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How Many Branched Chain Amino Acids Are There

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Amino Acid Biosynthesis And Catabolism

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Department of Physiology, Faculty of Medicine in Hradec Králové, Charles University, Šimkova 870, 50003 Hradec Králové, Czech Republic

Branched Chain Amino Acids In Cardiovascular Disease

Submission received: September 24, 2020 / Modified: October 4, 2020 / Accepted: October 7, 2020 / Published: October 11, 2020

Branched-chain amino acids (BCAAs; valine, leucine, and isoleucine) are elevated in fasting and diabetes mellitus. However, the pathogenesis has not been explained. BCAA catabolism has been shown to occur mostly in muscle due to the high activity of BCAA aminotransferase, which converts BCAAs and α-ketoglutarate (α-KG) to branched-chain ketoacids (BCKA) and glutamate. The loss of α-KG from the lemon cycle (cataplerosis) is attenuated by the conversion of glutamate to α-KG in the alanine aminotransferase and aspartate aminotransferase reactions, in which glycolysis is the main source of amino group acceptors, pyruvate and oxaloacetate. Irreversible oxidation of BCKA by BCKA dehydrogenase is sensitive to BCKA supply and NADH to NAD ratios

And acyl-CoA to CoA-SH. Decreased glycolysis and increased fatty acid oxidation, hallmarks of starvation and diabetes, are thought to cause changes in muscle leading to increased BCAA levels. The main changes include (i) impaired BCAA transamination due to reduced supply of amino group acceptors (α-KG, pyruvate and oxaloacetate) and (ii) inhibitory effect of NADH and acyl-CoA produced during fatty acid oxidation on the citric cycle and BCKA dehydrogenase. The article discusses the studies supporting the hypothesis and the pros and cons of increased BCAA concentrations.

Branched-chain amino acids (BCAAs; valine, leucine, and isoleucine) are essential amino acids that act as substrates and regulators of protein and energy metabolism and precursors of other amino acids. It has been repeatedly shown that their concentrations in blood plasma are exceptionally elevated during fasting and in diabetes mellitus type 1 (T1DM) and type 2 (T2DM) [1, 2, 3, 4, 5]. However, although elevated levels of BCAAs in starvation and diabetes have been recognized for decades and have received considerable attention, an explanation for the pathogenesis of their elevated levels is surprisingly lacking.

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In recent years, there has been an increasing number of studies on obese people that demonstrate a strong relationship between BCAA levels and insulin resistance (IR) and consider elevated BCAA levels relevant for predicting the development of T2DM [5, 6, 7]. Disorders of BCAA metabolism have also been described in other IR conditions associated with future onset of T2DM, including cancer, burns, trauma, sepsis, renal dysfunction, and fatty liver [ 7 , 8 , 9 ]. Much attention has been paid to the role of elevated BCAA levels in the etiology of IR, intervention outcomes and disease progression [10, 11].

Since transamination of BCAAs, the first step of BCAA catabolism, occurs, unlike other amino acids, in skeletal muscle [12] and several studies have shown that elevated plasma BCAA levels in fasting and diabetes are associated with increased muscle concentrations [4] , 13 , 14 , 15 , 16 ], muscles should play an important role in the pathogenesis of elevated BCAA levels in plasma and some other tissues.

Both early starvation and T1DM are associated with insulin depletion, increased proteolysis and increased BCAA oxidation in muscle [16, 17, 18, 19, 20]. It can therefore be assumed that the increased levels of BCAAs are due to an insufficient increase in their catabolism to compensate for their increased influx from muscle proteins. In T2DM, where insulin resistance is a characteristic feature and there is no significant activation of BCAA proteolysis and oxidation, the cause of increased BCAA levels should be the inhibition of their catabolism.

The aim of this article is to investigate the hypothesis that the disorder of glycolysis and the preferential use of fatty acids as an energy source, the characteristic features of starvation and both types of diabetes [21, 22, 23] are the main causes of the disorder of catabolism. BCAAs in the muscles, leading to increased levels of BCAAs in body fluids. First, I will provide a brief overview of BCAA catabolism and attempt to describe the effects of glycolysis and fatty acid oxidation on BCAA catabolism in muscle of healthy subjects. Second, I will examine the role of impaired glycolysis and increased fatty acid oxidation in the pathogenesis of elevated BCAA levels in fasting, T1DM, and T2DM.

Pdf] Branched Chain Amino Acids

BCAA catabolism has several common features. BCAA aminotransferase (BCAAT), the catalyst for the reversible transamination of BCAAs to branched-chain ketoacids (BCKAs), is the first enzyme in the catabolism of all three BCAAs. Each BCKA then undergoes irreversible decarboxylation by BCKA dehydrogenase (BCKAD) to the corresponding acyl-CoA esters. After that, catabolism diverges into separate pathways. Leucine is catabolized to acetyl-CoA and acetoacetate, valine to succinyl-CoA, and isoleucine to acetyl-CoA and succinyl-CoA. There is consensus that BCAAT and BCKAD play a major regulatory role in BCAA catabolism.

There are two isoenzymes of BCAAT, mitochondrial and cytosolic. Mitochondrial is expressed ubiquitously, cytosolic is limited to the brain, ovaries and placenta [24]. High activity of mitochondrial BCAAT is in skeletal muscle and very low expression is in liver [12]. Because the Km of BCAAT is two to four times higher than tissue BCAA concentrations [25], the rate of transamination responds rapidly to changes in tissue BCAA availability. It has been proposed that insulin exerts its effect on BCAA catabolism primarily through the regulation of protein metabolism and subsequent changes in BCAA availability [26].

The main acceptor of BCAA amino nitrogen is α-ketoglutarate (α-KG), which is converted to glutamic acid (GLU). Part of the GLU produced in the BCAAT reaction is used for GLN synthesis in an irreversible reaction catalyzed by GLN synthetase. Conversion of GLU to α-KG by alanine aminotransferase (ALT) and aspartate aminotransferase (AST) reactions, in which pyruvate (PYR) and oxaloacetate (OA) are converted to alanine (ALA) and aspartate (ASP), dampens the drain (cataplerosis) of α-KG from citric acid cycle (Krebs). Because the BCAAT and ALT and AST reactions are reversible and in equilibrium with their reactants [12, 27, 28], competition between amino donors (BCAA and GLU) and amino acceptors (BCKA, α-KG, PYR and OA) can affect the rate of transamination.

Most ALA and GLN synthesized in muscle are released into the systemic circulation, whereas most ASP is consumed in the purine nucleotide cycle and the malate-aspartate shuttle. BCKAs are released into the blood by monocarboxylate transporters or oxidized to BCKADs (Figure 1).

Bcaa Amino Acids, Bcaa Function, Benefits And Bcaa Supplement Uses

BCKAD is a mitochondrial multienzyme complex that catalyzes the irreversible decarboxylation of BCKA to branched-chain acyl-CoA esters. BCKAD activity is highest in liver, intermediate in kidney and heart, and low in muscle, adipose tissue, and brain [12]. Since BCKAD activity in muscle is much lower than BCAAT activity, most of the BCKA produced in muscle is released into the bloodstream and taken up by other tissues [12].

Long-term regulation of BCKAD activity occurs through changes in the expression of its subunits, short-term regulation of the complex occurs through reversible phosphorylation of its subunit Elα; a specific kinase inactivates and a specific phosphatase activates. The main regulatory role is performed by the BCKAD kinase, which is subject to BCKA inhibition [29]. Therefore, increased BCAA flux through BCAAT due to increased BCAA supply after protein intake or muscle protein breakdown increases the complex activity and rate of BCAA oxidation [30, 31]. In addition to phosphorylation, BCKA flux through BCKAD is inhibited by increased NADH to NAD + , acyl-CoA to CoA-SH ratios, and ATP concentration [ 12 ].

Glycolysis, the metabolic pathway that converts glucose to PYR, is activated in the postprandial state (the state following a meal that lasts approximately 4 hours) by increased glucose uptake and insulin production. Muscle tissue has been shown to take up 25-30% of an oral glucose load

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