Reproductive and Developmental Biology

The Korean Society of Animal Reproduction (한국동물번식학회)
권호 표지
DOI QR코드

DOI QR Code

Expression of Sirt1, Sirt2, Sirt5, and Sirt6 in the Mouse Testis

  • Ki, Byeong Seong (Department of Biomedical Science, CHA University) ;
  • Park, Miree (Department of Biomedical Science, CHA University) ;
  • Woo, Yunmi (Department of Biomedical Science, CHA University) ;
  • Lee, Woo Sik (Department of Biomedical Science, CHA University) ;
  • Ko, Jung Jae (Department of Biomedical Science, CHA University) ;
  • Choi, Youngsok (Department of Biomedical Science, CHA University)
  • Received : 2015.05.15
  • Accepted : 2015.05.20
  • Published : 2015.06.30
Download PDF
⟨ Previous Next ⟩

Abstract

Sirtuin proteins are evolutionary conserved Sir2-related $NAD^+$-dependent deacetylases and regulate many of cellular processes such as metabolism, inflammation, transcription, and aging. Sirtuin contains activity of either ADP-ribosyltransferase or deacetyltranfease and their activity is dependent on the localization in cells. However, the expression pattern of Sirtuins has not been well studied. To examine the expression levels of Sirtuins, RT-PCR was performed using total RNAs from various tissues including liver, small intestine, heart, brain, kidney, lung, spleen, stomach, uterus, ovary, and testis. Sirtuins were highly expressed in most of tissues including the testis. Immunostaining assay showed that Sirt1 and Sirt6 were mainly located in the nucleus of germ cells, spermatocytes, and spermatids in the seminiferous tubules, whereas Sirt2 and Sirt5 were exclusively present in the cytoplasm of germ cells and spermatocytes. Our results indicate that Sirtuins may function as regulators of spermatogenesis and their activities might be dependent on their location in the seminiferous tubules.

Keywords

References

  1. Afshar G, Murnane JP (1999): Characterization of a human gene with sequence homology to Saccharomyces cerevisiae SIR2. Gene 234:161-168. https://doi.org/10.1016/S0378-1119(99)00162-6
  2. Coussens M, Maresh JG, Yanagimachi R, Maeda G, Allsopp R (2008): Sirt1 deficiency attenuates spermatogenesis and germ cell function. PLoS One 3: e1571. https://doi.org/10.1371/journal.pone.0001571
  3. de la Fuente R, Parra MT, Viera A, Calvente A, Gomez R, Suja JA, et al. (2007): Meiotic pairing and segregation of achiasmate sex chromosomes in eutherian mammals: the role of SYCP3 protein. PLoS Genet 3:e198. https://doi.org/10.1371/journal.pgen.0030198
  4. Flick F, Luscher B (2012): Regulation of sirtuin function by posttranslational modifications. Front Pharmacol 3:29.
  5. Galli M, Van Gool F, Leo O (2011): Sirtuins and inflammation: Friends or foes? Biochem Pharmacol 81:569-576. https://doi.org/10.1016/j.bcp.2010.12.010
  6. Kiran S, Chatterjee N, Singh S, Kaul SC, Wadhwa R, Ramakrishna G (2013): Intracellular distribution of human SIRT7 and mapping of the nuclear/ nucleolar localization signal. FEBS J 280:3451-3466. https://doi.org/10.1111/febs.12346
  7. Liszt G, Ford E, Kurtev M, Guarente L (2005): Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase. J Biol Chem 280:21313-21320. https://doi.org/10.1074/jbc.M413296200
  8. McBurney MW, Yang X, Jardine K, Hixon M, Boekelheide K, Webb JR, et al. (2003): The mammalian SIR2alpha protein has a role in embryogenesis and gametogenesis. Mol Cell Biol 23:38-54. https://doi.org/10.1128/MCB.23.1.38-54.2003
  9. Michishita E, Park JY, Burneskis JM, Barrett JC, Horikawa I (2005): Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol Biol Cell 16:4623-4635. https://doi.org/10.1091/mbc.E05-01-0033
  10. Mostoslavsky R, Chua KF, Lombard DB, Pang WW, Fischer MR, Gellon L, et al. (2006): Genomic instability and aging-like phenotype in the absence of mammalian SIRT6. Cell 124:315-329. https://doi.org/10.1016/j.cell.2005.11.044
  11. Moynihan KA, Grimm AA, Plueger MM, Bernal- Mizrachi E, Ford E, Cras-Meneur C, et al. (2005): Increased dosage of mammalian Sir2 in pancreatic beta cells enhances glucose-stimulated insulin secretion in mice. Cell Metab 2:105-117. https://doi.org/10.1016/j.cmet.2005.07.001
  12. Nakagawa T, Lomb DJ, Haigis MC, Guarente L (2009): SIRT5 Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle. Cell 137: 560-570. https://doi.org/10.1016/j.cell.2009.02.026
  13. Nakamura Y, Ogura M, Tanaka D, Inagaki N (2008): Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5. Biochem Biophys Res Commun 366:174-179. https://doi.org/10.1016/j.bbrc.2007.11.122
  14. Noce T, Okamoto-Ito S, Tsunekawa N (2001): Vasa homolog genes in mammalian germ cell development. Cell Struct Funct 26:131-136. https://doi.org/10.1247/csf.26.131
  15. North BJ, Marshall BL, Borra MT, Denu JM, Verdin E (2003): The human Sir2 ortholog, SIRT2, is an $NAD^+$-dependent tubulin deacetylase. Mol Cell 11: 437-444. https://doi.org/10.1016/S1097-2765(03)00038-8
  16. North BJ, Verdin E (2004): Sirtuins: Sir2-related NADdependent protein deacetylases. Genome Biol 5:224. https://doi.org/10.1186/gb-2004-5-5-224
  17. Perrod S, Cockell MM, Laroche T, Renauld H, Ducrest AL, Bonnard C, et al. (2001): A cytosolic NADdependent deacetylase, Hst2p, can modulate nucleolar and telomeric silencing in yeast. EMBO J 20:197-209. https://doi.org/10.1093/emboj/20.1.197
  18. Preyat N, Leo O (2013): Sirtuin deacylases: a molecular link between metabolism and immunity. J Leukoc Biol 93:669-680. https://doi.org/10.1189/jlb.1112557
  19. Sakamoto J, Miura T, Shimamoto K, Horio Y (2004): Predominant expression of Sir2alpha, an NAD-dependent histone deacetylase, in the embryonic mouse heart and brain. FEBS Lett 556:281-286. https://doi.org/10.1016/S0014-5793(03)01444-3
  20. Seifert EL, Caron AZ, Morin K, Coulombe J, He XH, Jardine K, et al. (2012): SirT1 catalytic activity is required for male fertility and metabolic homeostasis in mice. FASEB J 26:555-566. https://doi.org/10.1096/fj.11-193979
  21. Shoba B, Lwin ZM, Ling LS, Bay BH, Yip GW, Kumar SD (2009): Function of sirtuins in biological tissues. Anat Rec (Hoboken) 292:536-543. https://doi.org/10.1002/ar.20875
  22. Tanno M, Sakamoto J, Miura T, Shimamoto K, Horio Y (2007): Nucleocytoplasmic shuttling of the $NAD^+$-dependent histone deacetylase SIRT1. J Biol Chem 282:6823-6832. https://doi.org/10.1074/jbc.M609554200
  23. Taylor DM, Maxwell MM, Luthi-Carter R, Kazantsev AG (2008): Biological and potential therapeutic roles of sirtuin deacetylases. Cell Mol Life Sci 65: 4000-4018. https://doi.org/10.1007/s00018-008-8357-y
  24. Vaquero A, Scher M, Lee D, Erdjument-Bromage H, Tempst P, Reinberg D (2004): Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. Mol Cell 16:93-105. https://doi.org/10.1016/j.molcel.2004.08.031
  25. Wilson JM, Le VQ, Zimmerman C, Marmorstein R, Pillus L (2006): Nuclear export modulates the cytoplasmic Sir2 homologue Hst2. EMBO Rep 7:1247-1251. https://doi.org/10.1038/sj.embor.7400829