Molecular and functional characterization of the rabbit epididymal secretory protein 52, REP52

Nixon, Brett, Jones, Russell C. and Holland, Michael K. (2008) Molecular and functional characterization of the rabbit epididymal secretory protein 52, REP52. Biology of Reproduction, 78 5: 910-920. doi:10.1095/biolreprod.107.065524

Author Nixon, Brett
Jones, Russell C.
Holland, Michael K.
Title Molecular and functional characterization of the rabbit epididymal secretory protein 52, REP52
Journal name Biology of Reproduction   Check publisher's open access policy
ISSN 0006-3363
Publication date 2008-05-01
Year available 2008
Sub-type Article (original research)
DOI 10.1095/biolreprod.107.065524
Volume 78
Issue 5
Start page 910
End page 920
Total pages 11
Place of publication Madison, WI, United States
Publisher Society for the Study of Reproduction
Language eng
Formatted 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.
Keyword Epididymis
Male reproductive tract
Sperm maturation
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Veterinary Science Publications
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Created: Mon, 15 Apr 2013, 14:42:25 EST by Dr Michael Holland on behalf of School of Veterinary Science