Lipid Emulsion Enhances Vasoconstriction Induced by Dexmedetomidine in the Isolated Endothelium-Intact Aortaopen access
- Lee, Soo Hee; Ok, Seong-Ho; Ahn, Seung Hyun; Kim, Hyun-Jin; Bae, Sung Il; Kim, Ji-Yoon; Park, Kyeong-Eon; Hwang, Yeran; Sohn, Ju-Tae
- Issue Date
- dexmedetomidine; lipid emulsion; nitric oxide; contraction; endothelial nitric oxide synthase
- INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, v.22, no.7
- Journal Title
- INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
- This study aimed to examine the effect of lipid emulsion (LE) on the vasoconstriction induced by dexmedetomidine (DMT) in the isolated rat aorta and elucidate the associated cellular mechanism. The effect of LE, N-W-nitro-L-arginine methyl ester (L-NAME), and methyl-beta-cyclodextrin (M beta CD) on the DMT-induced contraction was examined. We investigated the effect of LE on the DMT-induced cyclic guanosine monophosphate (cGMP) formation and DMT concentration. The effect of DMT, LE, 4-Amino-3-(4-chlorophenyl)-1-(t-butyl)-1H-pyrazolo[3,4-d]pyrimidine,4-Amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine (PP2), and rauwolscine on the phosphorylation of endothelial nitric oxide synthase (eNOS), caveolin-1, and Src kinase was examined in the human umbilical vein endothelial cells. L-NAME, M beta CD, and LE (1%, standardized mean difference (SMD): 2.517) increased the DMT-induced contraction in the endothelium-intact rat aorta. LE (1%) decreased the DMT (10(-6) M) concentration (SMD: -6.795) and DMT-induced cGMP formation (SMD: -2.132). LE (1%) reversed the DMT-induced eNOS (Ser1177 and Thr496) phosphorylation. PP2 inhibited caveolin-1 and eNOS phosphorylation induced by DMT. DMT increased the Src kinase phosphorylation. Thus, LE (1%) enhanced the DMT-induced contraction by inhibition of NO synthesis, which may be caused by the decreased DMT concentration. DMT-induced NO synthesis may be caused by the increased eNOS (Ser1177) phosphorylation and decreased eNOS (Thr495) phosphorylation potentially mediated by Src kinase-induced caveolin-1 phosphorylation.
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- College of Medicine > Department of Medicine > Journal Articles
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