PPAR alpha-activation results in enhanced carnitine biosynthesis and OCTN2-mediated hepatic carnitine accumulation

Biochim Biophys Acta. 2007 Sep;1767(9):1134-42. doi: 10.1016/j.bbabio.2007.07.001. Epub 2007 Jul 13.

Abstract

In fasted rodents hepatic carnitine concentration increases considerably which is not observed in PPAR alpha-/- mice, indicating that PPAR alpha is involved in carnitine homeostasis. To investigate the mechanisms underlying the PPAR alpha-dependent hepatic carnitine accumulation we measured carnitine biosynthesis enzyme activities, levels of carnitine biosynthesis intermediates, acyl-carnitines and OCTN2 mRNA levels in tissues of untreated, fasted or Wy-14643-treated wild type and PPAR alpha-/- mice. Here we show that both enhancement of carnitine biosynthesis (due to increased gamma-butyrobetaine dioxygenase activity), extra-hepatic gamma-butyrobetaine synthesis and increased hepatic carnitine import (OCTN2 expression) contributes to the increased hepatic carnitine levels after fasting and that these processes are PPAR alpha-dependent.

MeSH terms

  • Animals
  • Base Sequence
  • Carnitine / biosynthesis*
  • Carnitine / metabolism
  • Gene Expression Regulation*
  • Humans
  • Liver / metabolism
  • Mice
  • Mice, Transgenic
  • Models, Biological
  • Molecular Sequence Data
  • Organic Cation Transport Proteins / physiology*
  • PPAR alpha / metabolism*
  • Rats
  • Sequence Homology, Nucleic Acid
  • Solute Carrier Family 22 Member 5
  • gamma-Butyrobetaine Dioxygenase / metabolism

Substances

  • Organic Cation Transport Proteins
  • PPAR alpha
  • Slc22a5 protein, mouse
  • Solute Carrier Family 22 Member 5
  • gamma-Butyrobetaine Dioxygenase
  • Carnitine