Skip to main content
Springer Nature Link
Log in
Menu
Find a journal Publish with us Track your research
Search
Cart
  1. Home
  2. Chinese Science Bulletin
  3. Article

Comparative study of the promotion of porcine fetal fibroblast proliferation by overexpression of two transcriptional variants of SIRT6

  • Article
  • Cell Biology
  • Open access
  • Published: 23 March 2013
  • Volume 58, pages 1169–1174, (2013)
  • Cite this article
Download PDF

You have full access to this open access article

Chinese Science Bulletin
Comparative study of the promotion of porcine fetal fibroblast proliferation by overexpression of two transcriptional variants of SIRT6
Download PDF
  • XiaoXian Xie1,2,
  • Kan He1,
  • AiLing Zhang2,3,
  • Hao Zhang2,3,
  • QiShan Wang1,
  • JiaQi Li2,3 &
  • …
  • YuFang Ma1 
  • 657 Accesses

  • Explore all metrics

Abstract

Mammalian Sirtuin 6 (SIRT6) plays an important role in the transcriptional silencing of silent mating-type loci, telomeres, and rDNA. However, the roles of porcine SIRT6 in cell proliferation are poorly understood, and a better knowledge of these will help improve our understanding of the biological mechanisms of cell growth and development. In this study, a novel variant of porcine SIRT6 (SIRT6 V2) identified by reverse transcription-polymerase chain reaction and BLAST analysis showed a 124-bp deletion compared to wild-type SIRT6 mRNA (SIRT6 V1). Two recombinant plasmids overexpressing SIRT6 V1 and SIRT6 V2 were produced and their roles in the proliferation of porcine fetal fibroblasts (PFFs) were compared. Cells transfected with SIRT6 V1 proliferated significantly faster than those transfected with SIRT6 V2 (P<0.01), though both proliferated significantly faster than cells expressing an empty vector (P<0.01). These results might be caused by altered proportions of α helices and β sheets in the SIRT6 V2 structure relative to SIRT6 V1. These results indicate that overexpression of SIRT6 V1/V2 was involved in promoting PFF proliferation. Deletion of a 124-bp sequence attenuated the effects of SIRT6 on cell proliferation, possibly as a result of changes in the proportions of α helices and β sheets in the protein secondary structure.

Article PDF

Download to read the full article text

Similar content being viewed by others

Recombinant human SIRT1 protects against nutrient deprivation-induced mitochondrial apoptosis through autophagy induction in human intervertebral disc nucleus pulposus cells

Article Open access 15 September 2015

Inhibition of cell invasion and migration by targeting matrix metalloproteinase-9 expression via sirtuin 6 silencing in human breast cancer cells

Article Open access 15 July 2022

SIRT6 polymorphism rs117385980 is associated with longevity and healthy aging in Finnish men

Article Open access 11 April 2017

Explore related subjects

Discover the latest articles, books and news in related subjects, suggested using machine learning.
  • Cellular Senescence
  • Cell growth
  • Cell Proliferation
  • Embryonic Stem Cells
  • siRNAs
  • Telomeres
Use our pre-submission checklist

Avoid common mistakes on your manuscript.

References

  1. Landry J, Sutton A, Tafrov S T, et al. The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases. Proc Natl Acad Sci USA, 2000, 97: 5807–5811

    Article  Google Scholar 

  2. Kaeberlein M, McVey M, Guarente L. The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev, 1999, 13: 2570–2580

    Article  Google Scholar 

  3. Moazed D. Enzymatic activities of Sir2 and chromatin silencing. Curr Opin Cell Biol, 2001, 13: 232–238

    Article  Google Scholar 

  4. Liszt G, Ford E, Kurtev M, et al. Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase. J Biol Chem, 2005, 280: 21313–21320

    Article  Google Scholar 

  5. Michishita E, Park J Y, Burneskis J M, et al. Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol Biol Cell, 2005, 16: 4623–4635

    Article  Google Scholar 

  6. Du J, Jiang H, Lin H. Investigating the ADP-ribosyltransferase activity of sirtuins with nad analogues and 32P-NAD. Biochemistry, 2009, 48: 2878–2890

    Article  Google Scholar 

  7. Mostoslavsky R, Chua K F, Lombard D B, et al. Genomic instability and ageing-like phenotype in the absence of mammalian SIRT6. Cell, 2006, 124: 315–329

    Article  Google Scholar 

  8. Kawahara T L, Michishita E, Adler A S, et al. SIRT6 links histone H3 lysine 9 deacetylation to NF-kappaB-dependent gene expression and organismal life span. Cell, 2009, 136: 62–74

    Article  Google Scholar 

  9. Michishita E, McCord R A, Berber E, et al. SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin. Nature, 2008, 452: 492–496

    Article  Google Scholar 

  10. Zhong L, D’Urso A, Toiber D, et al. The histone deacetylase Sirt6 regulates glucose homeostasis via Hif1alpha. Cell, 2010, 140: 280–293

    Article  Google Scholar 

  11. Tennen R I, Berber E, Chua K F. Functional dissection of SIRT6: Identification of domains that regulate histone deacetylase activity and chromatin localization. Mech Ageing Dev, 2010, 131: 185–192

    Article  Google Scholar 

  12. Frye R A. Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem Biophys Res Commun, 1999, 260: 273–279

    Article  Google Scholar 

  13. Michishita E, McCord R A, Boxer L D, et al. Cell cycle-dependent deacetylation of telomeric histone H3 lysine K56 by human SIRT6. Cell Cycle, 2009, 8: 2664–2666

    Article  Google Scholar 

  14. Lombard D B, Schwer B, Alt F W, et al. SIRT6 in DNA repair, metabolism and ageing. J Intern Med, 2008, 263: 128–141

    Article  Google Scholar 

  15. Boquest A C, Day B N, Prather R S. Flow cytometric cell cycle analysis of cultured porcine fetal fibroblast cells. Biol Reprod, 1999, 60: 1013–1019

    Article  Google Scholar 

  16. Wang M H, Long M, Zhu B Y, et al. Effects of sargentgloryvine stem extracts on HepG-2 cells in vitro and in vivo. World J Gastroentero, 2011, 17: 2848

    Google Scholar 

  17. Schmittgen T D, Livak K J. Analyzing real-time PCR data by the comparative CT method. Nat Protoc, 2008, 3: 1101–1108

    Article  Google Scholar 

  18. Trog D, Moenkemann H, Haertel N, et al. Expression of ABC-1 transporter is elevated in human glioma cells under irradiation and temozolomide treatment. Amino Acids, 2005, 28: 213–219

    Article  Google Scholar 

  19. Blander G, Bhimavarapu A, Mammone T, et al. SIRT1 promotes differentiation of normal human keratinocytes. J Mol Biol, 2008, 129: 41–49

    Google Scholar 

  20. Kelley L A, Sternberg M. Protein structure prediction on the Web: A case study using the Phyre server. Nat Protoc, 2009, 4: 363–371

    Article  Google Scholar 

  21. Garnier J, Osguthorpe D, Robson B. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J Mol Biol, 1978, 120: 97–120

    Article  Google Scholar 

  22. Jin D, Tan H J, Lei T, et al. Molecular cloning and characterization of porcine sirtuin genes. Comp Biochem Physiol B Biochem Mol Biol, 2009, 153: 348–358

    Article  Google Scholar 

  23. Kanfi Y, Shalman R, Peshti V, et al. Regulation of SIRT6 protein levels by nutrient availability. FEBS Lett, 2008, 582: 543–548

    Article  Google Scholar 

  24. Branden C, Tooze J. Introduction to Protein Structure. New York: Garland Pub. Inc., 1998

    Google Scholar 

  25. Berman H M, Goodsell D S, Bourne P. Protein structures: From famine to feast. Am Sci, 2002, 90: 350

    Google Scholar 

  26. Kim P S, Baldwin R L. Intermediates in the folding reactions of small proteins. Annu Rev Biochem, 1990, 59: 631–660

    Article  Google Scholar 

  27. Karplus M, Weaver D L. Protein folding dynamics: The diffusion-collision model and experimental data. Protein Sci, 1994, 3: 650–668

    Article  Google Scholar 

  28. Sosnick T R, Jackson S, Wilk R R, et al. The role of helix formation in the folding of a fully alpha-helical coiled coil. Proteins, 1996, 24: 427–432

    Article  Google Scholar 

  29. Kim D E, Yi Q, Gladwin S T, et al. The single helix in protein L is largely disrupted at the rate-limiting step in folding. J Mol Biol, 1998, 284: 807–815

    Article  Google Scholar 

  30. Deechongkit S, Nguyen H, Jager M, et al. Beta-Sheet folding mechanisms from perturbation energetics. Curr Opin Struc Biol, 2006, 16: 94–101

    Article  Google Scholar 

  31. Zimmerman J. Enzyme kinetics and mechanism. Biochem Mol Biol Edu, 2007, 35: 386–388

    Article  Google Scholar 

  32. Rabinovich M, Melnick M, Bolobova A. The structure and mechanism of action of cellulolytic enzymes. Biochem (Moscow), 2002, 67: 850–871

    Article  Google Scholar 

  33. Page M, Di Cera E. Serine peptidases: Classification, structure and function. Cell Mol Life Sci, 2008, 65: 1220–1236

    Article  Google Scholar 

  34. Price N C. What is meant by ‘competitive inhibition’? Trends Biochem Sci, 1979, 4: N272–N273

    Article  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. School of Agriculture and Biology, Department of Animal Sciences, Shanghai Jiao Tong University, Shanghai Key Laboratory of Veterinary Biotechnology, Shanghai, 200240, China

    XiaoXian Xie, Kan He, QiShan Wang & YuFang Ma

  2. Department of Animal Genetics, Breeding and Reproduction, College of Animal Sciences, South China Agricultural University, Guangzhou, 510642, China

    XiaoXian Xie, AiLing Zhang, Hao Zhang & JiaQi Li

  3. Guangdong Provincial Key Laboratory of Agroanimal Genomics and Molecular Breeding, College of Animal Sciences, South China Agricultural University, Guangzhou, 510642, China

    AiLing Zhang, Hao Zhang & JiaQi Li

Authors
  1. XiaoXian Xie
    View author publications

    Search author on:PubMed Google Scholar

  2. Kan He
    View author publications

    Search author on:PubMed Google Scholar

  3. AiLing Zhang
    View author publications

    Search author on:PubMed Google Scholar

  4. Hao Zhang
    View author publications

    Search author on:PubMed Google Scholar

  5. QiShan Wang
    View author publications

    Search author on:PubMed Google Scholar

  6. JiaQi Li
    View author publications

    Search author on:PubMed Google Scholar

  7. YuFang Ma
    View author publications

    Search author on:PubMed Google Scholar

Corresponding author

Correspondence to YuFang Ma.

Additional information

This article is published with open access at Springerlink.com

Rights and permissions

This article is published under an open access license. Please check the 'Copyright Information' section either on this page or in the PDF for details of this license and what re-use is permitted. If your intended use exceeds what is permitted by the license or if you are unable to locate the licence and re-use information, please contact the Rights and Permissions team.

About this article

Cite this article

Xie, X., He, K., Zhang, A. et al. Comparative study of the promotion of porcine fetal fibroblast proliferation by overexpression of two transcriptional variants of SIRT6 . Chin. Sci. Bull. 58, 1169–1174 (2013). https://doi.org/10.1007/s11434-013-5706-5

Download citation

  • Received: 21 May 2012

  • Accepted: 28 September 2012

  • Published: 23 March 2013

  • Issue Date: April 2013

  • DOI: https://doi.org/10.1007/s11434-013-5706-5

Share this article

Anyone you share the following link with will be able to read this content:

Sorry, a shareable link is not currently available for this article.

Provided by the Springer Nature SharedIt content-sharing initiative

Keywords

  • SIRT6 variant
  • overexpression
  • porcine fetal fibroblast
  • proliferation
  • prediction assay
Use our pre-submission checklist

Avoid common mistakes on your manuscript.

Advertisement

Search

Navigation

  • Find a journal
  • Publish with us
  • Track your research

Discover content

  • Journals A-Z
  • Books A-Z

Publish with us

  • Journal finder
  • Publish your research
  • Language editing
  • Open access publishing

Products and services

  • Our products
  • Librarians
  • Societies
  • Partners and advertisers

Our brands

  • Springer
  • Nature Portfolio
  • BMC
  • Palgrave Macmillan
  • Apress
  • Discover
  • Your US state privacy rights
  • Accessibility statement
  • Terms and conditions
  • Privacy policy
  • Help and support
  • Legal notice
  • Cancel contracts here

152.53.39.118

Not affiliated

Springer Nature

© 2025 Springer Nature