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BOR - Papers in Press, published online ahead of print December 8, 2004.
Biol Reprod 2004, 10.1095/biolreprod.104.033753
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BIOLOGY OF REPRODUCTION 72, 879–889 (2005)
DOI: 10.1095/biolreprod.104.033753
© 2005 by the Society for the Study of Reproduction, Inc.

The Mouse Germ-Cell-Specific Leucine-Rich Repeat Protein NALP14: A Member of the NACHT Nucleoside Triphosphatase Family1

Michiharu Horikawa3,, Nikki J. Kirkman, Kelley E. Mayo4,, Sabine M. Mulders5,, Jian Zhou6,, Carolyn A. Bondy6,, Sheau-Yu Teddy Hsu7,, Gretchen J. King, and Eli Y. Adashi2,

Division of Reproductive Sciences, Department of Obstetrics and Gynecology, University of Utah Health Sciences Center, Salt Lake City, Utah 84112

Microscopy of sectioned neonatal mouse ovaries established the predominance of primordial follicles in Day 3 samples and the predominance of primary follicles by Day 8. To identify genetic determinants of the primordial to primary follicle transition, the transcriptome of Day 1 or Day 3 mouse ovaries was contrasted by differential display with that of Day 8 ovaries. This manuscript examines one of the up-regulated genes, the novel Nalp14 gene, whose transcript displayed 18- and 127-fold increments from Day 1 to Days 3 and 8, respectively. First noted by in situ hybridization in oocytes encased by primary follicles, Nalp14 transcripts were continuously expressed through the preovulatory stage. The transcripts declined when meiotic maturation resumed, and they were markedly diminished by the 2-cell embryo stage. The corresponding 3281-base pair, full-length cDNA coded for a 993 residue/104.6-kDa germ cell-specific protein. A member of the multifunctional NACHT NTPase family, the NALP14 protein featured 14 iterations of the leucine-rich-repeat domain, a region implicated in protein-protein interaction. Protein BLAST analysis of the NALP14 sequence revealed 2 previously reported germ cell-specific homologs (i.e., MATER [Maternal Antigen That Embryos Require], RNH2 [RiboNuclease/Angiogenin Inhibitor 2], and NALP4c). The structural attributes, expression pattern, and cellular localization of MATER and RNH2 largely conformed to those reported for NALP14.

1 E.Y.A. was supported in part by grants HD30288 and HD37845 from the National Institutes of Health.

2 Correspondence: Eli Y. Adashi, Department of Obstetrics and Gynecology, University of Utah Health Sciences Center, Salt Lake City, UT 84112. FAX: 801 585 9295; eadashi{at}hsc.utah.edu

3 Current address: Department of Obstetrics and Gynecology, Asahikawa Medical College, Midorigaoka Higashi 2-1-1-1, Asahikawa 078-8510, Japan

4 Current address: Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, 2205 Tech Drive, Evanston, IL 60208

5 Current address: Organon, Kloosterstraat 6, 5349 AB Oss, The Netherlands

6 Current address: Developmental Endocrinology Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD

7 Current address: Department of Gynecology and Obstetrics, Stanford University School of Medicine, 300 Pasteur Drive, Room A344, Stanford, CA 4305-5317




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