malonyl coa insulin

That skeletal muscle may be a specific site of malonyl-CoA dysregulation is suggested by the finding of a much higher RQ across leg muscle of humans with established obesity than in lean control subjects, despite twofold higher plasma levels of FFA in the obese group (67). Obesity has classically been defined as a disorder in which, for a period of time, energy intake exceeds energy expenditure and the caloric excess accumulates as fat (33). As pictured, an increase in glucose availability would both restrain the increase in glycolysis that it causes and diminish fatty acid oxidation. In addition, it increases fat oxidation in muscle (82, 124) and the pancreatic β-cell (122) and inhibits acetyl-CoA carboxylase in fat cells (7). Increases in cytosolic citrate leading to an increase in the concentration of malonyl-CoA occur when muscle is presented with insulin and glucose, or when it is made inactive by denervation, in keeping with a diminished need for fatty acid oxidation in these situations. 5, Nutrition, Metabolism and Cardiovascular Diseases, Vol. 8 is that it allows for the cytosolic concentration of LCFA-CoA in muscle to be increased, independently or in concert, by a number of mechanisms implicated in insulin resistance. Glucose is a major player in these events. In addition, the effect on malonyl-CoA … More recently, it has become apparent that malonyl-CoA levels in muscle can also be acutely (in minutes) regulated. 292, No. R 5, Arquivos Brasileiros de Endocrinologia & Metabologia, Vol. Taken together, these observations indicate a high evolutionary conservation of this fuel-sensing protein kinase family that responds to nutrient signals in the absence of hormones. 312, No. Key events, as proposed by many others (20, 97, 113), include:1) increases in the concentrations of oxaloacetate and acetyl-CoA in the mitochondria,2) the condensation of this acetyl-CoA and oxaloacetate to form citrate, and3) the efflux of citrate into the cytosol, via the citrate transporter, in exchange for malate and possibly other anions. 4, 7 November 2016 | Endocrine Reviews, Vol. 305, No. Dyck J., Gao G., Widmer J., Stapleton D., Fernandez C. S., Kemp B. E., Witters L. A. Although the effects of ZMP are most certainly nonspecific (likely mimicking other known effects of AMP on glycolysis and glycogenolysis) (150) and are not restricted to AMPK activation, these data provide additional evidence for a cause-effect link between AMPK activation and changes in malonyl-CoA content after exercise. The malonyl CoA hypothesis. Thus a high level of malonyl-CoA could contribute to the elevated concentrations of triglyceride, diacylglycerol, and LCFA-CoA observed in many insulin-resistant muscles (91) (Table 2). 6, 1 January 2010 | American Journal of Physiology-Endocrinology and Metabolism, Vol. 9.AMP regulation of ACCβ activity and fatty acid oxidation in skeletal muscle. The site of inhibition of hepatic fatty acid oxidation by malonyl-CoA. In contrast, in tissues such as skeletal and cardiac muscle, in which the synthesis of fatty acids de novo is minimal (6), regulation of CPT I is presumably its dominant role. Cytosolic OAA can be derived from transamination of aspartate with pyruvate and as a product of the ATP CL reaction. Malonyl CoA, long chain fatty acyl CoA and insulin resistance in skeletal muscle. A malonyl-CoA fuel-sensing mechanism in muscle: effects of insulin, glucose, and denervation. The AMP-activated protein kinase. 11, 1 February 2013 | American Journal of Physiology-Regulatory, Integrative and Comparative Physiology, Vol. It is our premise that dysregulation of the malonyl-CoA fuel-sensing and signaling mechanism, resulting in an inappropriately high concentration of malonyl-CoA (i.e., high for a given cytosolic LCFA-CoA level) in muscle and other tissues, could be a contributory factor. 95, No. Am J Physiol. This further diminishes the use of glucose as a fuel, although it may actually increase glucose incorporation into glycogen (66, 97). 32, No. 290, No. Collectively, these findings suggest that activation of an AMPK, most likely the α2 isoform, mediates the inhibition of ACCβ during contraction in rat muscle. On the other hand, changes in the assayable activity of ACCα and ACCβ due to phosphorylation have been observed in skeletal and cardiac muscle and liver in response to a variety of stressful stimuli, including ischemia/hypoxia, heat shock, inhibition of oxidative phosphorylation and glucose metabolism, and, in skeletal muscle, exercise (25, 48, 61, 65, 93, 112) (Fig.9). This can occur by at least two mechanisms: one involving cytosolic citrate, an allosteric activator of ACCβ and a precursor of its substrate cytosolic acetyl-CoA, and the other involving changes in ACCβphosphorylation. 1, 1 November 2001 | Journal of Applied Physiology, Vol. Cytosolic citrate and malonyl-CoA regulation in rat muscle in vivo. 151, No. It has been suggested that such a mechanism will also be found in adipocytes (94), glucose-sensing cells in the central nervous system, and other cells in which the use of glucose as a fuel is a function of its availability (108). These include direct allosteric regulation of AMPK, direct activation of AMPKK, enhancement of AMPK phosphorylation by AMPKK, and diminution of the susceptibility of AMPK to dephosphorylation by phosphatases (48). ND, not done. In liver, activation of AMPK leads not only to a compensatory increase in fatty acid oxidation through a malonyl-CoA-dependent mechanism, but also to diminutions in the rates of fatty acid and sterol biosynthesis. 296, No. Mandarino L. J., Consoli A., Jain A., Kelley D. E. Interaction of carbohydrate and fat fuels in human skeletal muscle: impact of obesity and NIDDM. Results are means ± SE for 6–10 muscles for each condition. 134). (1).]. 66for further details). A noteworthy aspect of these studies in humans was that the experimental subjects were all undergoing a euglycemic clamp. Stapleton D., Gao G., Michell B. J., Widmer J., Mitchelhill K., Teh T., House C. M., Witters L. A., Kemp B. E. Mammalian 5′-AMP-activated protein kinase non-catalytic subunits are homologs of proteins that interact with yeast Snf 1 protein kinase. In vitro, citrate counters the inhibition of ACC caused by malonyl-CoA and LCFA-CoA (2, 42). 2, Journal of Clinical Investigation, Vol. I. Whether the ketone bodies inhibit fatty acid oxidation effectively when glucose availability is low is not known. RIGLYCERIDE AND In keeping with this notion, perfusion of a rat heart with FFAs and glucose, although it causes an increase in citrate (97), is associated with a decrease rather than an increase in the concentration of malonyl-CoA (6). 2, 1 December 2000 | Journal of Applied Physiology, Vol. During intense contraction, when both cytosolic citrate and AMP are increased, the AMP-mediated effects appear to dominate. In the latter event, it would not be accessible to CPT I, which is located in the outer mitochondrial membrane.” Whatever the explanation, it is likely that the effective concentration of malonyl-CoA that interacts with CPT I in muscle is both lower than that measured in whole tissue and subject to greater variation. 8 and Table 2). In addition, oxaloacetate, generated in the cytosol by aspartate transamination and the ATP-citrate lyase reaction, is converted to malate to enter the mitochondria, where it repletes and expands the pool of tricarboxylic acid cycle intermediates (anaplerosis). In general, insulin and glucose increase the activity of ACCα by diminishing its phosphorylation and by inducing its synthesis, and glucagon and catecholamines have the opposite effects (47, 57, 58, 147). As pictured, an increase in glucose availability would both restrain the increase in glycolysis that it causes and diminish fatty acid oxidation. 281, No. The glucose-fatty acid cycle. In H4IIE cells, insulin increased CPT-I sensitivity to inhibition by malonyl-CoA in 4 h, and sensitivity continued to increase up to 24 h after insulin addition. Recent studies (63, 86, 116, 117) suggest that regulation of ACCβ by cytosolic citrate also occurs in vivo. 115). Studies in which muscle has been made to contract by electrical stimulation of its nerve supply for 5 min have revealed that this decrease in malonyl-CoA (29, 134) is associated with a diminution in ACCβ activity that is evident within seconds and persists for upwards of an hour after the cessation of contraction (134, 140) (Fig. Because of its predominant location in skeletal and cardiac muscle, it has been proposed that ACCβ is involved in the regulation of fatty acid oxidation rather than fatty acid biosynthesis (1, 11, 45, 64, 138). (Reproduced from Ref.116). Identification and purification of an isozyme of A carboxylase from rat heart. 1). Glucose is necessary for these events because it generates both pyruvate and the NADH required to convert cytosolic OAA to malate. Human acetyl CoA carboxylase 2. Because acetyl-CoA is an activator of pyruvate carboxylase (148), the increase in acetyl-CoA generation caused by ketone bodies (104) could also increase oxaloacetate formation in the mitochondria.Fig. 47, No. It is also our hypothesis that dysregulation of the malonyl-CoA regulatory mechanism, if it leads to sustained increases in the concentrations of malonyl-CoA and cytosolic LCFA-CoA, could play a key role in the pathogenesis of insulin resistance in muscle. 298, No. 10-12, 21 July 2010 | Diabetic Medicine, Vol. Citrate is formed in the mitochondria by the reaction of acetyl-CoA and oxaloacetate (OAA). A scheme that both links malonyl-CoA to insulin resistance in skeletal muscle and accounts for the occasional presence of insulin resistance when malonyl-CoA levels are not increased (108, 114) is depicted in Fig. According to proposed scheme, fatty acid oxidation will be restrained or enhanced, at least in part, by changes in concentration of malonyl-CoA, and glycolysis by changes in activity of PFK-1. Malonyl-CoA and Fatty Acid Metabolism. doi: 10.1152/ajpendo.1999.276.6.E1030. 8, 1 January 2004 | American Journal of Physiology-Heart and Circulatory Physiology, Vol. PFK, phosphofructokinase. 6, 1 November 1999 | Journal of Applied Physiology, Vol. 3, 19 May 2006 | Molecular and Cellular Biochemistry, Vol. 2, The Journal of Korean Diabetes Association, Vol. 17, No. Ketone bodies can potentiate the effects of glucose in these settings by serving as a source of mitochondrial acetyl-CoA; indeed, in the presence of glucose they increase the concentration of acetyl-CoA in rat skeletal muscle to levels well above those produced by glucose alone (104), even though they concurrently inhibit pyruvate dehydrogenase (46). 10). 108, No. 30, No. Interestingly, AICAR also increases glucose transport in rat skeletal muscle (74), and, like exercise, it does so by a mechanism not involving phosphatidylinositol (PI) 3-kinase (50). Cr/CrP, ratio of creatine to creatine phosphate. PFK-1 is inhibited by ATP, and this inhibition is enhanced by citrate and diminished by AMP (85, 129). Epub 2019 Aug 31. 311, No. The role of LCFA-CoA in regulating ACCαactivity in liver, in vivo, has also been questioned (2, 42, 135). 2, 1 December 2002 | American Journal of Physiology-Endocrinology and Metabolism, Vol. 8, No. 2020 Mar;52(2):647-652. doi: 10.1007/s11250-019-02052-4. Concentration of ketone bodies in arterial and venous blood of human subjects during starvation. … Citrate content of liver and kidney of rat in various metabolic states and in fluoroacetate poisoning. Its role in insulin sensitivity and the metabolic disturbances of diabetes mellitus. 52, 8 October 2020 | European Journal of Science and Technology, 1 January 2017 | American Journal of Physiology-Regulatory, Integrative and Comparative Physiology, Vol. 279, No. Bokyo E. J., Leonetti D. L., Bergstrom R. W., Newell-Morris L., Fujimoto W. Y. In muscle, the question of whether citrate functions principally as an allosteric activator of ACC or a provider of the cytosolic acetyl-CoA from which malonyl-CoA is synthesized is still unresolved. 27, No. Even in the absence of extra lipid, incubation with glucosamine has been demonstrated to alter PKC distribution in rat adipocytes (32). It has been suggested that ACCβ activity is also governed by the supply of its substrate, cytosolic acetyl-CoA (11), and by the cytosolic concentration of long-chain fatty acyl-CoA (LCFA-CoA), an allosteric inhibitor (131). An alternative angle on diabetes. 9). 110, No. One of these relates to the fact that CPT I is a different protein in skeletal muscle and liver and that the muscle isoform is more sensitive to inhibition by malonyl-CoA by two orders of magnitude (IC50 0.03 vs. 2.7 mM) (70). -dependent C (P. J. Randle, P. B. Garland. 286, No. Thus we have found concurrent increases in the concentrations of malonyl-CoA, citrate, and/or malate in rat muscle after a euglycemic-hyperglycemic clamp (4–5 h) (86), a prolonged glucose infusion (1–4 days) (63), and brief (5 h) infusions of insulin (117). Turinsky J., O’Sullivan D. M., Bayly B. P. 1,2-Diacylglycerol and ceramide levels in insulin-resistant tissues of the rat in vivo. Other proposed mechanisms by which increases in LCFA-CoA could lead to insulin resistance include alterations in protein acylation, membrane fluidity (94, 108, 114), gene transcription and hexosamine synthesis (49), and direct inhibition of enzymes such as glycogen synthase (144). We review the evidence in support of the emerging concept that malonyl-CoA and LC-CoA act as metabolic coupling factors in beta-cell signal transduction, linking fuel metabolism to insulin secretion. Saad M. J. 93, No. Witters L., Widmer J., King A., Fassihi K., Kuhajda F. Identification of human acetyl-CoA carboxylase isozymes in tissue and in breast cancer cells. Conversely, a single bout of exercise has been shown to increase insulin sensitivity in skeletal muscle in both humans (27) and experimental animals (101). Acute stimulation of glucose metabolism in mice by leptin treatment. AMPK subunits (protein or mRNA) have been detected in virtually all mammalian tissues examined to date (39, 40, 48, 75, 126). 2, 1 January 2002 | American Journal of Physiology-Regulatory, Integrative and Comparative Physiology, Vol. Odland L. M., Heigenhauser G. J. F., Lopaschuk G. D., Spriet L. L. Human skeletal muscle malonyl-CoA at rest and during prolonged submaximal exercise. In rats starved for 48 h, we have observed 1.5- to 2-fold increases in the concentration of malonyl-CoA in various muscles after 3–24 h of refeeding, but modest increases in the concentrations of citrate or malate, if any, or in the activity of ACCβ (26). 7.Effect of insulin and glucose on the disposition of LCFA-CoA in skeletal muscle. Regulation of fatty acid synthesis in isolated hepatocytes. (Adapted from Ref. 1, Annual Review of Nutrition, Vol. The notion that concurrent alterations in malonyl-CoA and cytosolic LCFA-CoA in these cells could produce signaling abnormalities that in turn cause hyperinsulinemia, impaired insulin action, and other manifestations of the insulin resistance syndrome, as well as obesity itself, has also been proposed (94, 108,114) (see Fig. We measured these events in the muscle samples and found (Fig. A similar citrate-mediated malonyl-CoA regulatory mechanism appears to exist in other tissues, including the pancreatic β-cell, the heart, and probably the central nervous system. It can provide acetyl-CoA for citrate synthesis; it is the principal source of pyruvate, required for the pyruvate carboxylase reaction in the mitochondria (134) and for the deamination of aspartate and glutamate (not shown) in the cytosol; and its metabolism in the glycolytic pathway results in the generation of the cytosolic NADH needed for the conversion of cytosolic oxaloacetate to malate (66, 106,113) (Fig. Also, in the one investigation in which it was measured (15), no increase in muscle citrate was observed. Saha A. K., Kurowski T. G., Ruderman N. B. Bai Y., Zhang S., Kim K. S., Lee J. K., Kim K. H. Obese gene expression alters the ability of 30A5 preadipocytes to respond to lipogenic hormones. 3, 1 June 2010 | American Journal of Physiology-Endocrinology and Metabolism, Vol. Palmitoyltransferase I the American Journal of Physiology-Endocrinology and Metabolism, Vol Cox,... Unexplained is the starved-fed transition hindquarter for the study of muscle Metabolism, 109 ) of.... 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