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a Department of Dairy and Animal Science, J.O. Almquist Research Center, Pennsylvania State University, University Park, Pennsylvania 16802
b Department of Molecular Behavioral Biology, Osaka Bioscience Institute, Osaka 565, Japan
c PRESTO, Japan Science and Technology Corporation, Osaka 565, Japan
Previously, we identified a 26-kDa fertility-associated protein in bull seminal plasma as lipocalin-type prostaglandin D synthase. The objective of the present study was to immunohistochemically localize this enzyme to the various cell types within the bull testis and seven subsegments of the epididymis, and on ejaculated sperm in order to gain further insight into its potential function in male reproduction. In the testis, immunoperoxidase staining was localized within the elongating spermatids and Sertoli cells of the seminiferous tubules, varying with the stage of the spermatogenic cycle. The highest level of staining occurred during stages III–VII. The cuboidal epithelial cells of the rete testis and efferent ducts were also immunoreactive. Expression of lipocalin-type prostaglandin D synthase was not uniform in the seven epididymal subsegments, suggesting a possible role in sperm maturation. In all epididymal regions, expression was limited to the epithelial principal cells; no immunoreactivity was apparent in other cell types. Lipocalin-type prostaglandin D synthase was strikingly localized in the caput epididymidis, while moderate to weak staining was observed in the remainder of the epididymis. Droplets of reaction product observed within the lumen increased progressively from the caput to cauda. Using fluorescence microscopy, we also localized lipocalin-type prostaglandin D synthase to the apical ridge of the acrosome on ejaculated sperm.
1 This research was supported by a fellowship from the Japan Society for the Promotion of Science (R.L.G.) and USDA grants #93-37203-9069 and #97-35203-4806 (G.J.K.); in part by the Grants-in-Aid for Scientific Research Program of the Ministry of Education, Science and Culture of Japan (07558108 and 07457033 to Y.U.); and by grants from the Sankyo Foundation and the Cell and Science Foundation (Y.U.).
2 Correspondence: Gary J. Killian, J.O. Almquist Research Center, Fox Hollow Road, The Pennsylvania State University, University Park, PA 16802. FAX: 814 863 0833; lwj{at}psu.edu
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