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Endocrinology Vol. 141, No. 3 1245-1253
Copyright © 2000 by The Endocrine Society

ARTICLES

HE2ß and HE2{gamma}, New Members of an Epididymis-Specific Family of Androgen-Regulated Proteins in the Human1

Katherine G. Hamil, P. Sivashanmugam, Richard T. Richardson, Gail Grossman, Steven M. Ruben, James L. Mohler, Peter Petrusz, Michael G. O’Rand, Frank S. French and Susan H. Hall

Departments of Pediatrics (K.G.H., F.S.F., S.H.H.), Cell Biology and Anatomy (P.S., R.T.R., G.G., P.P., M.G.O.), and Surgery (J.L.M.) and the Laboratories for Reproductive Biology (K.G.H., P.S., R.T.R., G.G., P.P., M.G.O., F.S.F., S.H.H.), University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599; and Human Genome Sciences, Inc. (S.M.R.), Rockville, Maryland 20850

Address all correspondence and requests for reprints to: Susan H. Hall, Laboratories for Reproductive Biology, CB 7500, 375 Medical Sciences Research Building, University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599-7500. E-mail: shh{at}med.unc.edu

HE2 is an epididymis-specific sperm-binding secretory protein. We isolated a family of HE2-related complementary DNAs from a human caput/corpus library. The transcripts code for identical 71-amino acid N-termini and different C-termini, and 5'- and 3'-untranslated regions. Compared with the original HE2, HE2ß and HE2{gamma} proteins have a 25-amino acid deletion near the C-terminus, and HE2{gamma} isoforms have a second deletion. These frame-shifting deletions result in C-termini differing in length, amino acid sequence, including number of cysteines, and isoelectric point. Identical sequences and deletion start and stop points indicate the HE2 isoforms are derived from alternative splicing of 8 or more exons of a single gene. Northern hybridization revealed that the 0.9-kb messenger RNA (mRNA) is most abundant in human caput; there is much less of it (20%) in corpus and little (<5%) in cauda. In castrated Macaca mulatta, HE2 mRNA decreased to 10% of sham-operated levels. Testosterone replacement maintained HE2 mRNA 3- to 5-fold higher than castrate levels, indicating its androgen dependence. Immunohistochemical staining revealed that the ß1 form is highly expressed in principal cells of the initial segment and caput. It is secreted into the lumen and binds to the sperm surface in the postacrosomal and neck regions. The ß2 form is expressed in principal cells primarily in efferent ducts.




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