Molecular Neurobiology

, Volume 44, Issue 1, pp 1–6 | Cite as

Modulation of Myelin Basic Protein Gene Expression by Acetyl-l-Carnitine

  • Giovanna TrainaEmail author
  • Giuseppe Federighi
  • Monica Macchi
  • Rodolfo Bernardi
  • Mauro Durante
  • Marcello Brunelli


Acetyl-l-carnitine (ALC), the acetyl ester of l-carnitine, is a naturally occurring molecule which plays an essential role in intermediary and mitochondrial metabolism. It has also neurotrophic and antioxidant actions, demonstrating efficacy and high tolerability in the treatment of neuropathies of various etiologies. ALC is a molecule of considerable interest for its clinical application in various neural disorders, although little is known regarding its effects on gene expression. Suppression subtractive hybridization methodology was used for the generation of subtracted complementary DNA libraries and the subsequent identification of differentially expressed transcripts in the rat brain after chronic ALC treatments. We provided evidence for a downregulation of the expression of all of the isoforms of myelin basic protein gene following prolonged ALC treatment, indicating a possible role in the modulation of myelin basic protein turnover, stabilizing and maintaining myelin integrity.


Acetyl-l-carnitine Myelin basic protein Suppression subtractive hybridization Rat brain 


  1. 1.
    Jones LL, McDonald DA, Borum PR (2010) Acylcarnitines: role in brain. Prog Lipid Res 49(1):61–75PubMedCrossRefGoogle Scholar
  2. 2.
    Barhwal K, Singh SB, Hota SK, Jayalakshmi K, Ilavazhagan G (2007) Acetyl-l-carnitine ameliorates hypobaric hypoxic impairment and spatial memory deficits in rats. Eur J Pharmacol 570(1–3):97–107PubMedCrossRefGoogle Scholar
  3. 3.
    Traina G, Federighi G, Brunelli M (2008) Up-regulation of kinesin light-chain 1 gene expression by acetyl-l-carnitine: therapeutic possibility in Alzheimer’s disease. Neurochem Int 53:244–247PubMedCrossRefGoogle Scholar
  4. 4.
    Calabrese V, Cornelius C, Mancuso C et al (2008) Cellular stress response: a novel target for chemoprevention and nutritional neuroprotection in aging, neurodegenerative disorders and longevity. Neurochem Res 33(12):2444–2471PubMedCrossRefGoogle Scholar
  5. 5.
    Calò LA, Pagnin E, Davis PA et al (2006) Antioxidant effect of l-carnitine and its short chain esters: relevance for the protection from oxidative stress related cardiovascular damage. Int J Cardiol 107:54–60PubMedCrossRefGoogle Scholar
  6. 6.
    Ando S, Tadenuma T, Tanaka Y et al (2001) Enhancement of learning capacity and cholinergic synaptic function by carnitine in aging rats. Neurosci Res 66:266–271CrossRefGoogle Scholar
  7. 7.
    Traina G, Valleggi S, Bernardi R et al (2004) Identification of differentially expressed genes induced in the rat brain by acetyl-l-carnitine as evidenced by suppression subtractive hybridisation. Mol Brain Res 132:57–63PubMedCrossRefGoogle Scholar
  8. 8.
    Mathisen PM, Pease S, Garvey J, Hood L, Readhead C (1993) Identification of an embryonic isoform of myelin basic protein that is expressed widely in the mouse embryo. Proc Natl Acad Sci USA 90:10125–10129PubMedCrossRefGoogle Scholar
  9. 9.
    Traina G, Bernardi R, Cataldo E et al (2008) In the rat brain acetil-l-carnitine treatment modulates the expression of gene involved in neuronal ceroid lipofuscinosis. Mol Neurobiol 38(2):146–152PubMedCrossRefGoogle Scholar
  10. 10.
    Kimura M, Sato M, Akatsuka A et al (1998) Overexpression of a minor component of myelin basic protein isoform (17.2 kDa) can restore myelinogenesis in transgenic shiverer mice. Brain Res 785:245–252PubMedCrossRefGoogle Scholar
  11. 11.
    Staugaitis SM, Colman DR, Pedraza L (1996) Membrane adhesion and other functions for the myelin basic proteins. Bioessay 18(1):13–18CrossRefGoogle Scholar
  12. 12.
    Baumann N, Pham-Dinh D (2001) Biology of oligodendrocyte and myelin in the mammalian central nervous system. Physiol Rev 81(2):871–927PubMedGoogle Scholar
  13. 13.
    Readhead C, Popko B, Takahashi N et al (1987) Expression of a myelin basic protein gene in transgenic shiverer mice: correction of the dysmyelinating phenotype. Cell 48(4):703–712PubMedCrossRefGoogle Scholar
  14. 14.
    Roaoach A, Boyland K, Horvath S, Prusiner SB, Hood LE (1983) Characterization of cloned cDNA representing rat myelin basic protein: absence of expression in brain of shiverer mutant mice. Cell 34(3):799–806CrossRefGoogle Scholar
  15. 15.
    Zhang QY, Huang JH, Li HZ et al (2008) Myelin-basic protein-reactive specific CD4+ and CD8+ NK lymphocytes induce morphological changes in neuronal cell bodies and myelin sheaths: implications for multiple sclerosis. Arch Med Res 39(1):45–51PubMedCrossRefGoogle Scholar
  16. 16.
    Lamers KJ, Vos P, Verbeek MM et al (2003) Protein S-100B, neuron-specific enolase (NSE), myelin basic protein (MBP) and glial fibrillary acidic protein (GFAP) in cerebrospinal fluid (CSF) and blood of neurological patients. Brain Res Bull 61:261–264PubMedCrossRefGoogle Scholar
  17. 17.
    Ikeda O, Murakami M, Ino H et al (2002) Effects of brain-derived neurotrophic factor (BDNF) on compression-induced spinal cord injury: BDNF attenuates down-regulation of superoxide dismutase expression and promotes up-regulation of myelin basic protein expression. J Neuropathol Exp Neurol 61(2):142–153PubMedGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC 2011

Authors and Affiliations

  • Giovanna Traina
    • 1
    Email author
  • Giuseppe Federighi
    • 2
  • Monica Macchi
    • 2
  • Rodolfo Bernardi
    • 3
  • Mauro Durante
    • 3
  • Marcello Brunelli
    • 2
  1. 1.Department of Economics and Food SciencesUniversity of PerugiaPerugiaItaly
  2. 2.Department of Biology, Unit of General PhysiologyUniversity of PisaPisaItaly
  3. 3.Department of Agricultural Plant Biology, Genetic SectionUniversity of PisaPisaItaly

Personalised recommendations