Russian Journal of Genetics

, Volume 54, Issue 3, pp 353–357 | Cite as

The First Report on Single Nucleotide Polymorphisms of the HSPA13 Gene in Koreans

Medical Genetics

Abstract

Heat shock proteins (HSPs) are known as molecular chaperones, and they function in response to cell stress. HSPA13, also called STCH, is a member of the HSP70 family. In general, HSP70 family may play a protective role in prion diseases. In a recent study, the overexpression of HSPA13 was shown to shorten the incubation time of prion diseases. Although the exact role of HSPA13 in the pathogenesis of prion diseases remains unknown, the expression level of HSPA13 is significantly associated with the latent phase of prion diseases. It has been known that single nucleotide polymorphisms (SNPs) in promoter and open reading frame (ORF) region of genes can affect either gene expression or gene function. The purpose of this study was to investigate genotype and allele frequencies of SNPs found in the promoter and ORF of HSPA13 in healthy Korean population to obtain the information for subsequent population genetics and prion diseases studies. We observed four SNPs in the promoter region of HSPA13, of which two have previous identified (c.-608C>G; rs2242662 and c.-381G>A; rs2242661) and two are novel (c.-321C>T and c.-300A>G). Interestingly, we did not observe any polymorphisms in the ORF of this gene. To our knowledge, this is the first study of polymorphisms in the human HSPA13 gene.

Keywords

HSPA13 heat shock protein single nucleotide polymorphism Korean population 

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References

  1. 1.
    Prusiner, S.B., Prions, Proc. Natl. Acad. Sci. U.S.A., 1998, vol. 95, no. 23, pp. 13363–13383.CrossRefPubMedPubMedCentralGoogle Scholar
  2. 2.
    Bratosiewicz-Wasik, J., Liberski, P.P., Golanska, E., et al., Regulatory sequences of the PRNP gene influence susceptibility to sporadic Creutzfeldt–Jakob disease, Neurosci. Lett., 2007, vol. 411, no. 3, pp. 163–167.CrossRefPubMedGoogle Scholar
  3. 3.
    Bratosiewicz-Wasik, J., Smolen-Dzirba, J., Watala, C., et al., Association of the PRNP regulatory region polymorphisms with the occurrence of sporadic Creutzfeldt–Jakob disease, Folia Neuropathol., 2012, vol. 50, no. 1, pp. 68–73.PubMedGoogle Scholar
  4. 4.
    Croes, E.A., Alizadeh, B.Z., Bertoli-Avella, A.M., et al., Polymorphisms in the prion protein gene and in the doppel gene increase susceptibility for Creutzfeldt—Jakob disease, Eur. J. Hum. Genet., 2004, vol. 12, no. 5, pp. 389–394.CrossRefPubMedGoogle Scholar
  5. 5.
    Jeong, B.H., Kim, N.H., Choi, E.K., et al., Polymorphism at 3' UTR +28 of the prion-like protein gene is associated with sporadic Creutzfeldt–Jakob disease, Eur. J. Hum. Genet., 2005, vol. 13, no. 9, pp. 1094–1097.CrossRefPubMedGoogle Scholar
  6. 6.
    Jeong, B.H., Lee, K.H., Lee, Y.J., et al., Absence of association between two HECTD2 polymorphisms and sporadic Creutzfeldt–Jakob disease, Dement. Geriatr. Cogn. Disord., 2011, vol. 31, no. 2, pp. 146–151.CrossRefPubMedGoogle Scholar
  7. 7.
    Jeong, B.H., Lee, K.H., Lee, Y.J., et al., Genetic association of a cathepsin D polymorphism and sporadic Creutzfeldt–Jakob disease, Dement. Geriatr. Cogn. Disord., 2009, vol. 28, no. 4, pp. 302–306.CrossRefPubMedGoogle Scholar
  8. 8.
    Jeong, B.H., Jin, H.T., Choi, E.K., Carp, R.I., and Kim, Y.S., Lack of association between 14-3-3 beta gene (YWHAB) polymorphisms and sporadic Creutzfeldt–Jakob disease (CJD), Mol. Biol. Rep., 2012, vol. 39, no. 12, pp. 10647–10653.CrossRefPubMedGoogle Scholar
  9. 9.
    Jeong, B.H., Kim, H.J., Lee, K.H., et al., RARB and STMN2 polymorphisms are not associated with sporadic Creutzfeldt–Jakob disease (CJD) in the Korean population, Mol. Biol. Rep., 2014, vol. 41, no. 4, pp. 2389–2395.CrossRefPubMedGoogle Scholar
  10. 10.
    Czarnik, U., Grzybowski, G., Zabolewicz, T., et al., Deletion/insertion polymorphism of the prion protein gene (PRNP) in Polish red cattle, Polish White-backed cattle and European bison (Bison bonasus L., 1758), Russ. J. Genet., 2009, vol. 45, no. 4, pp. 519–525.CrossRefGoogle Scholar
  11. 11.
    Zhang, Y., Casas-Tinto, S., Rincon-Limas, D.E., and Fernandez-Funez, P., Combined pharmacological induction of Hsp70 suppresses prion protein neurotoxicity in Drosophila, PLoS One, 2014, vol. 9, no. 2. e88522CrossRefPubMedPubMedCentralGoogle Scholar
  12. 12.
    Mazina, M.Y., Nikolenko, Y.V., Krasnov, A.N., and Vorobyeva, N.E., SWI/SNF protein complexes participate in the initiation and elongation stages of Drosophila hsp70 gene transcription, Russ. J. Genet., 2016, vol. 52, no. 2, pp. 164–169.CrossRefGoogle Scholar
  13. 13.
    Zhang, J., Wang, K., Guo, Y., et al., Heat shock protein 70 selectively mediates the degradation of cytosolic PrPs and restores the cytosolic PrP-induced cytotoxicity via a molecular interaction, Virol. J., 2012, vol. 9, p. 303.CrossRefPubMedPubMedCentralGoogle Scholar
  14. 14.
    Soo, E.T., Ng, Y.K., Bay, B.H., and Yip, G.W., Heat shock proteins and neurodegenerative disorders, Sci._World J., 2008, vol. 8, pp. 270–274.CrossRefGoogle Scholar
  15. 15.
    Fernandez-Funez, P., Casas-Tinto, S., Zhang, Y., et al., In vivo generation of neurotoxic prion protein: role for hsp70 in accumulation of misfolded isoforms, PLoS Genet., 2009, vol. 5, no. 6. e1000507CrossRefPubMedPubMedCentralGoogle Scholar
  16. 16.
    Grizenkova, J., Akhtar, S., Hummerich, H., et al., Overexpression of the Hspa13 (Stch) gene reduces prion disease incubation time in mice, Proc. Natl. Acad. Sci. U.S.A., 2012, vol. 109, no. 34, pp. 13722–13727.CrossRefPubMedPubMedCentralGoogle Scholar
  17. 17.
    Brodsky, G., Otterson, G.A., Parry, B.B., et al., Localization of STCH to human chromosome 21q11.1, Genomics, 1995, vol. 30, no. 3, pp. 627–628.CrossRefPubMedGoogle Scholar
  18. 18.
    Kampinga, H.H., Hageman, J., Vos, M.J., et al., Guidelines for the nomenclature of the human heat shock proteins, Cell Stress Chaperones, 2009, vol. 14, no. 1, pp. 105–111.CrossRefPubMedGoogle Scholar
  19. 19.
    Verbenko, V.N., Kuznetsova, L.V., Luchkina, L.A., and Klonov, N.V., Mutation in the cspH-cspG gene cluster enhances expression of heat-shock proteins and SOS repair system of Escherichia coli, Russ. J. Genet., 2009, vol. 45, no. 9, pp. 1194–1202.CrossRefGoogle Scholar
  20. 20.
    Galkin, A.P., Mironova, L.N., Zhuravleva, G.A., and Inge-Vechtomov, S.G., Yeast prions, mammalian amyloidoses, and the problem of proteomic networks, Russ. J. Genet., 2006, vol. 42, no. 11, pp. 1558–1570.CrossRefGoogle Scholar
  21. 21.
    Nizhnikov, A.A., Kondrashkina, A.M., and Galkin, A.P., Interactions of [NSI+] determinant with SUP35 and VTS1 genes in Saccharomyces cerevisiae, Russ. J. Genet., 2013, vol. 49, no. 10, pp. 1155–1164.CrossRefGoogle Scholar
  22. 22.
    Otterson, G.A. and Kaye, F.J., A “core ATPase,” Hsp70-like structure is conserved in human, rat, and C. elegans STCH proteins, Gene, 1997, vol. 199, pp. 287–292.CrossRefPubMedGoogle Scholar

Copyright information

© Pleiades Publishing, Inc. 2018

Authors and Affiliations

  1. 1.Korea Zoonosis Research InstituteChonbuk National UniversityIksanRepublic of Korea
  2. 2.Department of Bioactive Material SciencesChonbuk National UniversityJeonjuRepublic of Korea

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