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Amino Acids

, Volume 50, Issue 12, pp 1769–1773 | Cite as

PGC1α regulates ACMSD expression through cooperation with HNF4α

  • Manami Koshiguchi
  • Shizuka Hirai
  • Yukari EgashiraEmail author
Short Communication
  • 408 Downloads

Abstract

ACMSD is a tryptophan metabolic key enzyme. HNF4α regulates the transcription of some energy-metabolic enzymes by cooperating with PGC1α, a major transcriptional co-regulator involved in energy metabolism. In this study, we investigated the involvement of PGC1α in Acmsd expression through cooperation with HNF4α. Luciferase reporter assay was performed in NIH3T3 cells using a reporter vector containing HNF4α responsive elements in the Acmsd 5′ upstream transcriptional regulatory region together with HNF4α and/or PGC1α expression vectors. The Acmsd luciferase reporter activity was greatly elevated by co-overexpression of HNF4α and PGC1α in NIH3T3 cells. Moreover, the expression level of Acmsd mRNA was significantly increased by co-overexpression of HNF4α and PGC1α in primary hepatocytes compared with expression of either HNF4α or PGC1α alone. These results indicate that PGC1α is involved in Acmsd expression through cooperation with HNF4α.

Keywords

ACMSD PGC1α HNF4α Quinolinate Tryptophan NAD Nicotinamide 

Notes

Acknowledgements

This work was supported in part to Y.E. by a Grant-in-Aid from the Ministry of Education, Culture, Sports, Science and Technology of Japan and Initiative for Realizing Diversity in the Research Environment of Chiba University.

Compliance with ethical standards

Conflict of interest

The authors declare that we have no conflict of interest.

Ethical approval

The care and treatment of mice were in accordance with protocols approved by the local institutional guidelines for animal care of Chiba University and complied with the “Guide for the care and Use of Laboratory Animals” (NIH publication no. 85-23, revised 1985).

Human and animal rights statement

This article does not contain any studies with human participants performed by any of the authors. Animal experiments were performed according to the guidelines of the National Institutes of Health and the institutional rules for the use and care of laboratory animals at Chiba University.

References

  1. Cao W et al (2005) p38 Mitogen-activated protein kinase plays a stimulatory role in hepatic gluconeogenesis. J Biol Chem 280(52):42731–42737.  https://doi.org/10.1074/jbc.M506223200 CrossRefPubMedGoogle Scholar
  2. Egashira Y et al (2004) Differential effects of dietary fatty acids on rat liver alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase activity and gene expression. Biochim Biophys Acta 1686(1–2):118–124.  https://doi.org/10.1016/j.bbalip.2004.04.010 CrossRefPubMedGoogle Scholar
  3. Egashira Y et al (2007) Dietary protein level and dietary interaction affect quinolinic acid concentration in rats. Int J Vitam Nutr Res 77(2):142–148.  https://doi.org/10.1024/0300-9831.77.2.142 CrossRefPubMedGoogle Scholar
  4. Liu C, Lin JD (2011) PGC-1 coactivators in the control of energy metabolism. Acta Biochim Biophys Sin 43(4):248–257.  https://doi.org/10.1093/abbs/gmr007 CrossRefPubMedGoogle Scholar
  5. Lu H (2016) Crosstalk of HNF4α with extracellular and intracellular signaling pathways in the regulation of hepatic metabolism of drugs and lipids. Acta Pharm Sin B 6(5):393–408.  https://doi.org/10.1016/j.apsb.2016.07.003 CrossRefPubMedPubMedCentralGoogle Scholar
  6. Pucci L et al (2007) Tissue expression and biochemical characterization of human 2-amino 3-carboxymuconate 6-semialdehyde decarboxylase, a key enzyme in tryptophan catabolism. FEBS J 274(3):827–840.  https://doi.org/10.1111/j.1742-4658.2007.05635.x CrossRefPubMedGoogle Scholar
  7. Rhee J et al (2003) Regulation of hepatic fasting response by PPARgamma coactivator-1alpha (PGC-1): requirement for hepatocyte nuclear factor 4alpha in gluconeogenesis. Proc Natl Acad Sci USA 100(7):4012–4017.  https://doi.org/10.1073/pnas.0730870100 CrossRefPubMedGoogle Scholar
  8. Sanada H, Miyazaki M (1984) Effect of high-protein diet on liver alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase in rats. J Nutr Sci Vitaminol 30(2):113–123CrossRefGoogle Scholar
  9. Shin M et al (2006) Regulation of mouse hepatic alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase, a key enzyme in the tryptophan-nicotinamide adenine dinucleotide pathway, by hepatocyte nuclear factor 4 alpha and peroxisome proliferator-activated receptor alpha. Mol Pharmacol 70(4):1281–1290.  https://doi.org/10.1124/mol.106.026294 CrossRefPubMedGoogle Scholar
  10. Sugita Y et al (2008) Effect of biotin treatment on hepatic gene expression in streptozotocin-induced diabetic rats. Biosci Biotechnol Biochem 72(5):1290–1298.  https://doi.org/10.1271/bbb.70781 CrossRefPubMedGoogle Scholar
  11. Tanabe A et al (2002) Expression of rat hepatic 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase is affected by a high protein diet and by streptozotocin-induced diabetes. J Nutr 132(6):1153–1159.  https://doi.org/10.1093/jn/132.6.1153 CrossRefPubMedGoogle Scholar
  12. Watanabe M et al (2004) Bile acids lower triglyceride levels via a pathway involving FXR, SHP, and SREBP-1c. J Clin Investig 113(10):1408–1418.  https://doi.org/10.1172/JCI21025 CrossRefPubMedGoogle Scholar
  13. Yu L et al (2016) Evodia alkaloids suppress gluconeogenesis and lipogenesis by activating the constitutive androstane receptor. Biochim Biophys Acta 9:1100–1111.  https://doi.org/10.1016/j.bbagrm.2015.10.001 CrossRefGoogle Scholar

Copyright information

© Springer-Verlag GmbH Austria, part of Springer Nature 2018

Authors and Affiliations

  • Manami Koshiguchi
    • 1
  • Shizuka Hirai
    • 1
  • Yukari Egashira
    • 1
    Email author
  1. 1.Laboratory of Food and Nutrition, Division of Applied Biochemistry, Graduate School of HorticultureChiba UniversityMatsudoJapan

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