Overexpression of mitofusin 2 improves translocation of glucose transporter 4 in skeletal muscle of high‑fat diet‑fed rats through AMP‑activated protein kinase signaling.

KONG, DEXIAN; SONG, GUANGYAO; WANG, CHAO; MA, HUIJUAN; REN, LUPING; NIE, QIAN; ZHANG, XUEMEI; GAN, KEXIN

doi:10.3892/mmr.2013.1457

Cited by 29Metabolism, Diabetes, and CancerAdipose Tissue and MetabolismMitochondrial Function and Pathology

Overexpression of mitofusin 2 improves translocation of glucose transporter 4 in skeletal muscle of high‑fat diet‑fed rats through AMP‑activated protein kinase signaling.

Open access

KONG, DEXIAN, SONG, GUANGYAO, WANG, CHAO, MA, HUIJUAN, REN, LUPING, NIE, QIAN, ZHANG, XUEMEI, GAN, KEXIN·2013·Molecular Medicine Reports

DOI 10.3892/mmr.2013.1457

Open this paper in CoChat — free account Open PDF

Abstract

Mitofusin 2 (Mfn2) is a mitochondrial membrane protein that plays a role in mitochondrial fusion and metabolism in mammalian cells. Previous studies have reported a positive correlation between Mfn2 expression and insulin sensitivity in non‑diabetic and type 2 diabetic subjects. Thus, the aim of the present study was to investigate whether Mfn2 overexpression improves insulin sensitivity of high‑fat diet (HFD) rats and the possible underlying mechanisms. Male SD rats were randomly divided into four groups: negative control; HFD; HFD plus adenoviral vectors; and HFD plus adenoviral vectors encoding Mfn2. Following an 11‑week treatment protocol, the euglycemic‑hyperinsulinemic clamp technique was applied to evaluate insulin sensitivity in rats. The skeletal muscles from rats in each group were analyzed by real‑time PCR and western blot analysis to determine glucose transporter 4 (GLUT4) expression, translocation and relative translocation signaling. Consistent with Mfn2 repression and glucose intolerance, HFD downregulates GLUT4 expression at the mRNA and protein levels, while Mfn2 overexpression activates AMP‑activated protein kinase (AMPK), increases GLUT4 expression and translocation and improves insulin resistance in the skeletal muscles of HFD rats. Results of the present study indicate that Mfn2 overexpression improves insulin sensitivity and may regulate GLUT4 translocation in an AMPK‑dependent manner in the skeletal muscles of HFD rats. This study is likely to provide insight into the unique role of Mfn2 in promoting glucose uptake, leading to modulation of GLUT4 translocation signaling and maintenance of glucose homeostasis in vivo.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.3892/mmr.2013.1457

Cites

25 of 25 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

AMPK activity is reduced in skeletal muscle tissues of HFD-fed rats.
“Moreover, previous investigations have demonstrated that AMPK activity is reduced in skeletal muscle tissues of high-fat diet (HFD)-fed rats [17,18].”
From Resveratrol prevents sarcopenic obesity by reversing mitochondrial dysfunction and oxidative stress via the PKA/LKB1/AMPK pathway (2019) · cites this paper as [18]
MFN2-knockout mice exhibited enhanced hepatic glucose production and impaired response to insulin.
“For instance, MFN2-knockout mice exhibited enhanced hepatic glucose production and impaired response to insulin [67, 68].”
From Mitochondrial Adaptation in Skeletal Muscle: Impact of Obesity, Caloric Restriction, and Dietary Compounds (2024) · cites this paper as [68]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601 · see citing works
Mutation in mitochondrial tRNALeu(UUR) gene in a large pedigree with maternally transmitted type II diabetes mellitus and deafness
van den Ouweland, J. M. W., Lemkes, H. H. P. J., Ruitenbeek, W., Sandkuijl, L. A., de Vijlder, M. F., Struyvenberg, P. A. A., van de Kamp, J. J. P., & Maassen, J. A. (1992) · Nature Genetics · doi:10.1038/ng0892-368 · Cited by 1,127 · see citing works
Mitofusin-2 Determines Mitochondrial Network Architecture and Mitochondrial Metabolism
Bach, D., Pich, S., Soriano, F. X., Vega, N., Baumgartner, B., Oriola, J., Daugaard, J. R., Lloberas, J., Camps, M., Zierath, J. R., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212754200 · Cited by 832 · see citing works
Mitofusin 2 (Mfn2) links mitochondrial and endoplasmic reticulum function with insulin signaling and is essential for normal glucose homeostasis
Sebastián, D., Hernández-Alvarez, M. I., Segalés, J., Sorianello, E., Muñoz, J. P., Sala, D., Waget, A., Liesa, M., Paz, J. C., Gopalacharyulu, P., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1108220109 · Cited by 673 · see citing works
The Charcot-Marie-Tooth type 2A gene product, Mfn2, up-regulates fuel oxidation through expression of OXPHOS system
Pich, S., Bach, D., Briones, P., Liesa, M., Camps, M., Testar, X., Palacín, M., & Zorzano, A. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi149 · Cited by 455 · see citing works
Expression of <i>Mfn2</i>, the Charcot-Marie-Tooth Neuropathy Type 2A Gene, in Human Skeletal Muscle
Bach, D., Naon, D., Pich, S., Soriano, F. X., Vega, N., Rieusset, J., Laville, M., Guillet, C., Boirie, Y., Wallberg-Henriksson, H., et al. (2005) · Diabetes · doi:10.2337/diabetes.54.9.2685 · Cited by 369 · see citing works
Evidence for a Mitochondrial Regulatory Pathway Defined by Peroxisome Proliferator–Activated Receptor-γ Coactivator-1α, Estrogen-Related Receptor-α, and Mitofusin 2
Soriano, F. X., Liesa, M., Bach, D., Chan, D. C., Palacín, M., & Zorzano, A. (2006) · Diabetes · doi:10.2337/db05-0509 · Cited by 343 · see citing works
AICAR Administration Causes an Apparent Enhancement of Muscle and Liver Insulin Action in Insulin-Resistant High-Fat-Fed Rats
Iglesias, M. A., Ye, J.-M., Frangioudakis, G., Saha, A. K., Tomas, E., Ruderman, N. B., Cooney, G. J., & Kraegen, E. W. (2002) · Diabetes · doi:10.2337/diabetes.51.10.2886 · Cited by 290 · see citing works
Subjects With Early-Onset Type 2 Diabetes Show Defective Activation of the Skeletal Muscle PGC-1α/Mitofusin-2 Regulatory Pathway in Response to Physical Activity
Hernández-Alvarez, M. I., Thabit, H., Burns, N., Shah, S., Brema, I., Hatunic, M., Finucane, F., Liesa, M., Chiellini, C., Naon, D., et al. (2010) · Diabetes Care · doi:10.2337/dc09-1305 · Cited by 189 · see citing works
Mitochondrial dynamics as a bridge between mitochondrial dysfunction and insulin resistance
Zorzano, A., Liesa, M., & Palacı́n, M. (2009) · Archives of Physiology and Biochemistry · doi:10.1080/13813450802676335 · Cited by 123 · see citing works
Mitofusins are required for angiogenic function and modulate different signaling pathways in cultured endothelial cells
Lugus, J. J., Ngoh, G. A., Bachschmid, M. M., & Walsh, K. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.07.023 · Cited by 111 · see citing works
Muscle mitochondria and insulin resistance: a human perspective
Hoeks, J., & Schrauwen, P. (2012) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.05.007 · Cited by 94 · see citing works
Skeletal muscle triglycerides lowering is associated with net improvement of insulin sensitivity, TNF-α reduction and GLUT4 expression enhancement
Mingrone, G., Rosa, G. D., Rocco, P. D., Manco, M., Capristo, E., Castagneto, M., Vettor, R., Gasbarrini, G. B., & Greco, A. V. (2002) · International Journal of Obesity · doi:10.1038/sj.ijo.0802053 · Cited by 82 · see citing works
Bioactives from bitter melon enhance insulin signaling and modulate acyl carnitine content in skeletal muscle in high-fat diet-fed mice
Wang, Z. Q., Zhang, X. H., Yu, Y., Poulev, A., Ribnicky, D., Floyd, Z. E., & Cefalu, W. T. (2011) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2010.09.004 · Cited by 74 · see citing works
Self-citation
Overexpression of Mitofusin 2 inhibited oxidized low-density lipoprotein induced vascular smooth muscle cell proliferation and reduced atherosclerotic lesion formation in rabbit
Guo, Y., Chen, K., Gao, W. D., Li, Q., Chen, L., Wang, G., & Tang, J. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.08.191 · Cited by 70 · see citing works
Could the low level of expression of the gene encoding skeletal muscle mitofusin-2 account for the metabolic inflexibility of obesity?
Mingrone, G., Manco, M., Calvani, M., Castagneto, M., Naon, D., & Zorzano, A. (2005) · Diabetologia · doi:10.1007/s00125-005-1918-9 · Cited by 68 · see citing works
Mitofusin 2 Inhibits Angiotensin II-Induced Myocardial Hypertrophy
Yu, H., Guo, Y., Mi, L., Wang, Y., Li, L., & Gao, W. D. (2010) · Journal of Cardiovascular Pharmacology and Therapeutics · doi:10.1177/1074248410385683 · Cited by 61 · see citing works
POTENTIAL ROLE OF NITRIC OXIDE IN CONTRACTION‐STIMULATED GLUCOSE UPTAKE AND MITOCHONDRIAL BIOGENESIS IN SKELETAL MUSCLE
McConell, G. K., & Wadley, G. D. (2008) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.2008.05038.x · Cited by 38 · see citing works
Karanjin from Pongamia pinnata induces GLUT4 translocation in skeletal muscle cells in a phosphatidylinositol-3-kinase-independent manner
Jaiswal, N., Yadav, P. P., Maurya, R., Srivastava, A. K., & Tamrakar, A. K. (2011) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2011.08.049 · Cited by 37 · see citing works
17β-estradiol induces an interaction between adenosine monophosphate-activated protein kinase and the insulin signaling pathway in 3T3-L1 adipocytes
Kim, J.-Y., Jo, K.-J., Kim, B.-J., Baik, H., & Lee, S. (2012) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2012.1070 · Cited by 27 · see citing works
Effect of early insulin therapy on nuclear factor κB and cytokine gene expressions in the liver and skeletal muscle of high-fat diet, streptozotocin-treated diabetic rats
Bi, Y., Sun, W., Chen, X., Li, M., Liang, H., Cai, M., Zhu, Y., He, X., Xu, F. L., & Weng, J. (2008) · Acta Diabetologica · doi:10.1007/s00592-008-0038-7 · Cited by 26 · see citing works
Plasma membrane content of insulin‐regulated glucose transporter in skeletal muscle of the male Otsuka Long‐Evans Tokushima Fatty rat, a model of non‐insulin‐dependent diabetes mellitus
Sato, T., Man, Z., Toide, K., & Asahi, Y. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00369-4 · Cited by 24 · see citing works
Effect of mitofusin 2 overexpression on the proliferation and apoptosis of high-glucose-induced rat glomerular mesangial cells
Tang, W., Cui, T., Ben, W., Wu, W., & Fu, P. (2012) · Journal of Nephrology · doi:10.5301/jn.5000089 · Cited by 19 · see citing works
Liver-specific reduction of Mfn2 protein by RNAi results in impaired glycometabolism and lipid homeostasis in BALB/c mice
Chen, X., & Xu, Y. (2009) · Journal of Huazhong University of Science and Technology [Medical Sciences] · doi:10.1007/s11596-009-0603-5 · Cited by 16 · see citing works
Fatty acids inhibit insulin-mediated glucose transport associated with actin remodeling in rat L6 muscle cells
Zhao, H., Liu, L., Sui, Y., Ho, S. K. S., Tam, S.-K., Lai, F. M., Chan, J. C. N., & Tong, P. C. Y. (2010) · Acta Diabetologica · doi:10.1007/s00592-010-0225-1 · Cited by 5 · see citing works

Flagged first, then by citations

Sorted by citations

Metabolic control of cell death
Green, D. R., Galluzzi, L., & Kroemer, G. (2014) · Science · doi:10.1126/science.1250256 · Cited by 661 · see citing works
Resveratrol prevents sarcopenic obesity by reversing mitochondrial dysfunction and oxidative stress via the PKA/LKB1/AMPK pathway
Huang, Y., Zhu, X., Chen, K., Lang, H., Zhang, Y., Hou, P., Ran, L., Zhou, M., Zheng, J., Yi, L., et al. (2019) · Aging · doi:10.18632/aging.101910 · Cited by 167 · see citing works
Stress-responsive FKBP51 regulates AKT2-AS160 signaling and metabolic function
Balsevich, G., Häusl, A. S., Meyer, C. W., Karamihalev, S., Feng, X., Pöhlmann, M. L., Dournes, C., Uribe-Marino, A., Santarelli, S., Labermaier, C., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01783-y · Cited by 134 · see citing works
Mitochondrial dysfunction as a central event for mechanisms underlying insulin resistance: The roles of long chain fatty acids
Hafizi Abu Bakar, M., Kian Kai, C., Wan Hassan, W. N., Sarmidi, M. R., Yaakob, H., & Zaman Huri, H. (2015) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.2601 · Cited by 91 · see citing works
Mitofusin 2 as a Driver That Controls Energy Metabolism and Insulin Signaling
Zorzano, A., Hernández‐Álvarez, M. I., Sebastián, D., & Muñoz, J. P. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6208 · Cited by 83 · see citing works
Roles of mitochondrial fragmentation and reactive oxygen species in mitochondrial dysfunction and myocardial insulin resistance
Watanabe, T., Saotome, M., Nobuhara, M., Sakamoto, A., Urushida, T., Katoh, H., Satoh, H., Funaki, M., & Hayashi, H. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.02.027 · Cited by 81 · see citing works
Mechanisms underpinning AMP-activated protein kinase-related effects on behavior and hippocampal neurogenesis in an animal model of depression
Odaira, T., Nakagawasai, O., Takahashi, K., Nemoto, W., Sakuma, W., Lin, J.-R., & Tan–No, K. (2019) · Neuropharmacology · doi:10.1016/j.neuropharm.2019.03.026 · Cited by 80 · see citing works
Mitochondrial dynamics in skeletal muscle insulin resistance and type 2 diabetes
Fealy, C. E., Mulya, A., Axelrod, C. L., & Kirwan, J. P. (2018) · Translational Research · doi:10.1016/j.trsl.2018.07.011 · Cited by 63 · see citing works
Skeletal muscle mitochondrial network dynamics in metabolic disorders and aging
Fealy, C. E., Grevendonk, L., Joris Hoeks, J., & Hesselink, M. K. C. (2021) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2021.07.013 · Cited by 58 · see citing works
Mitochondrial dynamics, quality control and miRNA regulation in skeletal muscle: implications for obesity and related metabolic disease
Dahlmans, D., Houzelle, A., Schrauwen, P., & Joris Hoeks, J. (2016) · Clinical Science · doi:10.1042/cs20150780 · Cited by 44 · see citing works
Molecular insight and pharmacological approaches targeting mitochondrial dynamics in skeletal muscle during obesity
Jheng, H.-F., Huang, S.-H., Kuo, H.-M., Hughes, M. W., & Tsai, Y. (2015) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12863 · Cited by 34 · see citing works
Iso-Mukaadial Acetate from Warburgia salutaris Enhances Glucose Uptake in the L6 Rat Myoblast Cell Line
Msomi, N. Z., Shode, F. O., Pooe, O. J., Mazibuko-Mbeje, S. E., & Simelane, M. B. C. (2019) · Biomolecules · doi:10.3390/biom9100520 · Cited by 34 · see citing works
Influence of Obesity and Type 2 Diabetes on Calcium Handling by Skeletal Muscle: Spotlight on the Sarcoplasmic Reticulum and Mitochondria
Eshima, H. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.758316 · Cited by 32 · see citing works
Mitofusin 2: A link between mitochondrial function and substrate metabolism?
Emery, J., & Ortiz, R. M. (2021) · Mitochondrion · doi:10.1016/j.mito.2021.09.003 · Cited by 32 · see citing works
Mitochondrial Adaptation in Skeletal Muscle: Impact of Obesity, Caloric Restriction, and Dietary Compounds
Jun, L., Tao, Y.-X., Geetha, T., & Babu, J. R. (2024) · Current Nutrition Reports · doi:10.1007/s13668-024-00555-7 · Cited by 27 · see citing works
Combination of Exercise Training and Resveratrol Attenuates Obese Sarcopenia in Skeletal Muscle Atrophy
Bai, C., Alizargar, J., Peng, C.-Y., & Wu, J. (2020) · The Chinese Journal of Physiology · doi:10.4103/cjp.cjp_95_19 · Cited by 26 · see citing works
Mitofusion is required for MOTS‐c induced GLUT4 translocation
Bhullar, K. S., Shang, N., Kerek, E. M., Wu, K., & Wu, J. (2021) · Scientific Reports · doi:10.1038/s41598-021-93735-2 · Cited by 24 · see citing works
Role of mitochondria-associated endoplasmic reticulum membranes in insulin sensitivity, energy metabolism, and contraction of skeletal muscle
Nieblas, B., Pérez-Treviño, P., & Garcı́a, N. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.959844 · Cited by 24 · see citing works
Skeletal muscle bioenergetic health and function in people living with HIV: association with glucose tolerance and alcohol use
Levitt, D. E., Ferguson, T. F., Primeaux, S. D., Zavala, J. A., Ahmed, J., Marshall, R. H., Simon, L., & Molina, P. E. (2021) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00197.2021 · Cited by 19 · see citing works
Effect of Intermittent Hypoxia and Rimonabant on Glucose Metabolism in Rats: Involvement of Expression of GLUT4 in Skeletal Muscle
Wang, X., Yu, Q., Yue, H., Zeng, S., & Cui, F. (2015) · Medical Science Monitor · doi:10.12659/msm.896039 · Cited by 18 · see citing works
Mitochondria and endoplasmic reticulum: Targets for a better insulin sensitivity in skeletal muscle?
Boulinguiez, A., Staels, B., Duez, H., & Lancel, S. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2017.05.011 · Cited by 16 · see citing works
Swimming improves high-fat induced insulin resistance by regulating lipid and energy metabolism and the insulin pathway in rats
Song, A., Wang, C., Ren, L., & Zhao, J. (2014) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2014.1738 · Cited by 15 · see citing works
Self-citation
Early energy metabolism-related molecular events in skeletal muscle of diabetic rats: The effects of l-arginine and SOD mimic
Stančić, A., Filipović, M. R., Ivanović‐Burmazović, I., Masovic, S., Janković, A., Otašević, V., Korać, A., Buzadžić, B., & Korać, B. (2017) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2017.05.003 · Cited by 13 · see citing works
Prenatal Low-Protein Diet Affects Mitochondrial Structure and Function in the Skeletal Muscle of Adult Female Offspring
Vidyadharan, V. A., Betancourt, A., Smith, C., Yallampalli, C., & Blesson, C. S. (2022) · Nutrients · doi:10.3390/nu14061158 · Cited by 10 · see citing works
Maternal Low-Protein Diet Leads to Mitochondrial Dysfunction and Impaired Energy Metabolism in the Skeletal Muscle of Male Rats
Vidyadharan, V. A., Betancourt, A., Smith, C., Blesson, C. S., & Yallampalli, C. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252312860 · Cited by 8 · see citing works
Resveratrol attenuates high-fat diet-induced obesity and the aging-related sarcopenia mitochondrial dysfunction in skeletal musclePreprint
Bai, C., Alizargar, J., & Wu, J. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/823088 · Cited by 4 · see citing works
The Low Protein Diet induced Fetal Programming Leads to Mitochondrial Dysfunction and Metabolic Inflexibility in the Skeletal Muscle of Male RatsPreprint
Vidyadharan, V. A., Betancourt, A., Smith, C., Blesson, C. S., & Yallampalli, C. (2024) · Research Square · doi:10.21203/rs.3.rs-4103233/v1 · Cited by 1 · see citing works
Cellular functional roles of celastrol on mitochondrial dysfunction-induced insulin resistance
Bakar, A., & Bakar, M. H. A. (2015)
Papel da alça ECA2/Ang 1-7/Mas no músculo esquelético para a prevenção de distúrbios metabólicos por meio do treinamento físico aeróbio
Vecchiatto, B. (2019) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.100.2019.tde-01102019-220112

Mitofusin-2 ameliorates high-fat diet-induced insulin resistance in liver of rats
Kexin, Gan, Chao, Wang, Jin-Hu, Chen, Chun-Jing, Zhu, Z., Guangyao, G., & Сонг (2013)
Mitofusion-2-mediated alleviation of insulin resistance in rats through reduction in lipid intermediate accumulation in skeletal muscle
Zhang, X., Wang, C., Song, G., Gan, K., Kong, D., Nie, Q., & Ren, L. (2013) · Journal of Biomedical Science · doi:10.1186/1423-0127-20-45 · Cited by 27 · see citing works
Self-citation
Signalling GLUTtony keeps the sugar coming through glucose transporter expression
McGee, S. L. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2009.179093
ORIGINAL ARTICLE Ablation of AMP-Activated Protein Kinase �2 Activity Exacerbates Insulin Resistance Induced by High-Fat Feeding of Mice
Fujii, N., Ho, R. C., Manabe, Y., Jessen, N., Toyoda, T., Holl, W. L., Summers, S. A., Hirshman, M. F., & Goodyear, L. J. (2013)
Ablation of AMP-Activated Protein Kinase α2 Activity Exacerbates Insulin Resistance Induced by High-Fat Feeding of Mice
Fujii, N., Ho, R. C., Manabe, Y., Jessen, N., Toyoda, T., Holland, W. L., Summers, S. A., Hirshman, M. F., & Goodyear, L. J. (2008) · Diabetes · doi:10.2337/db07-1187 · Cited by 107 · see citing works

Authors: KONG, D., SONG, G., WANG, C., MA, H., REN, L., NIE, Q., ZHANG, X., & GAN, K.
Affiliations: Hebei Medical University (CN)
Hebei General Hospital (CN)
ORCID: KONG, DEXIAN
SONG, GUANGYAO
WANG, CHAO
MA, HUIJUAN
REN, LUPING
NIE, QIAN
GAN, KEXIN
Venue: Molecular Medicine Reports
Publisher: Spandidos Publications
Published: 2013-05-02
Volume: 8
Issue: 1
Pages: 205-210
ISSN: 1791-2997 (ISSN-L)
1791-3004
DOI: 10.3892/mmr.2013.1457
OpenAlex: W2017023704
Cited by: 29
References: 25
Citations by year: 2024: 3 · 2022: 2 · 2021: 5 · 2020: 1 · 2019: 5 · 2018: 1 · 2017: 3 · 2016: 1 · 2015: 4 · 2014: 4
FWCI: 1.34
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Molecular Medicine Reports (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Keywords: mitofusin 2, glucose transporter 4, GLUT4 translocation, AMPK, insulin sensitivity, insulin resistance, high-fat diet, skeletal muscle, glucose uptake, glucose homeostasis, mitochondrial fusion, adenoviral overexpression
MeSH terms: Animals, Blood Glucose, Fatty Acids, Gene Expression Regulation, Glucose, Insulin, Male, Membrane Proteins, Signal Transduction, Gene Expression, Muscle, Skeletal, GTP Phosphohydrolases, Protein Transport, Mitochondrial Proteins, Proto-Oncogene Proteins c-akt, Glucose Transporter Type 4, Rats, AMP-Activated Protein Kinases, Diet, High-Fat

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Overexpression of mitofusin 2 improves translocation of glucose transporter 4 in skeletal muscle of high‑fat diet‑fed rats through AMP‑activated protein kinase signaling.

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks