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• W2988892184 abstract "To explore the effect of LYRM1 over-expres- sion on basal and insulin-stimulated glucose uptake in rat skeletal muscle cells, and to understand the underlying mechanisms, Rat myoblasts (L6) transfected with either an empty expression vector (pcDNA3.1Myc/His B) or a LYRM1 expression vector were differentiated into myotu- bes. Glucose uptake was determined by measuring 2-deoxy-D-( 3 H) glucose uptake into L6 myotubes. Western blotting was performed to assess the translocation of insulin-sensitive glucose transporter 4 (GLUT4). It was also used to measure the phosphorylation and total protein contents of insulin-signaling proteins, such as the insulin receptor (IR), insulin receptor substrate (IRS)-1, phospha- tidylinositol-3-kinase (PI3K) p85, Akt, ERK1/2, P38, and JNK. LYRM1 over-expression in L6 myotubes reduced insulin-stimulated glucose uptake and impaired insulin- stimulated GLUT4 translocation. It also diminished insu- lin-stimulated tyrosine phosphorylation of IRS-1, PI3K (p85), and serine phosphorylation of Akt without affecting the phosphorylation of IR, ERK1/2, P38, and JNK. LYRM1 regulates the function of IRS-1, PI3K, and Akt, and decreases GLUT4 translocation and glucose uptake in response to insulin. These observations highlight the potential role of LYRM1 in glucose homeostasis and pos- sibly in the pathophysiology of type 2 diabetes related to obesity." @default.
• W2988892184 created "2019-11-22" @default.
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• W2988892184 date "2011-01-01" @default.
• W2988892184 modified "2023-09-27" @default.
• W2988892184 title "Over-expression of LYRM1 inhibits glucose transport in rat skeletal muscles via attenuated phosphorylation of PI3K (p85) and Akt" @default.
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• W2988892184 hasPublicationYear "2011" @default.
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