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Identification of a Novel Testis-Specific Leucine-Rich Protein in Humans and Mice¹

^a Department of Biochemistry, Molecular Biology & Cell Biology, Northwestern University, Evanston, Illinois 60208

A novel testis-specific protein, termed LRTP, was identified by screening both human and mouse testis and mouse pachytene spermatocyte cDNA libraries. Sequence analyses (GenBank accession number: AF092208) revealed that LRTP contains an amino terminus leucine-rich repeat domain. There are several acidic regions rich in glutamic acid in the C-terminus. The sequence, by GenBank search, shows similarities to LANP and SDS22+, leucine-rich repeat proteins localized to the nucleus and involved in the regulation of protein phosphatases. In mouse, the mRNA is first detected at about Day 14 postpartum, presumably when mid-pachytene spermatocytes are first seen. In situ hybridization confirmed the expression of the LRTP mRNA at this stage of spermatogenesis. Immunohistochemical analysis revealed that the protein is most abundant in the cytoplasm of pachytene and diplotene cells, corresponding to late prophase of meiosis I. Immunohistochemical localization is markedly reduced in secondary spermatocytes, suggesting a functional association of LRTP with meiosis. An LRTP cDNA probe did not bind to mouse ovary RNA in a dot blot assay.

First decision: 11 October 1999.

¹ This work was supported by NICHD Sub-5-U54-HD29099 and by P30 HD28048.

² Correspondence: Erwin Goldberg, Department of Biochemistry, Molecular Biology & Cell Biology, Northwestern University, 2153 North Campus Drive, Evanston, IL 60208. FAX: 847 467 1380; erv{at}nwu.edu

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