Leucine is an essential amino acid, used in the biosynthesis of proteins. Leucine is an α-amino acid, meaning it contains an α-amino group, an α-carboxylic acid group, a side chain isobutyl group, making it a non-polar aliphatic amino acid, it is essential in humans, meaning the body cannot synthesize it: it must be obtained from the diet. Human dietary sources are foods that contain protein, such as meats, dairy products, soy products, beans and other legumes, it is encoded by the codons UUA, UUG, CUU, CUC, CUA, CUG. Like valine and isoleucine, leucine is a branched-chain amino acid; the primary metabolic end products of leucine metabolism are acetoacetate. It is the most important ketogenic amino acid in humans. Leucine and β-hydroxy β-methylbutyric acid, a minor leucine metabolite, exhibit pharmacological activity in humans and have been demonstrated to promote protein biosynthesis via the phosphorylation of the mechanistic target of rapamycin; as a food additive, L-leucine is classified as a flavor enhancer.
The Food and Nutrition Board of the U. S. Institute of Medicine set Recommended Dietary Allowances for essential amino acids in 2002. For leucine, for adults 19 years and older, 42 mg/kg body weight/day; as a dietary supplement, leucine has been found to slow the degradation of muscle tissue by increasing the synthesis of muscle proteins in aged rats. However, results of comparative studies are conflicted. Long-term leucine supplementation does not increase muscle strength in healthy elderly men. More studies are needed, preferably ones based on an random sample of society. Factors such as lifestyle choices, gender, exercise, etc. must be factored into the analyses to isolate the effects of supplemental leucine as a standalone, or if taken with other branched chain amino acids. Until dietary supplemental leucine cannot be associated as the prime reason for muscular growth or optimal maintenance for the entire population. Both L-leucine and D-leucine protect mice against seizures. D-leucine terminates seizures in mice after the onset of seizure activity, at least as as diazepam and without sedative effects.
Decreased dietary intake of L-leucine promotes adiposity in mice. High blood levels of leucine are associated with insulin resistance in humans and rodents; this might be due to the effect of leucine to stimulate mTOR signaling. Dietary restriction of leucine and the other BCAAs can reverse diet-induced obesity in wild-type mice by increasing energy expenditure, can restrict fat mass gain of hyperphagic rats. Leucine toxicity, as seen in decompensated maple syrup urine disease, causes delirium and neurologic compromise, can be life-threatening. A high intake of leucine may cause or exacerbate symptoms of pellagra in people with low niacin status because it interferes with the conversion of L-tryptophan to niacin. Leucine at a dose exceeding 500 mg/kg/d was observed with hyperammonemia; as such, unofficially, a tolerable upper intake level for leucine in healthy adult men can be suggested at 500 mg/kg/d or 35 g/d under acute dietary conditions. Leucine is a dietary amino acid with the capacity to directly stimulate myofibrillar muscle protein synthesis.
This effect of leucine arises results from its role as an activator of the mechanistic target of rapamycin, a serine-threonine protein kinase that regulates protein biosynthesis and cell growth. The activation of mTOR by leucine is mediated through Rag GTPases, leucine binding to leucyl-tRNA synthetase, leucine binding to sestrin 2, other mechanisms. Leucine metabolism occurs in many tissues in the human body. Adipose and muscle tissue use leucine in the formation of other compounds. Combined leucine use in these two tissues is seven times greater than in the liver. In healthy individuals 60% of dietary L-leucine is metabolized after several hours, with 5% of dietary L-leucine being converted to β-hydroxy β-methylbutyric acid. Around 40% of dietary L-leucine is converted to acetyl-CoA, subsequently used in the synthesis of other compounds; the vast majority of L-leucine metabolism is catalyzed by the branched-chain amino acid aminotransferase enzyme, producing α-ketoisocaproate. Α-KIC is metabolized by the mitochondrial enzyme branched-chain α-ketoacid dehydrogenase, which converts it to isovaleryl-CoA.
Isovaleryl-CoA is subsequently metabolized by isovaleryl-CoA dehydrogenase and converted to MC-CoA, used in the synthesis of acetyl-CoA and other compounds. During biotin deficiency, HMB can be synthesized from MC-CoA via enoyl-CoA hydratase and an unknown thioesterase enzyme, which convert MC-CoA into HMB-CoA and HMB-CoA into HMB respectively. A small amount of α-KIC is metabolized in the liver by the cytosolic enzyme 4-hydroxyphenylpyruvate dioxygenase, which converts α-KIC to HMB. In healthy individuals, this minor pathway – which involves the conversion of L-leucine to α-KIC and HMB – is the predominant route of HMB synthesis. A small fraction of L-leucine metabolism – less than 5% in all tissues except the testes where it accounts for about 33% – is catalyzed by leucine aminomutase, producing β-leucine, subsequently metabolized into β-ketoisocaproate, β-ketoisocaproyl-CoA, acetyl-CoA by a series of uncharacterized enzymes; the metabolism of HMB i
Sululta is one of the woredas in the Oromia Region of Ethiopia. It was part of former Mulona Sululta woreda, separated for Mulo and Sululta woredas. Part of the Oromia Special Zone Surrounding Finfinne, Sululta is bordered on the south by the city of Addis Ababa, on the west by the Mulo and Mirab Shewa Zone, on the north by Semien Shewa Zone, on the east by Bereh. Towns in Sululta include Chancho, Muger Sheleko, Rob Gebeya and Segno Gebeya; this woreda is characterized by the Sululta plain, a wide, shallow valley with an elevation of 2500 meters above sea level completely surrounded by mountains with numerous small rivers which drain into the Muger. The plain is swampy with some quite large areas of open water in the rainy season, but it reverts to grazing land during the dry months; the surrounding mountainsides were covered with forest dominated by Juniperus procera, the lower slopes supported groves of Acacia, but now most of the hillsides are covered with plantations of Eucalyptus with only the odd native tree remaining, except for the groves protected by the presence of a church.
Despite being a popular destination for both foreign and domestic investment, many residents in Sululta still do not have household access to clean drinking water. This has caused mass protests to arise in Sululta in December 2015 and during the 2016 Ethiopian protests; the 2007 national census reported a total population for this woreda of 129,000, of whom 64,516 were men and 64,484 were women. The majority of the inhabitants said they practised Ethiopian Orthodox Christianity, with 94.34% of the population reporting they practised that belief, 2.76% were Protestant, 2.07% were Muslim. Based on figures published by the Central Statistical Agency in 2005, Mulona Sululta had an estimated total population of 188,124, of whom 95,156 were men and 92,968 were women. With an estimated area of 1,520.32 square kilometers, Mulona Sululta had an estimated population density of 123.7 people per square kilometer, less than the Zone average of 143. The 1994 national census reported a total population for this woreda of 133,950, of whom 66,523 were men and 67,427 women.
The two largest ethnic groups reported in Mulona Sululta were the Oromo, the Amhara. Oromiffa was spoken as a first language by 94.8%, 4.82% spoke Amharic. The majority of the inhabitants professed Ethiopian Orthodox Christianity, with 98.17% of the population reporting they practiced that belief, while 1.04% of the population said they observed traditional beliefs, the largest group of this faith in the Zone. The Kenenisa Camp, a high-altitude athletics training camp built by Olympian Kenenisa Bekele, is located in Sululta
Joseph Mazilier was a 19th-century French dancer and choreographer. He was born as Giulio Mazarini, he was most noted for his ballets Le Corsaire. He created the role of James in La Sylphide with Marie Taglioni. Marie Guy-Stéphan debuted in Mysis at the Paris Opéra when she moved in 1853 to Paris. La Gypsy La Vendetta Le Diable Amoureux Lady Henrietta, or the Servant of Greenwich Le Diable à Quatre Paquita Betty Griseldis, ou les Cinq sens Vert-vert Orfa Aelia et Mysis, ou l'Atellane Jovita, ou les Boucaniers La Fonti Le Corsaire Les Elfes Marco Spada ou La Fille du Bandit Une fête au port James in La Sylphide by Filippo Taglioni in 1832 Fernando in La Tempête by Jean Coralli in 1834 Stenio in La Gypsy in 1839 Master of the Paris Opera Ballet from 1839 until 1851. Master of the Saint Petersburg Ballet from 1851 until 1852 Master of the Paris Opera Ballet from 1852 until 1857. Master of the Lyon Ballet from 1862 until 1866 Master of ballet at the Théâtre royal de la Monnaie in Brussels from 1866 until 1867