) corpus epididymidis and associates weakly with the sperm surface overlying the principal piece of the tail. Sequencing of cloned REP52 cDNA demonstrated that this protein represents a novel member of the highly conserved fibronectin type II (FN2) module protein family. The protein appears related but not homologous to ungulate seminal plasma proteins and is the first known example to be identified as a rabbit epididymal secretory protein. Consistent with other members of this protein family, REP52 possessed a high level of sequence identity within the FN2 module-encoding domains, but a highly variable N-terminal sequence that failed to show significant homology with published sequences. By analogy with evidence from studies of the ungulate seminal plasma proteins it is hypothesized that the tandemly arranged FN2 modules could facilitate the association of REP52 with sperm phosphatidylcholine residues on the outer leaflet of the sperm tail. It is also considered likely that these domains represent key elements for the function of this novel protein, a conclusion supported by the fact that antisera raised against the REP52 protein blocked in vitro fertilization in a concentration-dependent fashion.

epididymis, male reproductive tract, sperm maturation

FOOTNOTES

1Supported by a grant from the Australian Research Council, the Research Management Committee, University of Newcastle, and the Pest Animal Control Cooperative Research Centre, Canberra, Australia.

Correspondence: 2Brett Nixon, School of Environmental and Life Sciences, Discipline of Biological Sciences, University of Newcastle, University Dr., Callaghan, NSW 2308, Australia. FAX: 61 2 4921 6308; e-mail: Brett.Nixon{at}newcastle.edu.au






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Copyright © 2008 by the Society for the Study of Reproduction.