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Regulation of glycogen synthase and phosphorylase activities by glucose and insulin in human skeletal muscle.
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We examined the insulin dose-response characteristics of human muscle glycogen synthase and phosphorylase activation. We also determined whether increasing the rate of glucose disposal by hyperglycemia at a fixed insulin concentration activates glycogen synthase. Physiological increments in plasma insulin but not glucose increased the fractional activity of glycogen synthase. The ED50: s for insulin stimulation of whole body and forearm glucose disposal were similar and unaffected by glycemia. Glycogen synthase activation was exponentially related to the insulin-mediated component of whole body and forearm glucose disposal at each glucose concentration. Neither insulin nor glucose changed glycogen phosphorylase activity. These results suggest that insulin but not the rate of glucose disposal per se regulates glycogen synthesis by a mechanism that involves dephosphorylation of glycogen synthase but not phosphorylase. This implies that the low glycogen synthase activities found in insulin-resistant states are a consequence of impaired insulin action rather than reduced glucose disposal.
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“Glycogen synthase is the key insulin-regulated enzyme that controls the rate of muscle glycogen synthesis [148, 150, 200, 212–214].”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [212]
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Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
Glucose clamp technique: a method for quantifying insulin secretion and resistance.
DeFronzo, R. A., Tobin, J. D., & Andres, R. (1979) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1979.237.3.e214 · Cited by 7,425
Classification and diagnosis of diabetes mellitus and other categories of glucose intolerance.
National Diabetes Data Group (1979) · Diabetes · doi:10.2337/diab.28.12.1039 · Cited by 4,909
Coated Charcoal Immunoassay of Insulin
Herbert, V. D., Lau, K., Gottlieb, C. W., & Bleicher, S. J. (1965) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem-25-10-1375 · Cited by 2,969
DeLÉAN, A., Munson, P. J., & Rodbard, D. (1978) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1978.235.2.e97 · Cited by 2,384
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
Assessment of Insulin Sensitivityin Vivo*
Bergman, R. N., Finegood, D. T., & Ader, M. (1985) · Endocrine Reviews · doi:10.1210/edrv-6-1-45 · Cited by 1,072
Measurement of Size and Turnover Rate of Body Glucose Pool by the Isotope Dilution Method
Steele, R., Wall, J. S., de Bodo, R. C., & Altszuler, N. (1956) · American Journal of Physiology-Legacy Content · doi:10.1152/ajplegacy.1956.187.1.15 · Cited by 816
A New and Rapid Method for the Determination of Glucose by Measurement of Rate of Oxygen Consumption
Kadish, A. H., Litle, R. L., & Sternberg, J. (1968) · Clinical Chemistry · doi:10.1093/clinchem/14.2.116 · Cited by 739
Effects of arterial versus venous sampling on analysis of glucose kinetics in man
McGuire, E. A., Helderman, J. H., Tobin, J. D., Andres, R., & Berman, M. D. (1976) · Journal of Applied Physiology · doi:10.1152/jappl.1976.41.4.565 · Cited by 704
Cited by
Sorted by citations
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
Shulman, G. I., Rothman, D. L., Jue, T., Stein, P., DeFronzo, R. A., & Shulman, R. G. (1990) · New England Journal of Medicine · doi:10.1056/nejm199001253220403 · Cited by 1,248
Pathogenesis of insulin resistance in skeletal muscle
Abdul-Ghani, M. A., & DeFronzo, R. A. (2010) · Journal of Biomedicine and Biotechnology · doi:10.1155/2010/476279 · Cited by 670
“Glycogen synthase is the key insulin-regulated enzyme that controls the rate of muscle glycogen synthesis [148, 150, 200, 212–214].”
BackgroundLeighton, B., & Cooper, G. J. S. (1988) · Nature · doi:10.1038/335632a0 · Cited by 473
Insulin: The master regulator of glucose metabolism
Norton, L., Shannon, C. E., Gastaldelli, A., & DeFronzo, R. A. (2022) · Metabolism · doi:10.1016/j.metabol.2022.155142 · Cited by 367
Rothman, D. L., Magnusson, I., Cline, G., Gerard, D., Kahn, C. R., Shulman, R. G., & Shulman, G. I. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.4.983 · Cited by 325
Rothman, D. L., Shulman, R. G., & Shulman, G. I. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115686 · Cited by 327
Shepherd, P. R., Navé, B. T., & Siddle, K. (1995) · Biochemical Journal · doi:10.1042/bj3050025 · Cited by 277
Kelley, D. E., & Mandarino, L. J. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114935 · Cited by 210
Obesity and insulin resistance: Lessons learned from the Pima indians
Lillioja, S., & Bogardus, C. (1988) · Diabetes/Metabolism Reviews · doi:10.1002/dmr.5610040508 · Cited by 203
Self-citationSuikkari, A., Koivisto, V. A., Koistinen, R. A., Seppälä, M. T., & Yki‐Järvinen, H. (1989) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem-68-1-135 · Cited by 199
Self-citationThorburn, A. W., Gumbiner, B., Bulacan, F., Wallace, P., & Henry, R. R. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114468 · Cited by 185
The regulation of carbohydrate and fat metabolism during and after exercise
Holloszy, J. O. (1998) · Frontiers in bioscience · doi:10.2741/a342 · Cited by 180
Nuutila, P., Raitakari, M., Laine, H. K., Kirvelä, O., Takala, T., Utriainen, T., Mäkimattila, S., Pitkänen, O., Ruotsalainen, U., Iida, H., et al. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118601 · Cited by 156
Self-citationIn vivo regulation of muscle glycogen synthase and the control of glycogen synthesis.
Shulman, R. G., Bloch, G., & Rothman, D. L. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.19.8535 · Cited by 152
Thorburn, A. W., Gumbiner, B., Bulacan, F., Brechtel, G., & Henry, R. R. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115022 · Cited by 150
Cooper, G. J. S., Day, A. J., Willis, A. C., Roberts, A. N., Reid, K. B. M., & Leighton, B. (1989) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(89)90220-6 · Cited by 143
Effects of insulin on skeletal muscle glucose storage, oxidation, and glycolysis in humans
Kelley, D. E., Reilly, J. P., Veneman, T. F., & Mandarino, L. J. (1990) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1990.258.6.e923 · Cited by 138
The mode of action and clinical pharmacology of gliclazide: a review
Campbell, D. B., Lavielle, R., & Nathan, C. (1991) · Diabetes Research and Clinical Practice · doi:10.1016/0168-8227(91)90005-x · Cited by 129
Goldfine, A. B., Conlin, P. R., Halperin, F., Koška, J., Permana, P. A., Schwenke, D. C., Shoelson, S. E., & Reaven, P. D. (2013) · Diabetologia · doi:10.1007/s00125-012-2819-3 · Cited by 127
“As lowering glucose levels per se improves peripheral glucose utilisation [21, 43], studying individuals with impaired fasting glucose and/or impaired glucose tolerance provides a direct assessment of the insulinsensitising effects of the medication in the absence of hyperglycaemia.”
Regulation of Carbohydrate and Fat Metabolism During and After Exercise
Holloszy, J. O., & Kohrt, W. M. (1996) · Annual Review of Nutrition · doi:10.1146/annurev.nu.16.070196.001005 · Cited by 130
“There has been much interest in the concept that glycogen synthase activity limits and determines the rate of muscle glycogen synthesis (177,182-184).”
BackgroundKoška, J., Ortega, E., Bunt, J. C., Gasser, A., Impson, J., Hanson, R. L., Forbes, J. M., de Courten, B. V., & Krakoff, J. A. (2008) · Diabetologia · doi:10.1007/s00125-008-1239-x · Cited by 122
“Normalisation for insulin concentration reflects the fact that whole-body glucose uptake progressively increases with higher rates of insulin infusions and the consequent rise in systemic insulin concentrations within the high physiological range [29, 34, 35].”
BackgroundAcute and chronic effects of hyperglycaemia on glucose metabolism
Yki-J�rvinen, H. (1990) · Diabetologia · doi:10.1007/bf00400200 · Cited by 108
“dephosphorylation of glycogen synthase and pyruvate dehydrogenase, [14,15]), hyperglycaemia increases muscle glycogen content without dephosphorylation of glycogen synthase in humans [14,16].”
BackgroundSelf-citationEffect of endurance exercise training on muscle glycogen supercompensation in rats
Nakatani, A., Han, D., Hansen, P. A., Nolte, L. A., Host, H. H., Hickner, R. C., & Holloszy, J. O. (1997) · Journal of Applied Physiology · doi:10.1152/jappl.1997.82.2.711 · Cited by 95
“It has also been proposed that GS activity plays a key role in determining the rates of insulin-stimulated glucose uptake and glycogen synthesis in muscle (5, 18, 29).”
BackgroundHow to measure insulin action in vivo
Scheen, A. J., Paquot, N., Castillo, M. J., & Lefèbvre, P. J. (1994) · Diabetes/Metabolism Reviews · doi:10.1002/dmr.5610100206 · Cited by 90
Non-insulin-dependent Diabetes Mellitus - A Collision between Thrifty Genes and an Affluent Society
Groop, L., & Tuomi, T. (1997) · Annals of Medicine · doi:10.3109/07853899708998742 · Cited by 88
Hyperglycemia and Inhibition of Glycogen Synthase in Streptozotocin-treated Mice
Parker, G. J., Taylor, R. P., Jones, D., & McClain, D. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312139200 · Cited by 84
Predominant role of gluconeogenesis in the hepatic glycogen repletion of diabetic rats.
Giaccari, A., & Rossetti, L. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115583 · Cited by 84
Interaction of carbohydrate and fat fuels in human skeletal muscle: impact of obesity and NIDDM
Mandarino, L. J., Consoli, A., Jain, A., & Kelley, D. E. (1996) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1996.270.3.e463 · Cited by 82
Brugnara, L., Vinaixa, M., Murillo, S., Samino, S., Rodriguez, M. A., Beltran, A., Lerín, C., Davison, G. W., Correig, X., & Novials, A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040600 · Cited by 84
Assessment of insulin action and glucose effectiveness in diabetic and nondiabetic humans.
Alzaid, A., Dinneen, S. F., Turk, D., Caumo, A., Cobelli, C., & Rizza, R. A. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117599 · Cited by 80
“In addition, previous investigations have shown that the effect of glucose on its own disposal in both nondiabetic humans and people with type 1 diabetes mellitus is dependent on insulin (14-16); an increment in glucose concentration results in a greater increment in glucose disposal when insulin concentrations are hi…”
BackgroundGlucose Plus Fructose Ingestion for Post-Exercise Recovery—Greater than the Sum of Its Parts?
Gonzalez, J., Fuchs, C., Betts, J., & Van Loon, L. (2017) · Nutrients · doi:10.3390/nu9040344 · Cited by 77
Kruszynska, Y. T., Harry, D. S., Bergman, R. N., & McIntyre, N. (1993) · Diabetologia · doi:10.1007/bf00400692 · Cited by 71
“The model assumes: (1) that glucose inhibits HGO and increases tissue glucose utilisation in proportion to its concentration in plasma [16-19]; (2) that insulin enhances these effects of glucose; and (3) that the effect of insulin to promote glucose disappearance from plasma depends on the concentration of insulin in…”
MethodBak, J. F., Møller, N., Schmitz, O., Saaek, A., & Pedersen, O. B. (1992) · Diabetologia · doi:10.1007/bf00429100 · Cited by 72
“It appears that acute elevations of plasma glucose do not interfere with insulin activation of muscle GS in normoglycaemic healthy control subjects [36, 38 ] whereas chronic hyperglycaemia in diabetic patients may be important for insulin stimulation of GS [34, 35, 39].”
BackgroundMoniruzzaman, M., Rokeya, B., Ahmed, S., Bhowmik, A., Khalil, M. I., & Gan, S. H. (2012) · Molecules · doi:10.3390/molecules171112851 · Cited by 71
“Glycogen is the primary intracellular storable form of glucose and its levels in various tissues are a direct reflection of insulin activity because insulin promotes the activity of intracellular glycogen synthase and inhibits glycogen phosphorylase [41,42].”
BackgroundVaag, A. A., Damsbo, P., Nielsen, O. H., & Beck‐Nielsen, H. (1992) · Diabetologia · doi:10.1007/bf00400856 · Cited by 67
“It was previously shown that hyperglycaemia per se does not stimulate the fractional activity of glycogen synthase in muscle biopsies from normal subjects during somatostatin infusion [ 42 ] or in Type 1 (insulin-dependent) diabetic subjects [43].”
BackgroundInsulin increases near-membrane but not global Ca 2+ in isolated skeletal muscle
Bruton, J. D., Katz, A., & Westerblad, H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3281 · Cited by 68
Xirouchaki, C. E., Mangiafico, S. P., Bate, K. L., Ruan, Z., Huang, A. M., Tedjosiswoyo, B. W., Lamont, B. J., Pong, W., Favaloro, J. M., Blair, A. R., et al. (2016) · Molecular Metabolism · doi:10.1016/j.molmet.2016.01.004 · Cited by 69
Syed, N., & Khandelwal, R. L. (2000) · Molecular and Cellular Biochemistry · doi:10.1023/a:1007159422667 · Cited by 69
Giebelstein, J., Poschmann, G., Højlund, K., Schechinger, W., Dietrich, J. W., Levin, K., Beck‐Nielsen, H., Podwojski, K., Stühler, K., Meyer, H. E., et al. (2012) · Diabetologia · doi:10.1007/s00125-012-2456-x · Cited by 68
“Thus, activity of PYGM was not found to be different in muscle from obese individuals with type 2 diabetes [11, 41] or regulated by changes in glucose or insulin levels [42].”
BackgroundAmylin activates glycogen phosphorylase in the isolated soleus muscle of the rat
Young, A. A., Mott, D. M., Stone, K., & Cooper, G. J. S. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80380-l · Cited by 66
Self-citationRossetti, L., & Hu, M. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116919 · Cited by 60
Metabolic handling of orally administered glucose in cirrhosis.
Kruszynska, Y. T., Meyer-Alber, A., Darakhshan, F., Home, P. D., & McIntyre, N. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116263 · Cited by 58
Shamoon, H., Friedman, S., Canton, C., Zacharowicz, L., Hu, M., & Rossetti, L. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117267 · Cited by 57
Crook, E. D., Zhou, J., Daniels, M. C., Neidigh, J. L., & McClain, D. A. (1995) · Diabetes · doi:10.2337/diab.44.3.314 · Cited by 57
“Hyperglycemia has been shown to decrease GS activity in normal rats (28), but glucose does not modulate GS activity in normal human subjects (29).”
BackgroundEffects of Insulin on Subcellular Localization of Hexokinase II in Human Skeletal Muscle in Vivo
Vogt, C., Yki-Järvinen, H., Iozzo, P., Pipek, R., Pendergrass, M., Koval, J., Ardehali, H., Printz, R. L., Granner, D. K., DeFronzo, R. A., et al. (1998) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.83.1.230 · Cited by 58
“The time course of insulin’s activation of glycogen synthase has previously been reported ( 27 ), although to our knowledge this is the earliest demonstration of activation of glycogen synthase by insulin in human muscle.”
BackgroundRitz, P., Krempf, M., Cloarec, D., Champ, M. M. J., & Charbonnel, B. H. (1991) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/54.5.855 · Cited by 54
VILLAR‐PALASI, C. (1991) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(91)90109-b · Cited by 54
3 Action of insulin on glucose metabolism in vivo
Yki‐Järvinen, H. (1993) · Baillière s Clinical Endocrinology and Metabolism · doi:10.1016/s0950-351x(05)80239-3 · Cited by 52
Self-citationFournier, P. A., Bräu, L., Ferreira, L. D. M. C.-B., Fairchild, T., Raja, G., James, A., & Palmer, T. N. (2002) · Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology · doi:10.1016/s1095-6433(02)00254-4 · Cited by 51
Vind, B. F., Birk, J. B., Vienberg, S. G., Andersen, B., Beck‐Nielsen, H., Wojtaszewski, J. F. P., & Højlund, K. (2012) · Diabetologia · doi:10.1007/s00125-012-2482-8 · Cited by 52
“Our results are in line with an earlier study of the effect of hyperglycaemia in healthy individuals [36].”
MethodResultInfluentialHuman embryonic stem cells: Possibilities for human cell transplantation
Liew, C.-G., Moore, H. D. M., Ruban, L., Shah, N., Cosgrove, K. E., Dunne, M. J., & Andrews, P. W. (2005) · Annals of Medicine · doi:10.1080/07853890500379463 · Cited by 49
Role of impaired intracellular glucose metabolism in the insulin resistance of aging
Gumbiner, B. M., Thorburn, A. W., Ditzler, T. M., Bulacan, F., & Henry, R. R. (1992) · Metabolism · doi:10.1016/0026-0495(92)90296-m · Cited by 49
Regulation of hexokinase II expression in human skeletal muscle in vivo
Vogt, C., Ardehali, H., Iozzo, P., Yki-Järvinen, H., Koval, J., Maezono, K., Pendergrass, M., Printz, R., Granner, D., DeFronzo, R., et al. (2000) · Metabolism · doi:10.1053/meta.2000.6245 · Cited by 45
Self-citationAntidiabetic activity of standardized extract of Picrorhiza kurroa in rat model of NIDDM.
Husain, G. M., Singh, P. N., & Kumar, V. (2009) · PubMed · Cited by 44
Peripheral modulation of the endocannabinoid system in metabolic disease
Shrestha, N., Cuffe, J. S. M., Hutchinson, D. S., Headrick, J. P., Perkins, A. V., McAinch, A. J., & Hryciw, D. H. (2018) · Drug Discovery Today · doi:10.1016/j.drudis.2018.01.029 · Cited by 43
Munger, R., Temler, E., Jallut, D., Haesler, E., & Jp, F. (1993) · Metabolism · doi:10.1016/0026-0495(93)90169-o · Cited by 40
Insulin increases the release of endothelin in endothelial cell cultures in vitro but not in vivo
Metsarinne, K. P., Saijonmaa, O. J., Yki‐Järvinen, H., & Fyhrquist, F. (1994) · Metabolism · doi:10.1016/0026-0495(94)90270-4 · Cited by 39
Self-citationLiu, Z., Wu, Y., Nicklas, E. W., Jahn, L. A., Price, W. J., & Barrett, E. J. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00146.2003 · Cited by 36
“Consistent with a number of studies showing that physiological hyperinsulinemia activates GS in human muscle (3, 24, 45), physiological hyperinsulinemia significantly activated GS in the current study.”
BackgroundMukundwa, A., Mukaratirwa, S., & Masola, B. (2015) · Journal of Diabetes · doi:10.1111/1753-0407.12260 · Cited by 34
Henriksen, J. E., Alford, F., Vaag, A., Handberg, A., & Beck-Nielsen, H. (1999) · Metabolism · doi:10.1016/s0026-0495(99)90126-9 · Cited by 33
Ortmeyer, H. K., Bodkin, N. L., & HANSEN, B. C. (1997) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1997.272.1.e133 · Cited by 33
Insulin Stimulates Dephosphorylation of Phosphorylase in Rat Epitrochlearis Muscles
Zhang, J. N., Hiken, J., Davis, A. E., & Lawrence, J. C. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71523-8 · Cited by 33
Husain, G. M., Singh, P. N., Singh, R. K., & Kumar, V. (2011) · Phytotherapy Research · doi:10.1002/ptr.3491 · Cited by 28
“…storable form of glucose and its levels in various tissues are a direct reflection of insulin activity as insulin promotes intracellular glycogen deposition by stimulating glycogen synthase and inhibiting glycogen phosphorylase (Yki‐Jarvinen et al., 1987; Groop and Orho‐Melander, 2008).”
BackgroundSubsensitivity to insulin in adipocytes from rats submitted to foot-shock stress
Farias-Silva, E., Sampaio-Barros, M. M., do Amaral, M. E. C., Carneiro, E. M., Boschero, A. C., Kassisse, D. M. G., & Spadari-Bratfisch, R. C. (2002) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y02-104 · Cited by 28
“Moreover, insulin inhibits glycogen phosphorylase activity only in the liver (Kelley et al. 1992; Yki-Jarvinen et al. 1987; Nuttall et al. 1983; Witters and Avruch 1978; Damsbo et al. 1991; Ciudad et al. 1979).”
BackgroundKida, Y., Nyomba, B. L. G., Bogardus, C., & Mott, D. M. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115045 · Cited by 28
“We have previously reported that increased glucose flux into human muscle at constant insulin concentration fails to stimulate glycogen synthase activity (35).”
BackgroundSelf-citationPost-exercise recovery for the endurance athlete with type 1 diabetes: a consensus statement
Scott, S. N., Fontana, F. Y., Cocks, M. S., Morton, J. P., Jeukendrup, A. E., Dragulin, R., Wojtaszewski, J. F. P., Jensen, J., Castol, R., Riddell, M. C., et al. (2021) · The Lancet Diabetes & Endocrinology · doi:10.1016/s2213-8587(21)00054-1 · Cited by 31
Flux control in the rat gastrocnemius glycogen synthesis pathway by in vivo13C/31P NMR spectroscopy
Chase, J. R., Rothman, D. L., & Shulman, R. G. (2001) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2001.280.4.e598 · Cited by 28
“The low flux control coefficient of GSase seems paradoxical, given the known increase in GSase activity with insulin concentration (7, 35, 39).”
BackgroundResultGlucose-6-phosphate stimulation of human muscle glycogen synthase phosphatase
Okubo, M., Bogardus, C., Lillioja, S., & Mott, D. M. (1988) · Metabolism · doi:10.1016/0026-0495(88)90196-5 · Cited by 27
Self-citationFurukawa, F., Irachi, S., Koyama, M., Baba, O., Akimoto, H., Okumura, S., Kagawa, H., & Uchida, K. (2018) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2018.07.003 · Cited by 26
Richter, E. A. (1996) · Comprehensive physiology · doi:10.1002/cphy.cp120120 · Cited by 27
Insulin resistance in skeletal muscles of patients with diabetes mellitus
Beck‐Nielsen, H. (1989) · Diabetes/Metabolism Reviews · doi:10.1002/dmr.5610050602 · Cited by 25
Johnson, A. B., Argyraki, M., Thow, J. C., Broughton, D., Jones, I. R., & Taylor, R. (1990) · Diabetic Medicine · doi:10.1111/j.1464-5491.1990.tb01417.x · Cited by 23
Bak, J. F., Møller, N., Schmitz, O., Richter, E. A., & Pedersen, O. B. (1991) · Metabolism · doi:10.1016/0026-0495(91)90011-k · Cited by 23
Insulinopenia and hyperglycemia influence the in vivo partitioning of GE and SI
Christopher, M., Rantzau, C., Ward, G. M., & ALFORD, F. P. (1995) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1995.268.3.e410 · Cited by 22
�rskov, L., Bak, J. F., Abildg�rd, N., Schmitz, O., Andreasen, F., Richter, E. A., Skj�rb�k, C., & M⊘ller, N. (1996) · Diabetologia · doi:10.1007/bf00403967 · Cited by 22
“05) in our study cannot account for the pronounced suppression of glycogen synthase activity and non-oxidative glucose disposal [36, 55].”
BackgroundJohnson, A. B., Argyraki, M., Thow, J. C., Jones, I. R., Broughton, D., Miller, M. A., & Taylor, R. (1991) · Diabetic Medicine · doi:10.1111/j.1464-5491.1991.tb01580.x · Cited by 21
Regulation of Muscle Glucose Uptake In Vivo
Mandarino, L. J., Bonadonna, R. C., McGuinness, O. P., Halseth, A. E., & Wasserman, D. H. (2001) · Comprehensive physiology · doi:10.1002/cphy.cp070227 · Cited by 19
Stem Cell Therapy to Treat Diabetes Mellitus
Liew, C. G., & Andrews, P. W. (2008) · The Review of Diabetic Studies · doi:10.1900/rds.2008.5.203 · Cited by 19
Nyomba, B. L., Freymond, D., Raz, I., Stone, K., Mott, D. M., & Bogardus, C. (1990) · Metabolism · doi:10.1016/0026-0495(90)90096-u · Cited by 17
Self-citationGluconeogenesis and glycogen metabolism during development of Pacific abalone,Haliotis discus hannai
Koyama, M., Furukawa, F., Koga, Y., Funayama, S., Furukawa, S., Baba, O., Lin, C.-C., Hwang, P., Moriyama, S., & Okumura, S. (2020) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00211.2019 · Cited by 17
Insulin Resistance in Pima Indians
Lillioja, S., & Bogardus, C. (1987) · Acta Medica Scandinavica · doi:10.1111/j.0954-6820.1987.tb05934.x · Cited by 16
Self-citationMontell, E., Arias, A., & Gómèz‐Foix, A. M. (1999) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.1999.276.5.r1489 · Cited by 16
“A lack of effect of insulin on GP activation in human muscle biopsies was also reported by YkiJarvinen and colleagues (28) when studying the effect of varying combinations of glycemia and insulinemia in vivo.”
BackgroundRegulation of glycogen breakdown by glycogen level in contracting rat muscle
Vandenberghe, Richter, E. A., & Hespel, P. (1999) · Acta Physiologica Scandinavica · doi:10.1046/j.1365-201x.1999.00506.x · Cited by 15
Metabolic and Molecular Pathogenesis of Type 2 Diabetes Mellitus
DeFronzo, R. A., Mandarino, L. J., & Ferrannini, E. (2003) · Wiley eBooks · doi:10.1002/0470862092.d0310 · Cited by 15
Pathogenesis of Type 2 Diabetes Mellitus
DeFronzo, R. A. (2018) · Endocrinology · doi:10.1007/978-3-319-45015-5_8 · Cited by 14
Determinants of insulin‐stimulated skeletal muscle glycogen metabolism in man
Schalin‐Jäntti, C., Laurila, E., Löfman, M., & Groop, L. (1995) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.1995.tb01988.x · Cited by 13
Pathogenesis of type 2 diabetes mellitus
DeFronzo, R. A. (2015) · Wiley eBooks · doi:10.1002/9781118387658.ch25 · Cited by 17
Pedersen, O. B., Nielsen, O. H., Bak, J. F., Hjøllund, E., & Beck‐Nielsen, H. (1991) · The American Journal of Medicine · doi:10.1016/0002-9343(91)90414-s · Cited by 13
Zhang, J., Wu, W., Huang, K., Dong, G., Chen, X., Xu, C., Ni, Y., & Fu, J. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.1037289 · Cited by 12
“Some studies have considered that high physiological levels of exogenous insulin and hyperglycemia could be responsible for insulin resistance in T1D patients (38, 39).”
BackgroundMingrone, G., Gaetano, A. D., Av, G., Capristo, E., Benedetti, G., Castagneto, M., & Gasbarrini, G. B. (1999) · Journal of Parenteral and Enteral Nutrition · doi:10.1177/014860719902300280 · Cited by 12
James, A. P., FLYNN, B. C., JONES, L. S., Palmer, T. N., & Fournier, P. A. (1998) · Biochemical Journal · doi:10.1042/bj3290341 · Cited by 12
Pathogenesis of Type 2 Diabetes Mellitus
DeFronzo, R. A. (2018) · Endocrinology · doi:10.1007/978-3-319-27317-4_8-1 · Cited by 11
Gliclazide and insulin action in human muscle
Bak, J. F., & Pedersen, O. B. (1991) · Diabetes Research and Clinical Practice · doi:10.1016/0168-8227(91)90009-3 · Cited by 10
(2012) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/978160805361211201010039 · Cited by 7
Zhyzhneuskaya, S. V., & Taylor, R. (2017) · Endocrinology · doi:10.1007/978-3-319-47685-8_21-1 · Cited by 8
Schmitz, O., Lund, S. A., Bak, J. F., �rskov, L., Andersen, P. H., M⊘ller, N., Rasmussen, O., Christiansen, J. S., & Pedersen, O. B. (1994) · Acta Diabetologica · doi:10.1007/bf00580757 · Cited by 7
“The effect of hyperglycaemia in stimulating GS has even been proposed as characteristic of type 2 diabetic subjects [27] since hyperglycaemia probably has no such effect on GS in normal subjects [16, 32 ].”
BackgroundDecreased insulin sensitivity and muscle enzyme activity in elderly subjects
Kruszynska, Y. T., PETRANYI, G., & Alberti, K. G. M. M. (1988) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.1988.tb01045.x · Cited by 5
이상현, & Park, D. (2014) · Exercise Science · doi:10.15857/ksep.2014.23.2.139 · Cited by 4
Resistance to Injection: 1991 RD Lawrence Lecture
Taylor, R. (1992) · Diabetic Medicine · doi:10.1111/j.1464-5491.1992.tb01744.x · Cited by 4
Metadata
- Authors
- Yki-Järvinen, H., Mott, D., Young, A. A., Stone, K., & Bogardus, C.
- Affiliations
- National Institutes of Health (US)
- ORCID
- Bogardus, C
- Venue
- Journal of Clinical Investigation
- Published
- 1987-07-01
- Volume
- 80
- Issue
- 1
- Pages
- 95-100
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC442206
- OpenAlex
- W2023027042
- Cited by
- 123
- References
- 47
- Citations by year
- 2024: 1 · 2023: 2 · 2022: 2 · 2021: 1 · 2020: 1 · 2019: 2 · 2018: 4 · 2017: 3 · 2016: 2 · 2015: 3 · 2014: 1 · 2013: 4 · 2012: 5
- FWCI
- 2.48
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Glycogen Storage Diseases and Myoclonus
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes, Cardiovascular Risks, and Lipoproteins
- Keywords
- glycogen synthase, glycogen phosphorylase, insulin, glucose disposal, skeletal muscle, glycogen synthesis, insulin resistance, enzyme dephosphorylation, hyperglycemia, dose-response relationship, forearm glucose uptake
- MeSH terms
- Adult, Blood Glucose, Enzyme Activation, Glucose, Phosphorylases, Glycogen Synthase, Humans, Insulin, Male, Muscles
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