Munc18c is not rate-limiting for glucose and long-chain fatty acid uptake in the heart

Daphna D.J. Habets, Debbie C. Thurmond, Will A. Coumans, Arend Bonen, Jan F.C. Glatz, Joost J.F.P. Luiken

Research output: Contribution to journalArticle

6 Scopus citations


The role of soluble N -ethylmaleimide-sensitive factor attachment protein receptor (SNARE)- and SNARE-associated proteins have not yet been assessed in regulation of cardiac glucose uptake, nor in the regulation of long-chain fatty acid (LCFA) uptake in any tissue. Munc18c is a SNARE-associated protein that regulates GLUT4 translocation in skeletal muscle and adipose tissue. Using cardiomyocytes from Munc18c-/+ mice (with 56% reduction of Munc18c protein expression), we investigated whether this syntaxin4-associated protein is involved in regulation of cardiac substrate uptake. Basal, insulin- and oligomycin (a 5′ AMP-activated protein kinase-activating agent)-stimulated glucose and LCFA uptake were not altered significantly in Munc18c-/+ cardiomyocytes compared to wild-type cells. We conclude, therefore, that Munc18c is not rate-limiting for cardiac substrate uptake, neither under basal conditions nor when maximally stimulated metabolically.

Original languageEnglish (US)
Pages (from-to)81-86
Number of pages6
JournalMolecular and Cellular Biochemistry
Issue number1-2
StatePublished - Jan 1 2009



  • Cardiomyocytes
  • Glucose uptake
  • Long-chain fatty acid uptake
  • Munc18c

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Habets, D. D. J., Thurmond, D. C., Coumans, W. A., Bonen, A., Glatz, J. F. C., & Luiken, J. J. F. P. (2009). Munc18c is not rate-limiting for glucose and long-chain fatty acid uptake in the heart. Molecular and Cellular Biochemistry, 322(1-2), 81-86.