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Activators of AMP-activated protein kinase enhance GLUT4 translocation and its glucose transport activity in 3T3-L1 adipocytes.
Am J Physiol Endocrinol Metab. 2005 Oct; 289(4):E643-9.AJ

Abstract

To determine whether the increase in glucose uptake following AMP-activated protein kinase (AMPK) activation in adipocytes is mediated by accelerated GLUT4 translocation into plasma membrane, we constructed a chimera between GLUT4 and enhanced green fluorescent protein (GLUT4-eGFP) and transferred its cDNA into the nucleus of 3T3-L1 adipocytes. Then, the dynamics of GLUT4-eGFP translocation were visualized in living cells by means of laser scanning confocal microscopy. It was revealed that the stimulation with 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside (AICAR) and 2,4-dinitrophenol (DNP), known activators of AMPK, promptly accelerates its translocation within 4 min, as was found in the case of insulin stimulation. The insulin-induced GLUT4 translocation was markedly inhibited after addition of wortmannin (P < 0.01). However, the GLUT4 translocation through AMPK activators AICAR and DNP was not affected by wortmannin. Insulin- and AMPK-activated translocation of GLUT4 was not inhibited by SB-203580, an inhibitor of p38 mitogen-activated protein kinase (MAPK). Glucose uptake was significantly increased after addition of AMPK activators AICAR and DNP (P < 0.05). AMPK- and insulin-stimulated glucose uptake were similarly suppressed by wortmannin (P < 0.05-0.01). In addition, SB-203580 also significantly prevented the enhancement of glucose uptake induced by AMPK and insulin (P < 0.05). These results suggest that AMPK-activated GLUT4 translocation in 3T3-L1 adipocytes is mediated through the insulin-signaling pathway distal to the site of activated phosphatidylinositol 3-kinase or through a signaling system distinct from that activated by insulin. On the other hand, the increase of glucose uptake dependent on AMPK activators AICAR and DNP would be additionally due to enhancement of the intrinsic activity in translocated GLUT4 protein, possibly through a p38 MAPK-dependent mechanism.

Authors+Show Affiliations

Third Department of Internal Medicine, Kyorin University School of Medicine, Mitaka, Tokyo 181-8611, Japan.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15928020

Citation

Yamaguchi, Shinya, et al. "Activators of AMP-activated Protein Kinase Enhance GLUT4 Translocation and Its Glucose Transport Activity in 3T3-L1 Adipocytes." American Journal of Physiology. Endocrinology and Metabolism, vol. 289, no. 4, 2005, pp. E643-9.
Yamaguchi S, Katahira H, Ozawa S, et al. Activators of AMP-activated protein kinase enhance GLUT4 translocation and its glucose transport activity in 3T3-L1 adipocytes. Am J Physiol Endocrinol Metab. 2005;289(4):E643-9.
Yamaguchi, S., Katahira, H., Ozawa, S., Nakamichi, Y., Tanaka, T., Shimoyama, T., Takahashi, K., Yoshimoto, K., Imaizumi, M. O., Nagamatsu, S., & Ishida, H. (2005). Activators of AMP-activated protein kinase enhance GLUT4 translocation and its glucose transport activity in 3T3-L1 adipocytes. American Journal of Physiology. Endocrinology and Metabolism, 289(4), E643-9.
Yamaguchi S, et al. Activators of AMP-activated Protein Kinase Enhance GLUT4 Translocation and Its Glucose Transport Activity in 3T3-L1 Adipocytes. Am J Physiol Endocrinol Metab. 2005;289(4):E643-9. PubMed PMID: 15928020.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Activators of AMP-activated protein kinase enhance GLUT4 translocation and its glucose transport activity in 3T3-L1 adipocytes. AU - Yamaguchi,Shinya, AU - Katahira,Hiroshi, AU - Ozawa,Sachihiko, AU - Nakamichi,Yoko, AU - Tanaka,Toshiaki, AU - Shimoyama,Tatsuhiro, AU - Takahashi,Kazuto, AU - Yoshimoto,Katsuhiko, AU - Imaizumi,Mica Ohara, AU - Nagamatsu,Shinya, AU - Ishida,Hitoshi, Y1 - 2005/05/31/ PY - 2005/6/2/pubmed PY - 2005/10/29/medline PY - 2005/6/2/entrez SP - E643 EP - 9 JF - American journal of physiology. Endocrinology and metabolism JO - Am. J. Physiol. Endocrinol. Metab. VL - 289 IS - 4 N2 - To determine whether the increase in glucose uptake following AMP-activated protein kinase (AMPK) activation in adipocytes is mediated by accelerated GLUT4 translocation into plasma membrane, we constructed a chimera between GLUT4 and enhanced green fluorescent protein (GLUT4-eGFP) and transferred its cDNA into the nucleus of 3T3-L1 adipocytes. Then, the dynamics of GLUT4-eGFP translocation were visualized in living cells by means of laser scanning confocal microscopy. It was revealed that the stimulation with 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside (AICAR) and 2,4-dinitrophenol (DNP), known activators of AMPK, promptly accelerates its translocation within 4 min, as was found in the case of insulin stimulation. The insulin-induced GLUT4 translocation was markedly inhibited after addition of wortmannin (P < 0.01). However, the GLUT4 translocation through AMPK activators AICAR and DNP was not affected by wortmannin. Insulin- and AMPK-activated translocation of GLUT4 was not inhibited by SB-203580, an inhibitor of p38 mitogen-activated protein kinase (MAPK). Glucose uptake was significantly increased after addition of AMPK activators AICAR and DNP (P < 0.05). AMPK- and insulin-stimulated glucose uptake were similarly suppressed by wortmannin (P < 0.05-0.01). In addition, SB-203580 also significantly prevented the enhancement of glucose uptake induced by AMPK and insulin (P < 0.05). These results suggest that AMPK-activated GLUT4 translocation in 3T3-L1 adipocytes is mediated through the insulin-signaling pathway distal to the site of activated phosphatidylinositol 3-kinase or through a signaling system distinct from that activated by insulin. On the other hand, the increase of glucose uptake dependent on AMPK activators AICAR and DNP would be additionally due to enhancement of the intrinsic activity in translocated GLUT4 protein, possibly through a p38 MAPK-dependent mechanism. SN - 0193-1849 UR - https://www.unboundmedicine.com/medline/citation/15928020/Activators_of_AMP_activated_protein_kinase_enhance_GLUT4_translocation_and_its_glucose_transport_activity_in_3T3_L1_adipocytes_ L2 - http://www.physiology.org/doi/full/10.1152/ajpendo.00456.2004?url_ver=Z39.88-2003&amp;rfr_id=ori:rid:crossref.org&amp;rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -