Habets Daphna D J, Thurmond Debbie C, Coumans Will A, Bonen Arend, Glatz Jan F C, Luiken Joost J F P
Department of Molecular Genetics, Cardiovascular Research Institute Maastricht (CARIM), Maastricht University, P.O. Box 616, 6200 MD, Maastricht, The Netherlands.
Mol Cell Biochem. 2009 Feb;322(1-2):81-6. doi: 10.1007/s11010-008-9942-y. Epub 2008 Nov 14.
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.
可溶性N - 乙基马来酰亚胺敏感因子附着蛋白受体（SNARE）及SNARE相关蛋白在心脏葡萄糖摄取调节中的作用尚未得到评估，在任何组织的长链脂肪酸（LCFA）摄取调节中也未得到评估。Munc18c是一种SNARE相关蛋白，可调节骨骼肌和脂肪组织中GLUT4的转位。我们使用来自Munc18c（ - / +）小鼠的心肌细胞（Munc18c蛋白表达降低56%），研究这种与 syntaxin4相关的蛋白是否参与心脏底物摄取的调节。与野生型细胞相比，Munc18c（ - / +）心肌细胞中基础、胰岛素和寡霉素（一种5' AMP激活蛋白激酶激活剂）刺激的葡萄糖和LCFA摄取均未显著改变。因此，我们得出结论，无论是在基础条件下还是在最大程度代谢刺激时，Munc18c都不是心脏底物摄取的限速因素。
