Visfatin, a novel adipokine, stimulates glucose uptake through the Ca2+-dependent AMPK-p38 MAPK pathway in C2C12 skeletal muscle cells
- Authors
- Lee, Jung Ok; Kim, Nami; Lee, Hye Jeong; Lee, Yong Woo; Kim, Joong Kwan; Kim, Hyung Ip; Lee, Soo Kyung; Kim, Su Jin; Park, Sun Hwa; Kim, Hyeon Soo
- Issue Date
- 6월-2015
- Publisher
- BIOSCIENTIFICA LTD
- Keywords
- adipokine; AMPK; calcium; diabetes; glucose transport
- Citation
- JOURNAL OF MOLECULAR ENDOCRINOLOGY, v.54, no.3, pp.251 - 262
- Indexed
- SCIE
SCOPUS
- Journal Title
- JOURNAL OF MOLECULAR ENDOCRINOLOGY
- Volume
- 54
- Number
- 3
- Start Page
- 251
- End Page
- 262
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/93353
- DOI
- 10.1530/JME-14-0274
- ISSN
- 0952-5041
- Abstract
- Visfatin is a novel adipocytokine produced by visceral fat. In the present study, visfatin increased AMP-activated protein kinase (AMPK) phosphorylation in mouse C2C12 skeletal muscle cells. It also increased phosphorylation of the insulin receptor, whose knockdown blocked visfatin-induced AMPK phosphorylation and glucose uptake. Visfatin stimulated glucose uptake in differentiated skeletal muscle cells. However, inhibition of AMPK alpha 2 with an inhibitor or with knockdown of AMPK alpha 2 using siRNA blocked visfatin-induced glucose uptake, which indicates that visfatin stimulates glucose uptake through the AMPK alpha 2 pathway. Visfatin increased the intracellular Ca2+ concentration. STO-609, a calmodulin-dependent protein kinase kinase inhibitor, blocked visfatin-induced AMPK phosphorylation and glucose uptake. Visfatin-mediated activation of p38 MAPK was AMPK alpha 2-dependent. Furthermore, both inhibition and knockdown of p38 MAPK blocked visfatin-induced glucose uptake. Visfatin increased glucose transporter type 4 (GLUT4) mRNA and protein levels. In addition, visfatin stimulated the translocation of GLUT4 to the plasma membrane, and this effect was suppressed by AMPK alpha 2 inhibition. The present results indicate that visfatin plays an important role in glucose metabolism via the Ca2+-mediated AMPK-p38 MAPK pathway.
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Collections - College of Medicine > Department of Medical Science > 1. Journal Articles
- Graduate School > Department of Biomedical Sciences > 1. Journal Articles
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