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L6肌细胞分化过程中GLUT1和GLUT4葡萄糖转运蛋白的差异表达。

Differential expression of the GLUT1 and GLUT4 glucose transporters during differentiation of L6 muscle cells.

作者信息

Mitsumoto Y, Burdett E, Grant A, Klip A

机构信息

Division of Cell Biology, Hospital for Sick Children, Toronto, Canada.

出版信息

Biochem Biophys Res Commun. 1991 Mar 15;175(2):652-9. doi: 10.1016/0006-291x(91)91615-j.

Abstract

Skeletal muscle is the main tissue responsible for glucose utilization in the fed state, and it expresses the ubiquitous GLUT1 glucose transporter and the muscle/fat specific GLUT4 glucose transporter. Here we investigated the expression of these transporters during muscle cell differentiation in vitro. Rat L6 muscle cells were grown to the stages of myoblasts, alignment and fused myotubes. Glucose (2-deoxy-D-glucose) transport was higher in myoblasts, decreasing with the progression of alignment and cell fusion. Conversely, insulin-stimulated glucose uptake was negligible in myoblasts, and increased with cell alignment and fusion. The cellular content of GLUT1 transporters decreased and that of GLUT4 transporters increased with cell fusion. Insulin rapidly stimulated glucose uptake in fused myotubes maintained in 2% serum but not in 10% serum. In 10% serum, basal glucose uptake increased as did the cellular content of GLUT1 transporters, while GLUT4 transporter content did not change. These results indicate that both transporters are regulated oppositely during muscle cell differentiation, and that high serum concentrations override the capacity of insulin to regulate transport by inducing overexpression of the GLUT1 transporter.

摘要

骨骼肌是进食状态下负责葡萄糖利用的主要组织,它表达普遍存在的GLUT1葡萄糖转运蛋白以及肌肉/脂肪特异性的GLUT4葡萄糖转运蛋白。在此,我们研究了这些转运蛋白在体外肌肉细胞分化过程中的表达情况。将大鼠L6肌肉细胞培养至成肌细胞、排列和融合肌管阶段。成肌细胞中的葡萄糖(2-脱氧-D-葡萄糖)转运较高,随着排列和细胞融合的进展而降低。相反,胰岛素刺激的葡萄糖摄取在成肌细胞中可忽略不计,并随着细胞排列和融合而增加。随着细胞融合,GLUT1转运蛋白的细胞含量减少,而GLUT4转运蛋白的细胞含量增加。胰岛素能迅速刺激维持在2%血清中的融合肌管摄取葡萄糖,但在10%血清中则不能。在10%血清中,基础葡萄糖摄取增加,GLUT1转运蛋白的细胞含量也增加,而GLUT4转运蛋白的含量没有变化。这些结果表明,在肌肉细胞分化过程中,这两种转运蛋白受到相反的调节,并且高血清浓度通过诱导GLUT1转运蛋白的过表达而超过了胰岛素调节转运的能力。

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