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The role of skeletal muscle Akt in the regulation of muscle mass and glucose homeostasis
Open accessAbstract
OBJECTIVE: Skeletal muscle insulin signaling is a major determinant of muscle growth and glucose homeostasis. Protein kinase B/Akt plays a prominent role in mediating many of the metabolic effects of insulin. Mice and humans harboring systemic loss-of-function mutations in Akt2, the most abundant Akt isoform in metabolic tissues, are glucose intolerant and insulin resistant. Since the skeletal muscle accounts for a significant amount of postprandial glucose disposal, a popular hypothesis in the diabetes field suggests that a reduction in Akt, specifically in skeletal muscle, leads to systemic glucose intolerance and insulin resistance. Despite this common belief, the specific role of skeletal muscle Akt in muscle growth and insulin sensitivity remains undefined. METHODS: We generated multiple mouse models of skeletal muscle Akt deficiency to evaluate the role of muscle Akt signaling in vivo. The effects of these genetic perturbations on muscle mass, glucose homeostasis and insulin sensitivity were assessed using both in vivo and ex vivo assays. RESULTS: Surprisingly, mice lacking Akt2 alone in skeletal muscle displayed normal skeletal muscle insulin signaling, glucose tolerance, and insulin sensitivity despite a dramatic reduction in phosphorylated Akt. In contrast, deletion of both Akt isoforms (M-AktDKO) prevented downstream signaling and resulted in muscle atrophy. Despite the absence of Akt signaling, in vivo and ex vivo insulin-stimulated glucose uptake were normal in M-AktDKO mice. Similar effects on insulin sensitivity were observed in mice with prolonged deletion (4 weeks) of both skeletal muscle Akt isoforms selectively in adulthood. Conversely, short term deletion (2 weeks) of skeletal muscle specific Akt in adult muscles impaired insulin tolerance paralleling the effect observed by acute pharmacological inhibition of Akt in vitro. Mechanistically, chronic ablation of Akt induced mitochondrial dysfunction and activation of AMPK, which was required for insulin-stimulated glucose uptake in the absence of Akt. CONCLUSIONS: Together, these data indicate that chronic reduction in Akt activity alone in skeletal muscle is not sufficient to induce insulin resistance or prevent glucose uptake in all conditions. Therefore, since insulin-stimulated glucose disposal in skeletal muscle is markedly impaired in insulin-resistant states, we hypothesize that alterations in signaling molecules in addition to skeletal muscle Akt are necessary to perturb glucose tolerance and insulin sensitivity in vivo.
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“recent studies utilizing skeletal muscle-specific knockouts of both Akt1 and Akt2 demonstrated that deletion of both isoforms reduces both muscle size and muscle protein synthesis, indicating that only minimal amounts of Akt in muscle are needed to transmit downstream signaling and preserve muscle mass in vivo [19,20].”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [19]
In the citing paper
“Skeletal muscle Akt signaling is both required and sufficient for muscle hypertrophy, as genetic loss of Akt isoforms in the muscle leads to decreased muscle size in adult mice [19,20,22].”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [19]
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“As described in prior studies, these mice display significant deficits in muscle growth and protein synthesis, consistent with a major anabolic role for Akt in muscle [19,20].”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [19]
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“Residual Akt1 expression in whole muscle tissue is due to the expression of Akt1 in non-muscle cells [19].”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [19]
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“Furthermore, the AKT1 rs1130214 polymorphism affects the AKT pathway, a critical component of the mTOR signaling cascade, influencing MPS rates [59].”
From Beyond Calories: Individual Metabolic and Hormonal Adaptations Driving Variability in Weight Management—A State-of-the-Art Narrative Review (2024) · cites this paper as [59]
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Cites
Watterson, K. R., Bestow, D., Gallagher, J. R., Hamilton, D. L., Ashford, F. B., Meakin, P. J., & Ashford, M. L. J. (2012) · Neurosignals · doi:10.1159/000334144 · Cited by 3,395
The selectivity of protein kinase inhibitors: a further update
Bain, J., Plater, L., Elliott, M., Shpiro, N., Hastie, C. J., McLauchlan, H., Klevernic, I. V., Arthur, J. S. C., Alessi, D. R., & Cohen, P. (2007) · Biochemical Journal · doi:10.1042/bj20070797 · Cited by 2,522
Skeletal Muscle Insulin Resistance Is the Primary Defect in Type 2 Diabetes
DeFronzo, R. A., & Tripathy, D. (2009) · Diabetes Care · doi:10.2337/dc09-s302 · Cited by 2,102
Cho, H., Mu, J., Kim, J. K., Thorvaldsen, J. L., Chu, Q., Crenshaw, E. B., Kaestner, K. H., Bartolomei, M. S., Shulman, G. I., & Birnbaum, M. J. (2001) · Science · doi:10.1126/science.292.5522.1728 · Cited by 1,860
DeFronzo, R. A., Jacot, E., Jequier, E., Maeder, E., Wahren, J., & Felber, J. P. (1981) · Diabetes · doi:10.2337/diab.30.12.1000 · Cited by 1,770
The pathogenesis of insulin resistance: integrating signaling pathways and substrate flux
Samuel, V. T., & Shulman, G. I. (2016) · Journal of Clinical Investigation · doi:10.1172/jci77812 · Cited by 1,484
Pathogenesis of type 2 diabetes mellitus
DeFronzo, R. A. (2004) · Medical Clinics of North America · doi:10.1016/j.mcna.2004.04.013 · Cited by 1,342
Cho, H., Thorvaldsen, J. L., Chu, Q., Feng, F., & Birnbaum, M. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100462200 · Cited by 959
Mu, J., Brozinick, J. T., Valladares, O., Bucan, M., & Birnbaum, M. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00251-9 · Cited by 924
Peng, X.-D., Xu, P.-Z., Chen, M.-L., Hahn-Windgassen, A., Skeen, J. E., Jacobs, J., Sundararajan, D., Chen, W. S., Crawford, S. E., Coleman, K. G., et al. (2003) · Genes & Development · doi:10.1101/gad.1089403 · Cited by 836
Garofalo, R. S., Orena, S. J., Rafidi, K., Torchia, A. J., Stock, J. L., Hildebrandt, A. L., Coskran, T., Black, S. C., Brees, D. J., Wicks, J. R., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci16885 · Cited by 726
Role of Akt/protein kinase B in metabolism
Whiteman, E. L., Cho, H., & Birnbaum, M. J. (2002) · Trends in Endocrinology and Metabolism · doi:10.1016/s1043-2760(02)00662-8 · Cited by 671
Role for Akt3/Protein Kinase Bγ in Attainment of Normal Brain Size
Easton, R., Cho, H., Roovers, K., Shineman, D. W., Mizrahi, M., Forman, M. S., Lee, V. M. ‐., Szabolcs, M. J., de Jong, R., Oltersdorf, T., et al. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.5.1869-1878.2005 · Cited by 551
AMPK in skeletal muscle function and metabolism
Kjøbsted, R., Hingst, J. R., Fentz, J., Foretz, M., Sanz, M.-N., Pehmøller, C. K., Shum, M., Marette, A., Mounier, R., Treebak, J. T., et al. (2017) · The FASEB Journal · doi:10.1096/fj.201700442r · Cited by 517
Exercise-induced increase in muscle insulin sensitivity
Holloszy, J. O. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00123.2005 · Cited by 494
Emerging role for AS160/TBC1D4 and TBC1D1 in the regulation of GLUT4 traffic
Sakamoto, K., & Holman, G. D. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90331.2008 · Cited by 481
The Glycogen-Binding Domain on the AMPK β Subunit Allows the Kinase to Act as a Glycogen Sensor
McBride, A., Ghilagaber, S., Nikolaev, A., & Hardie, D. G. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2008.11.008 · Cited by 432
Steinberg, G. R., Michell, B. J., van Denderen, B. J. W., Watt, M. J., Carey, A. L., Fam, B. C., Andrikopoulos, S., Proietto, J., Görgün, C. Z., Carling, D., et al. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.11.005 · Cited by 424
PREPARATION AND CHARACTERIZATION OF A PLASMA MEMBRANE FRACTION FROM ISOLATED FAT CELLS
McKeel, D. W., & Jarett, L. (1970) · The Journal of Cell Biology · doi:10.1083/jcb.44.2.417 · Cited by 402
Insulin regulates liver metabolism in vivo in the absence of hepatic Akt and Foxo1
Lu, M., Wan, M., Leavens, K. F., Chu, Q., Monks, B. R., Fernandez, S., Ahima, R. S., Ueki, K., Kahn, C. R., & Birnbaum, M. J. (2012) · Nature Medicine · doi:10.1038/nm.2686 · Cited by 392
Protein Kinase Bα/Akt1 Regulates Placental Development and Fetal Growth
Yang, Z.-Z., Tschopp, O., Hemmings-Mieszczak, M., Feng, J., Brodbeck, D., Perentes, E., & Hemmings, B. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302847200 · Cited by 384
Skeletal muscle glycolysis, oxidation, and storage of an oral glucose load.
Kelley, D. E., Mitrakou, A., Marsh, H. W., Schwenk, F. W., Benn, J., Sonnenberg, G. E., Arcangeli, M. A., Aoki, T. T., Sorensen, J., & Berger, M. (1988) · Journal of Clinical Investigation · doi:10.1172/jci113489 · Cited by 327
IRS1-Independent Defects Define Major Nodes of Insulin Resistance
Hoehn, K. L., Hohnen-Behrens, C., Cederberg, A., Wu, L. E., Turner, N. A., Yuasa, T., Ebina, Y., & James, D. E. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.04.005 · Cited by 318
The Effects of Wortmannin on Rat Skeletal Muscle
Yeh, J., Gulve, E. A., Rameh, L. E., & Birnbaum, M. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.5.2107 · Cited by 313
Insulin-Stimulated Akt Kinase Activity Is Reduced in Skeletal Muscle From NIDDM Subjects
Krook, A., Roth, R. A., Jiang, X. J., Zierath, J. R., & Wallberg‐Henriksson, H. (1998) · Diabetes · doi:10.2337/diab.47.8.1281 · Cited by 309
Activation of p38 MAP kinase enhances sensitivity of muscle glucose transport to insulin
Geiger, P. C., Wright, D. C., Han, D., & Holloszy, J. O. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00477.2004 · Cited by 306
Effect of Acute Exercise on AMPK Signaling in Skeletal Muscle of Subjects with Type 2 Diabetes
Sriwijitkamol, A., Coletta, D. K., Wajcberg, E., Balbontin, G. B., Reyna, S. M., Barrientes, J., Eagan, P. A., Jenkinson, C. P., Cersosimo, E., DeFronzo, R. A., et al. (2007) · Diabetes · doi:10.2337/db06-1119 · Cited by 304
Karlsson, H., Zierath, J. R., Kane, S., Krook, A., Lienhard, G. E., & Wallberg‐Henriksson, H. (2005) · Diabetes · doi:10.2337/diabetes.54.6.1692 · Cited by 299
Titchenell, P. M., Quinn, W. J., Lu, M., Chu, Q., Lu, W., Li, C., Chen, H., Monks, B. R., Chen, J., Rabinowitz, J. D., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.04.022 · Cited by 298
Self-citationBandyopadhyay, G. K., Yu, J. G., Ofrecio, J., & Olefsky, J. M. (2006) · Diabetes · doi:10.2337/db06-0062 · Cited by 291
Cokorinos, E., Delmore, J. E., Reyes, A. R., Albuquerque, B., Kjøbsted, R., Eskesen, N. O., Tran, J.-L., Jatkar, A., Cialdea, K., Esquejo, R. M., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.04.010 · Cited by 272
Taylor, E. B., An, D., Kramer, H. F., Yu, H., FUJII, N. L., Röckl, K. S. C., Bowles, N. P., Hirshman, M. F., Xie, J., Feener, E. P., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708839200 · Cited by 268
Taylor, R., Magnusson, I., Rothman, D. L., Cline, G. W., Caumo, A., Cobelli, C., & Shulman, G. I. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118379 · Cited by 258
Activation of AMP kinase enhances sensitivity of muscle glucose transport to insulin
Fisher, J. S., Gao, J., Han, D.-H., Holloszy, J. O., & Nolte, L. A. (2002) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2002.282.1.e18 · Cited by 244
Tremblay, F., Lavigne, C., Jacques, H., & Marette, A. (2001) · Diabetes · doi:10.2337/diabetes.50.8.1901 · Cited by 219
Sylow, L., Jensen, T. E., Kleinert, M., Højlund, K., Kiens, B., Wojtaszewski, J. F. P., Prats, C., Schjerling, P., & Richter, E. A. (2013) · Diabetes · doi:10.2337/db12-1148 · Cited by 210
Inducible Cre transgenic mouse strain for skeletal muscle-specific gene targeting
McCarthy, J. J., Srikuea, R., Kirby, T. J., Peterson, C. A., & Esser, K. A. (2012) · Skeletal Muscle · doi:10.1186/2044-5040-2-8 · Cited by 194
Muscle and adipose tissue insulin resistance: malady without mechanism?
Fazakerley, D. J., Krycer, J. R., Kearney, A. L., HOCKING, S. L., & James, D. E. (2018) · Journal of Lipid Research · doi:10.1194/jlr.r087510 · Cited by 188
Insulin and IGF-1 receptors regulate FoxO-mediated signaling in muscle proteostasis
O'Neill, B. T., Lee, K. Y., Klaus, K. A., Softic, S., Krumpoch, M. T., Fentz, J., Stanford, K. I., Robinson, M. M., Cai, W., Kleinridders, A., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci86522 · Cited by 185
Long, Y. C., Cheng, Z., Copps, K. D., & White, M. F. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00983-10 · Cited by 183
Enhanced muscle insulin sensitivity after contraction/exercise is mediated by AMPK
Kjøbsted, R., Munk-Hansen, N., Birk, J. B., Foretz, M., Viollet, B., Björnholm, M., Zierath, J. R., Treebak, J. T., & Wojtaszewski, J. F. P. (2017) · Diabetes · doi:10.2337/db16-0530 · Cited by 178
Differential role of insulin/IGF-1 receptor signaling in muscle growth and glucose homeostasis
O’Neill, B. T., Lauritzen, H. P. M. M., Hirshman, M. F., Smyth, G., Goodyear, L. J., & Kahn, C. R. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.037 · Cited by 171
Defective Signaling Through Akt-2 and -3 But Not Akt-1 in Insulin-Resistant Human Skeletal Muscle
Brozinick, J. T., Roberts, B. R., & Dohm, G. L. (2003) · Diabetes · doi:10.2337/diabetes.52.4.935 · Cited by 164
Chen, S., Wasserman, D. H., MacKintosh, C., & Sakamoto, K. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2010.12.005 · Cited by 161
Decreased Akt kinase activity and insulin resistance in C57BL/KsJ-Leprdb/db mice
Shao, J., Yamashita, H., Qiao, L., & Friedman, J. (2000) · Journal of Endocrinology · doi:10.1677/joe.0.1670107 · Cited by 150
Insulin, but Not Contraction, Activates Akt/PKB in Isolated Rat Skeletal Muscle
Brozinick, J. T., & Birnbaum, M. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.24.14679 · Cited by 149
Sylow, L., Kleinert, M., Pehmøller, C. K., Prats, C., Chiu, T. T., Klip, A., Richter, E. A., & Jensen, T. E. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.11.007 · Cited by 147
Kjøbsted, R., Treebak, J. T., Fentz, J., Lantier, L., Viollet, B., Birk, J. B., Schjerling, P., Björnholm, M., Zierath, J. R., & Wojtaszewski, J. F. P. (2014) · Diabetes · doi:10.2337/db14-1402 · Cited by 135
AMP-activated protein kinase selectively inhibited by the type II inhibitor SBI-0206965
Dite, T. A., Langendorf, C. G., Hoque, A., Galić, S., Rebello, R. J., Ovens, A. J., Lindqvist, L., Ngoei, K. R. W., Ling, N. X. Y., Furic, L., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003547 · Cited by 132
Dissociation of AMPK activity and ACCβ phosphorylation in human muscle during prolonged exercise
Wojtaszewski, J. F. P., Mourtzakis, M., Hillig, T., Saltin, B., & Pilegaard, H. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02465-8 · Cited by 126
Luo, J., Sobkiw, C. L., Hirshman, M. F., Logsdon, M. N., Li, T. Q., Goodyear, L. J., & Cantley, L. C. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.04.003 · Cited by 123
Ueda, S., Kitazawa, S., Ishida, K., Nishikawa, Y., Matsui, M., Matsumoto, H., Aoki, T., Nozaki, S., Takeda, T., Tamori, Y., et al. (2010) · The FASEB Journal · doi:10.1096/fj.09-137380 · Cited by 122
Tonks, K. T. T., Ng, Y., Miller, S., Coster, A. C. F., Samocha‐Bonet, D., Iseli, T. J., Xu, A., Patrick, E., Yang, J. Y. H., Junutula, J. R., et al. (2013) · Diabetologia · doi:10.1007/s00125-012-2811-y · Cited by 121
Green, C., Göransson, O., Kular, G. S., Leslie, N. R., Gray, A., Alessi, D. R., Sakamoto, K., & Hundal, H. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802623200 · Cited by 113
Cozzone, D., Fröjdö, S., Disse, E., Debard, C., Laville, M., Pirola, L., & Vidal, H. (2008) · Diabetologia · doi:10.1007/s00125-007-0913-8 · Cited by 111
Impaired postprandial glucose utilization in non-insulin-dependent diabetes mellitus
Kelley, D., Mokan, M., & Veneman, T. (1994) · Metabolism · doi:10.1016/0026-0495(94)90015-9 · Cited by 107
Steinberg, G. R., Watt, M. J., McGee, S. L., Chan, S., Hargreaves, M., Febbraio, M. A., Stapleton, D., & Kemp, B. E. (2006) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h06-003 · Cited by 104
H19 lncRNA Promotes Skeletal Muscle Insulin Sensitivity in Part by Targeting AMPK
Geng, T., Liu, Y., Xu, Y., Jiang, Y., Zhang, N., Wang, Z., Carmichael, G., Taylor, H. S., Li, D., & Huang, Y. (2018) · Diabetes · doi:10.2337/db18-0370 · Cited by 101
AS160 deficiency causes whole-body insulin resistance via composite effects in multiple tissues
Wang, H. Y., Ducommun, S., Quan, C., Xie, B., Li, M., Wasserman, D. H., Sakamoto, K., MacKintosh, C., & Chen, S. (2012) · Biochemical Journal · doi:10.1042/bj20120702 · Cited by 92
Hamada, T., Arias, E. B., & Cartee, G. D. (2006) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00416.2006 · Cited by 84
Insulin action in skeletal muscle from patients with NIDDM
Zierath, J. R., Krook, A., & Wallberg‐Henriksson, H. (1998) · Springer eBooks · doi:10.1007/978-1-4615-5647-3_16 · Cited by 82
Højlund, K., Birk, J. B., Klein, D. K., Levin, K., Rose, A. J., Hansen, B. F., Nielsen, J. N., Beck‐Nielsen, H., & Wojtaszewski, J. F. P. (2009) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2009-0897 · Cited by 77
Loss of Akt1 in Mice Increases Energy Expenditure and Protects against Diet-Induced Obesity
Wan, M., Easton, R., Gleason, C. E., Monks, B. R., Ueki, K., Kahn, C. R., & Birnbaum, M. J. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05806-11 · Cited by 76
Funai, K., & Cartee, G. D. (2009) · Diabetes · doi:10.2337/db08-1477 · Cited by 76
Insulin action in skeletal muscle from patients with NIDDM
Zierath, J. R., Krook, A., & Wallberg‐Henriksson, H. (1998) · Molecular and Cellular Biochemistry · doi:10.1023/a:1006861628496 · Cited by 65
Tunduguru, R., Chiu, T. T., Ramalingam, L., Elmendorf, J. S., Klip, A., & Thurmond, D. C. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.08.033 · Cited by 61
Lai, Y., Liu, Y., Jacobs, R., & Rider, M. H. (2012) · Biochemical Journal · doi:10.1042/bj20120772 · Cited by 57
A role for AMPK in increased insulin action after serum starvation
Ching, J. K., Rajguru, P., Marupudi, N., Banerjee, S., & Fisher, J. S. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00514.2009 · Cited by 50
Nozaki, S., Takeda, T., Kitaura, T., Takenaka, N., Kataoka, T., & Satoh, T. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.02.023 · Cited by 43
Whitfield, J., Paglialunga, S., Smith, B. K., Miotto, P. M., Simnett, G., Robson, H. L., Jain, S. S., Herbst, E. A. F., Desjardins, E. M., Dyck, D. J., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.806786 · Cited by 42
Regulation of glucose transport by the AMP-activated protein kinase
FUJII, N. L., Aschenbach, W. G., Musi, N., Hirshman, M. F., & Goodyear, L. J. (2004) · Proceedings of The Nutrition Society · doi:10.1079/pns2004340 · Cited by 37
AICAR and hyperosmotic stress increase insulin-stimulated glucose transport
Smith, J. L., Patil, P. B., & Fisher, J. S. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01297.2004 · Cited by 36
Ducommun, S., Wang, H. Y., Sakamoto, K., MacKintosh, C., & Chen, S. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00379.2011 · Cited by 35
Takenaka, N., Yasuda, N., Nihata, Y., Hosooka, T., Noguchi, T., Aiba, A., & Satoh, T. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.07.002 · Cited by 29
AKT 2 is the predominant AKT isoform expressed in human skeletal muscle
Matheny, R. W., Geddis, A. V., Abdalla, M. N., Leandry, L. A., Ford, M. G., McClung, H. L., & Pasiakos, S. M. (2018) · Physiological Reports · doi:10.14814/phy2.13652 · Cited by 28
Takenaka, N., Araki, N., & Satoh, T. (2019) · PLoS ONE · doi:10.1371/journal.pone.0212219 · Cited by 21
Putting Rac1 on the Path to Glucose Uptake
Rudich, A., & Klip, A. (2013) · Diabetes · doi:10.2337/db13-0381 · Cited by 15
AKT2 is the Predominant Akt Isoform Expressed in Human Skeletal Muscle
Geddis, A. V., Abdalla, M. N., Leandry, L. A., McClung, H. L., Pasiakos, S. M., & Matheny, R. W. (2017) · The FASEB Journal · doi:10.1096/fasebj.31.1_supplement.lb144 · Cited by 3
Flagged first, then by citations
3 of the 81 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Moller, 2019, The role of p-21 activated kinases (PAKs) in glucose homeostasis and skeletal muscle glucose uptake, BioRxiv
Cited by
Sorted by citations
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Mechanisms of muscle insulin resistance and the cross‐talk with liver and adipose tissue
Rosa, S. C. D. S., Nayak, N., Caymo, A. M., & Gordon, J. W. (2020) · Physiological Reports · doi:10.14814/phy2.14607 · Cited by 271
Insulin signalling and GLUT4 trafficking in insulin resistance
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Metadata
- Authors
- Jaiswal, N., Gavin, M. G., Quinn, W. J., Luongo, T. S., Gelfer, R. G., Baur, J. A., & Titchenell, P. M.
- Affiliations
- University of Pennsylvania (US)
- Corresponding author
- Titchenell, P.M.
- Venue
- Molecular Metabolism
- Publisher
- Elsevier BV
- Published
- 2019-10
- Volume
- 28
- Pages
- 1-13
- ISSN
- 2212-8778 (ISSN-L)
- PMC
- PMC6822261
- OpenAlex
- W2964701486
- Cited by
- 167
- References
- 81
- Citations by year
- 2026: 10 · 2025: 28 · 2024: 27 · 2023: 20 · 2022: 40 · 2021: 23 · 2020: 18 · 2019: 1
- FWCI
- 6.78
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Molecular Metabolism (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- University of Pennsylvania
- National Institutes of Health (P30 19525, K01 111715)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Keywords
- AKT2, Akt isoforms, muscle mass, muscle atrophy, glucose homeostasis, insulin resistance, insulin sensitivity, insulin-stimulated glucose uptake, mitochondrial dysfunction, AMPK, skeletal muscle insulin signaling
- MeSH terms
- Animals, Glucose, Homeostasis, Humans, Male, Weight Gain, Muscle, Skeletal, Proto-Oncogene Proteins c-akt, Mice
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 ›
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