A more general intepretar oxidation-reduction reactions is to remember that are based on the release of electrons (oxidation) and the addition of electrons (reduction) of the atoms in a molecule. The electrons are never free, they are transferred to an electron acceptor that he comes to be reduced in the process. For example, iron in the respiratory chain cytochromes undergoes reductions and oxidations terminal based on the addition or release electrons, respectively.

Free radicals and reactive oxygen species

Free radicals are chemical species that have an unpaired electron, and can therefore be regarded as highly reactive fragments of molecules. According to this concept in the biochemistry of free radicals, the major reactants in the cell are formed by oxygen radicals and their derivatives, as well as transition metals such as iron in the redox states of ferric and ferrous and copper in the cuprous and cupric.

Reactive species are known to more complex molecules that may or may not have oxygen in the reaction, can sometimes be more reactive than the same free radicals.

Some free radicals and reactive species are: molecular oxygen, hydroxyl radical, superoxide anion, organic radical, alkoxy radical, peroxyl radical, phenoxy radical, radical nitroanión, nitroxyl radical, thiyl radical, perhydroxyl radical, hydrogen peroxide, singlet oxygen, organic hydroperoxide.

Formation of free radicals and reactive species
Free radicals are formed from molecules stable by homolytic fission process and electron transfer reactions. Factors known to favor the formation of free radicals are:
a) ionizing radiation (ultraviolet, visible, thermal)
b) excess availability of transition metals
c) adverse effects of drugs and toxic chemicals
d) excess oxygen or increase in concentration
e) oxidative stress in various disease states
f) excessive leukocytosis or phagocytosis
g) interruption of the mitochondrial electron chain
h) activation of the arachidonic acid metabolism
i) fragmentation with release of heme iron
j) decrease in the antioxidant enzyme, as in malnutrition

The half-life of free radicals is from fractions of seconds and it is very difficult to quantify and requires a very complex technology. Therefore, recent guidelines are essentially directed towards the identification and evaluation of the modified molecules by free radicals and reactive species.

Lipid peroxidation
Is a phenomenon in which a reactive molecule attacks an unsaturated fatty acid in a neighboring carbon bond p, which is due to the more reactive double bond. This starts the change of the molecular structure and, a series of chain reactions which can even lead to destruction of the membranes and to form secondary products capable of inactivating the enzymes or specific groups react with proteins or interact with DNA cell.

Protein oxidation
All amino acid side chains that are part of proteins are sensitive to the action of the oxidants and free radicals. Thus, exposure of proteins to free radical generating systems leads to modifications of the tertiary structure, which may be accompanied by loss of their biological function. Since the secondary structure is set by hydrogen bonds between the links of the chain peptíticos, also in these changes are shown by the presence of free radicals and oxidants.

The consequences of protein damage by free radicals can be: a) inhibition of various enzymatic activities, b) modification of cell membranes, c) alteration of cell function, d) modifying the transport of substrates and nutrients, e) aggregation and crosslinking of hormone receptors, f) involvement of ion transport (Na + and K +) and inhibition of ATPase and Ca 2 +, g) changes in epitopes, h) changes in hormones and antibodies, i) alteration of the structure of lipoproteins.

Oxidation of carbohydrates
The oxidation of carbohydrates can lead to formation of molecules capable of reacting with the carbonyl groups of proteins, facts that occurs with the monosaccharides such as glucose, and as described in diabetes mellitus.

Pathology and free radicals

Pathological entities that is permitted to be related to actions of free radicals and reactive species are:
1. Inflammatory and immune glomerulonephritis, vasculitis, autoimmune diseases, rheumatoid arthritis.
2. Ischemic conditions: myocardial infarction, transplant rejection, freezing, Dupuytren’s contracture.
3. Reactions induced by drugs and toxins, idiopathic hemochromatosis, thalassemia and other chronic anemias, nutritional deficiencies, alcoholism
4. Radiation damage: nuclear exposure, radiation
5. Aging.
6. Alterations of erythrocytes: lead poisoning, processes of hemolysis, hemolytic anemias.
7. Pneumological Disorders: snuff smoke effects, pulmonary emphysema, pulmonary dysplasia, pneumoconiosis professionals.
8. Abnormalities of the cardiovascular system: alcoholic cardiomyopathy, atherosclerosis.
9. Nephrological disorders: nephrotic syndrome, nephrotoxicity by heavy metals.
10. Digestive disorders: hepatitis oil, pancreatitis, gastrointestinal lesions caused by NSAIDs.
11. Trastonros nervous system and muscle: vitamin E deficiency, Parkinson’s disease, brain injury hypertensive musccular dystrophy, multiple sclerosis.
12. Eye disorders: cataract, retinal degeneration, retrolental fibroplasia.
13. Integumentary disorders: injury from solar radiation, heat, porphyria, photosensitivity, contact dermatitis.

Antioxidants

Biological function antioxidant is a substance that is present in very small concentrations, reduces or prevents the oxidation of an oxidizable substrate to act as a powerful reducing agent. Can be regarded as an electron donor capable of preventing a chain reaction of oxidation-reduction.

Antioxidants, as the mechanism of action, are classified as: a) prevention b) secondary.
a) preventive antioxidants act at the beginning of a chain oxidation, such as reducing organic and inorganic peroxides: enzymes, glutathione peroxidase, catalase and peroxidase.
b) secondary antioxidants blocked at some stage in the chain oxidation, once started, to scavenge free radicals: vitamins E and C, the enzyme superoxide dismutase.

Antioxidants according to their chemical structure and biological function are classified.
a) enzymes: glutathione peroxidase, catalase and superoxide dismutase.
b) non-enzymatic compounds: vitamins C and E, carotenoids, flavonoids, phenols, polyphenols, phytoestrogens, selenium and manganese lipoic acid, CoQ10.

Disease and Antioxidants
There are several pathological entities that are believed to be related and be able to benefit by the action of antioxidants. The most studied have been
a) cardiovascular disease. It has long been thought that the disease begins with the oxidation of free radicals in LDL cholesterol.
b) Cancer. A fundamental alteration common to all cancers is DNA damage, and antioxidants are part of the protection that minimizes this damage.
c) Changes of vision. Two eye diseases are partly due to the action of free radicals, which are cataracts and macular degeneration. A number of studies suggests that a diet rich in antioxidants help in preventing these diseases.
d) Aging. One of the theories that are supported as a cause of aging is the action of free radicals. Until now there has been no positive events with the use of antioxidants in the prevention of the involution of the human being.

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Much of the dietary lipids are found as triglycerides. On average, 40% of energy requirements of the diet of humans in industrialized countries are provided by the triacylglycerols, which are hydrolyzed in the intestine to fatty acids and monoacylglycerols, molecules that are absorbed, and transported reesterifican blood reaching the liver and adipose tissue.

Absorption of triacylglycerols
In the cells of the intestinal mucosa triacylglycerols, diacylglycerols, monoacylglycerols, glycerol and free fatty acids are converted into triacylglycerols and bind to cholesterol in the diet, along with a specific protein to form chylomicrons. These compounds, which contain apolipoprotein C-II (apo C-II), leaving the intestinal mucosa into the lymphatic system, enter the blood and reach the muscle and adipose tissue.

In the capillaries of these tissues the enzyme lipoprotein lipase is activated by apo C-II, which hydrolyzes the triacylglycerols to free fatty acids and glycerol, both products picked up by the cells in tissues.

In muscle, fatty acids are oxidized for energy, and adipose tissue for storage as reesterifican triacilgliceroles.Los chylomicron remnants, which contain cholesterol and apolipoproteins apo E and apo B-48 and is conveyed by the blood reaching the liver . This body can be oxidized to provide energy or as precursors of ketone bodies.

Fatty acids
De novo synthesis of fatty acids takes place from acetyl coenzyme A (CoA) in the extramitochondrial space, by a gupo of synthetases. This process is governed by the enzyme acetyl-CoA carboxylase, which converts acetyl-CoA to malonyl-CoA. A number of units of malonyl-CoA are added in a fatty acid chain to terminate in the formation of palmitic acid (C16: 0). From this time, elongation and desaturation, fatty acids are created more complex. Humans do not possess enzymes capable of inserting points of unsaturation in places less than the n-7 carbons, for which reason the n-6 fatty acids and n-3 essential.

Faced with energy requirements, the hormones adrenaline and glucagon stimulate deposits of adipose tissue triacylglycerols to release fatty acids, which are transported to other tissues such as muscle and kidney cortex, where they can be oxidized. The transport is performed in conjunction with serum albumin, which then dissociate, and diffuse into the cell cytosol. Since enzymes that oxidize fatty acids are found within mitochondria, previously have to pass the mitochondrial membrane transport is performed by three reactions in which enzymes are involved: a) acyl-CoA synthase, carnitine acyltransferase I and carnitine aciltranferasa II.

Beta-oxidation of fatty acids
The fatty acid oxidation produces acetyl-CoA and preferably takes place in the mitochondria. During this process, the fatty acid chain undergoes a cyclic degradation in 4 phases: dehydrogenation, hydration, dehydrogenation and fraccinamiento. These four phases of oxidation are repeated until the fatty acid is completely degraded to acetyl-CoA. Fatty acids of 18 or less carbon atoms enter the mitrocondria through carnitine transport. The medium or short chain not require the presence of carnitine for penetrating into the mitochondria for oxidation.

Beta oxidation is also carried out in peroxisomes by a process similar to that which takes place in the mitochondria, but not identical. Is carried out in chain fatty acids of more than 18 carbon atoms. In peroxisomal oxidation, the initial desaturation is performed by means of acyl-CoA oxidase, whereas in the mitochondrial oxidation is the first enzyme acting acyl-CoA dehydrogenase. There are also other differences between the two types of oxidation, since peroxisomal beta-oxidation is not related to the electron transfer chain. Thus, in the peroxisonas, electrons produced during the initial phase oxidation is transferred directly to molecular oxygen. The oxygen generated hydrogen peroxide is degraded to water by catalase. The energy produced in the second oxidation step is kept as high energy electrons from NADH:

The metabolic state of the organism influences the speed of fat oxidation. Situations such as hunger and promote long-term exercise increased lipolysis and oxidation. Conversely, increased glucose and insulin levels limit it.

Eicosanoids
Eicosanoids are derived from fatty acids n-3 and n-6, which have 20 carbon atoms. Include prostaglandins (PGs), thromboxanes (TXs), leukotrienes (LTs), hydroxy acids and lipoxins (LXs). Prostaglandins and thromboxanes are generated by the action of cyclooxygenase enzymes, leukotrienes, hydroxy acids, lipoxins, by lipoxygenase (LO).

In the synthesis of eicosanoids are obtained from: a) the path of linoleate: prostanoids PGE-1, PGF-1, TXA-1 and LTA-3 leukotrienes, LTC-3, LTD-3, b) arachidonate: prostanoids PGD-2, PGE-2, PGI-2, TXA-2, leukotriene LTA-4, LTB-4, LTC-4, LTD-4, LTE-4 and lipoxins LXA-4, LXB-4, LXC -4, LXD-4, LXE-4, c) alpha-linolenate: prostanoid-3 PGD, PGE-3, PGF-3, PGI-3, TSA-3 and leukotrienes: LTA-5, LTB-5, LTC- 5.

Eicosanoids produced a wide range of biological effects on the inflammatory response in joints, skin and eyes on the intensity and duration of pain and fever, and on reproductive function. Play also an important role in the inhibition of acid secretion in the stomach, blood pressure relulan through vasodilation or vasoconstriction and inhibit or activate platelet aggregation and thrombosis

Cholesterol Biosynthesis
Cholesterol synthesis should control it carefully to prevent abnormal deposit in the body, especially if it occurs in the coronary arteries.

Less than half of cholesterol from the body comes from the de novo biosynthesis. The liver performs approximately 10%, and intestine to 15% of the total amount of each day. The synthesis of cholesterol is carried in the cytoplasm and in microsomes from two carbons of the acetate group of acetyl-Co A.

The process takes place in five main steps: 1. Acetyl-CoA is converted to 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA). 2. HMG-CoA is converted to mevalonate. 3. Mevalonate is converted to the base molecule isoprene, isopentenyl pyrophosphate (IPP), with the loss of CO2. 4. IPP is converted to squalene. 5. Squalene is converted to cholesterol.

Acetyl-CoA used for the biosynthesis of cholesterol is derived from an oxidation reaction (fatty acid or pyruvate), which takes place in the mitochondria, but is then transported to the cytoplasm. Acetyl-CoA can also come from cytoplasmic ethanol oxidation by acetyl-CoA synthetase. All reactions of reduction of cholesterol synthesis using NADPH as a cofactor.

Isoprenoid compounds of the biosynthesis of cholesterol can be from other synthesis reactions, such as dolichol, or of coenzyme Q

Units are converted to acetyl-CoA to mevalonate by a series of reactions beginning with the formation of HMG-CoA. The steps and the enzymes are as follows. Two moles of acetyl-CoA are condensed in a reversal of the thiolase reaction, forming acetoacetyl-CoA. Acetoacetyl-CoA and a third mole of acetyl-CoA is converted to HMG-CoA by the action of HMG-CoA synthase. HMG-CoA to mevalonate is converted by HMG-CoA reductase. HMG-CoA reductase requires NADPH as cofactor and two moles of NADPH consumed during the conversion of HMG-CoA to mevalonate. The reaction catalyzed by HMG-CoA reductase is a limiting step in cholesterol biosynthesis, this enzyme is subject to complex regulatory controls.

Mevalonate is then activated by three successive phosphorylations, giving 5-pyrophosphomevalonate. Phosphorylations maintain its solubility, because it is a water insoluble compound. Upon phosphorylation, a decarboxylation, ATP-dependent, given isopentenyl pyrophosphate, IPP, isoprenoid molecule activated. Isopentenyl pyrophosphate is in equilibrium with its isomer, dimethylallyl pyrophosphate, DMPP. One molecule of IPP condenses with another of DMPP to generate geranyl pyrophosphate, GPP. GPP then condenses with another molecule of IPP to give farnesyl pirofosfate, FPP. Finally, with NADPH, the enzyme squalene synthase catalyzes the condensation of head to tail, of the molecules of FPP, giving squalene. Squalene undergoes a two-step cyclization to yield lanosterol. The first reaction is catalyzed by squalene monooxigenase. This enzyme uses NADPH as a cofactor to introduce molecular oxygen as an epoxide at the 2,3 position of squalene. After a series of 19 additional reactions, lanosterol is converted to cholesterol.

Regulating the synthesis of cholesterol
A normal adult synthesizes approximately 1 gram per day and consumes about 0.3 grams per day. Relatively constant concentrations of cholesterol, about 150-200 mg / dL, control the synthesis de novo. The concentrations are in part regulated by dietary intake of cholesterol

Cholesterol from both diet and the synthesis is used in the formation of membranes and in the synthesis of steroid hormones and to a greater proportion of bile acids.

Cellular cholesterol intake is maintained at a stable level for three different mechanisms of regulation 1. Activity and levels of HMG-CoA reductase. 2. Excess of intracellular free cholesterol, through the activity of acyl-CoA: cholesterol acyltransferase, ACAT. 3. Plasma levels of cholesterol uptake via receptor-LDL and HDL inverse transport

Since the intracellular levels of cAMP is controlled by hormonal stimuli, regulation of biosynthesis of cholesterol is hormonally. Insulin promotes the increase of cAMP, which in turn activates the synthesis of cholesterol. Alternatively, glucagon and epinephrine, with increasing levels of CCAMP, inhibit cholesterol synthesis.

The long-term control of HMG-CoA actividadad reductase principalmentee performed through the synthesis and degradation of the enzyme by hormonal stimuli for expression of its genes. Also, the rate of production of the enzyme HMG-CoA cholesterol depends on the input, if high, increases the degradation of the enzyme.

Lipoproteins
Cholesterol is transported in plasma predominantly as cholesterol esters together with lipoproteins. Dietary cholesterol is the small intestine to the liver within chylomicrons, the synthesized in this body, as well as the dietary needs exceeds the liver, serum is transported inside LDLs. The liver synthesizes these VLDLs and LDLs are converted into particles by the action of endothelial cells together with lipoprotein lipase.

The cholesterol found in the plasma membranes can be extracted by HDLs and esterified by the enzyme LCAT, HDL-associated. The captured in peripheral tissues by HDLs can then be transferred to VLDLs and LDLs, via the action of the protein transfer of cholesterol ester (APOD) associated with HDLs. The reverse cholesterol transport allows peripheral cholesterol back to the liver in LDLs.

Finally, cholesterol is excreted in the bile as free cholesterol or as bile salts following conversion in the liver, bile acids.

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Proteins

Protein turnover
Almost all proteins of the organism are in constant dynamic synthesis (1-2% of total protein), from amino acids, and degradation to new amino acids. This activity causes a net nitrogen loss per day in the form of urea, which corresponds to about 35-55 grams of protein. When dietary intake compensates the loss is said that the body is in nitrogen balance.

Nitrogen balance can be positive or negative. Is positive when the nitrogen intake exceeds losses, as in growth, pregnancy, recovering from illness. Is negative if the nitrogen intake is less than losses, such as in malnutrition, anorexia prolonged postraumatismos, burns, an essential amino acid deficiency.

Degradation pathways of proteins
There are two pathways by which proteins are degraded by proteases (cathepsins).

1. Ubiquitin pathway (small basic protein). Cytosolic proteins fractionated abnormal and short-lived. It is ATP dependent and is located in the cell cytosol.

2. Lysosomal pathway. Fractionated proteins long, membrane and organelles such as extracellular mitrocondrias. ATP is independent and is located in lysosomes.

Elimination of protein nitrogen
Excess amino acids the body needs to be broken, and for that the body eliminates the amino group, forming ammonia, which happens to urea (urea cycle), eliminating this element in the urine. A small amount of ammonia can pass glutamine. The primary site of amino acid degradation is the liver.

Ammonia is a highly toxic compound, and therefore it becomes the body as a non-toxic, urea. Urea characteristics favor their formation: a) small molecule, b) about 50% of their weight is nitrogen, c) low energy required for their synthesis.

Formation of urea cycle ornithine
In hepatocytes are located five reactions constituting the cycle.
1. Carbamyl-phosphate formation, irreversible step catalyzed by carbamyl-phosphate synthase I.
2. Formation of citrulline, ornithine transcarbamylase by
3. Argininosuccinate synthesis. Argininosuccinate synthase catalyzes the condensation of aspartic acid citrulline.
4. Argininosuccinate cleavage to fumarate and arginine by argininosuccinate lyase.
5. Cleavage of arginine ornithine and urea by arginase

Amino

Essential and nonessential amino acids
Amino acids are present in the body 20. Of these, 9 are essential and the other 11 are not essential.

Essential amino acids, histidine (His), valine (Val), leucine (Leu), isoleucine (Ile), lysine (Lys), methionine (Met), threonine (Thr), Phenylalanine (Phe), tryptophan (Trp).

Histidine and arginine are considered essential during periods of rapid cell growth (infancy and childhood)

Nonessential amino acids, and can be synthesized by the body: tyrosine (Tyr), glycine (Gly), alanine (Ala), cysteine ??(Cys), serine (Ser), aspartic acid (Asp), asparaguina (Asn), acid glutamic acid (Glu), glutamine (Gln), arginine (Arg), proline (Pro).

Reactions in the metabolism of amino acids
The two main reactions in the metabolism of amino acids are: transamination and oxidative deamination

Transamination
This is a process, performed in the cytosol and mitochondria, which becomes an amino acid other. Is performed by means of transaminases that catalyze the transfer of alpha-amino group (NH3 +) of an amino acid to an alpha-keto acid, such as pyruvate, oxaloacetate or more alpha-ketoglutarate frequently. Consequently, creates a new amino acid and a new ketoacid.

Transaminases most commonly involved in transamination are: alanine aminotransferase (ALT) and aspartate aminotransferase (AST). Require, as a cofactor, pyridoxal phosphate (PLP), a derivative of vitamin B6.

Oxidative deamination
Process, performed in the mitochondria, and in which the enzyme glutamic acid dehydrogenase removes the amino group of glutamic acid. Ammonia is formed enters the urea cycle and the carbon skeletons are to be glycolytic intermediates and the Krebs cycle.

The products of deamination of amino acids are:
Amino acid (s) photoproduct

Ile, Leu, Lys-CoA fotoAcetil

Tyr, Phe fotoAcetoacetato

Gln, Pro, Arg and alpha-ketoglutarate fotoGlu

His fotoGlu and alpha-ketoglutarate

Thr, Met, Val-CoA fotoSuccinil

Tyr, Phe, Asp fotoFumarato

Asp, Asn fotoOxaloacetato

Ser, Gly, Cys fotoPiruvato

Trp fotoAlanina and pyruvate

Amino acid synthesis
The synthesis of amino acids except cysteine ??and tyrosine, is attached to the tricarboxylic acid cycle (TCA) or by transamination or by fixing the ammonium. The alpha-amino group is central to all synthesis of amino acids and ammonium derived from the amino groups of L-glutamate. Of these are synthesized glutamine, proline and arginine. Glutamic acid is the primary source of amino groups to the transamination.
Cysteine ??is formed in the cell cytosol, from serine and the essential amino acid methionine.
Tyrosine is formed by hydroxylation of the essential amino acid phenylalanine hydroxylase for phenylalanine.

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The concentrations of blood glucose in adults are usually between 72.0 – 99.0 mg/100 mL (4.0-5.5 mmol / L). But when you eat a meal containing carbohydrates, blood glucose may rise to 135.0 mg / 100 mL, for a certain period of time. In one phase of fast, can be as low as 54.0 – 63.0 mg/100 mL. If blood sugar levels are around 180.0 mg / 100 mL, as in diabetes mellitus, or higher levels, as some individuals in serious pathological conditions, comes to appear glucose in the urine (glycosuria).

There are several processes involved in carbohydrate metabolism, which are presented below.

Glycolysis
Glycolysis is called a set of enzymatic reactions in metabolize glucose and other sugars, releasing energy in the form of ATP. Aerobic glycolysis, which is performed in the presence of oxygen, producing pyruvic acid, and anaerobic glycolysis in the absence of oxygen, lactic acid.

Glycolysis is the major route for the utilization of the monosaccharides glucose, fructose and galactose, which are important energy sources in diets containing carbohydrates. Postabsortiva during the glucose must also from other sources. After intestinal absorption process, the sugars glucose, fructose and galactose are transported by the portal vein to the liver, where fructose and galactose are rapidly converted into glucose. Fructose can enter directly in the pathway of glycolysis.

Glycolysis is carried out in the cytosol of all cells. Although many different reactions catalyzed by enzymes, glycolysis is regulated primarily by three enzymes hexokinase, phosphofructokinase and pyruvate kinase, which intervene in the step of hexoses to pyruvate. Under aerobic conditions pyruvate is transported into the mitochondria, by a conveyor, where it is decarboxylated to acetyl CoA which enters the citric acid cycle. Under anaerobic conditions, pyruvate is converted to lactate, which is tranportado the liver, where it mediates the process of gluconeogenesis, and passed back into the circulation to intervene in the oxidation of the tissues and lactic acid cycle, or Cori.

Oligosaccharides and polysaccharides not digested and not absorbed in the small intestine reach the bulk where they are hydrolyzed to monosaccharides by enzymes secreted by bacteria membrane, the monosaccharides are converted to pyruvate, which is immediately metabolized to short chain fatty acids such as acetate, propionate, butyrate, and gases such as carbon dioxide, methane and hydrogen.

Gluconeogenesis
Gluconeogenesis is the formation of carbohydrates from fatty acids and proteins, rather than carbohydrate. Involved addition of pyruvate, amino acids and other substrates such as glycerol. It takes place in the cytosol of liver cells and involves the enzyme glucose-6-phosphatase, fructose 1,6-bisphosphatase and phosphoenolpyruvate carboxykinase, instead of hexokinase, phosphofructokinase and pyruvate kinase, respectively, which is the latter enzymes involved in glycolysis.

The amino acid alanine, transported from muscle to liver, can be converted into glucose.

In adipose tissue, acylglycerols, by hydrolysis, continuously pass free glycerol, which reaches the liver where it initially becomes fructose 1,6-bisphosphate and then into glucose.

Glycogen
Glycogen is a polysaccharide, formed from glucose. In animals, when glucose exceeds circulating levels and is not used as a source of energy is stored as glycogen, preferably in liver and muscle. The main function of glycogen in the liver, is to provide glucose when it is available from dietary sources. In muscle provides immediate metabolic fuel inputs.

Glycogenolysis
Glycogenolysis is the process by which glycogen is converted into glucose. If the glucose is deficient, the glycogen is hydrolyzed by the action of debranching enzymes and phosphorylase, producing glucose-1-phosphate, which becomes, via phosphoglucomutase, glucose-6-phosphate, which by action of glucose-6-phosphatase, leaves the cell as glucose, after passing pre-glucose-1-phosphate and glucose-6-phosphate

Glycogenesis
It is the reverse process of glycogenolysis. Glycogen pathway occurs in the cell cytosol and in it are required: a) three enzymes, which are uridine diphosphate (UDP)-glucose pyrophosphorylase, glycogen synthase and branching enzyme, amilol (1.4 -> 1.6) transglycosylase, b) donor glucose, UDP-glucose, c) a primer to initiate synthesis of glycogen if there is a preexisting glycogen molecule, d) energy

Regulation of glycogen metabolism
It is a very complex and still poorly known. It is necessary to consider two levels: allosteric and hormonal. The allosteric control depends primarily on the actions of the enzyme glycogen phosphorylase and synthase. At hormone adrenaline into the muscle and liver, and glucagon, only in the liver, stimulate the division of glycogen. Although insulin action is not well known, being an anabolic hormone is assumed that stimulates synthesis and inhibits breakdown of glycogen.

Glycogen storage diseases or tesaurismosis
A number of inherited defects in metabolism leading to a disease, for enzymatic alteration, which is detected glycogen storage. Known 9 different types of diseases:

I. Von Gierke disease
Deficient enzyme: glucose-6-phosphatase
Allocation: liver and kidney. Clinical hepatomegaly, impaired growth, hypoglycemia
II. Pompe disease
Deficient enzyme: alpha-(1 -> 4)-glucan-6-glucosiltrasferasa
Allocation: liver, heart and muscle. Clinical cardiopulmonary insufficiency can be fatal before 2 years of age.
III. Cori Disease
Deficient enzyme: amyl-(1 ->)-glucosidase
Allocation: liver and muscle. Clinical hepatomegaly, impaired growth, hypoglycemia, although with less intensity than in type I
IV. Andersen disease
Deficient enzyme: amyl-(1 -> 4, 1 -> 6)-glucosyltransferase
Allocation: liver. Clinical liver cirrhosis can be fatal before 2 years of age.
V McArdle disease
Deficient enzyme: phosphorylase
Involvement: muscle. Clinic: fatigue and muscle weakness
VI. Hers Disease
Deficient enzyme: phosphorylase
Allocation: liver. Clinical hepatomegaly, impaired growth, hypoglycemia, although with less intensity than in type I
VII. Phosphofructokinase deficiency disease
Deficient enzyme: phosphofructokinase.
Involvement: muscle. Clinic: fatigue and muscle weakness
VIII. Tarui disease
Deficient enzyme: fosforilasacinasa
Allocation: liver. Clinical hepatomegaly, impaired growth, hypoglycemia, but with less intensity than in type I.
IX. Deficiency disease hepatic glycogen synthase
Low concentrations of the enzyme glycogen biosynthesis perform some

Via the pentose phosphate
The route of the pentose phosphate pathway, also known as fosfoglucanato is an alternative to glucose metabolism. It takes place in the cytoplasm of liver cells, mammary glands during lactation, adipose tissue, adrenal glands and red blood cells.

The main functions of this pathway are:
a) production of NADPH, this pathway is not consumed, nor produces ATP. Both NADP and NADPH are considered high energy molecules in which the electrons are used for reducing synthesis reactions.
b) production of ribose for the synthesis of nucleotides and nucleic acid.
c) regenenación in red blood cells, the reduced form of glutathione, an antioxidant.

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Dietary therapy can be understood as a pyramid. At the base metabolic settle the biochemical basis of the human body, essential nutrients and their dynamics interrelaciones.El component is formed immediately above the needs of the life cycle of various nutrients in relation to growth, development, maturation and maintenance. Finally, at the apex of the pyramid is therapeutic nutrition, considering the changes that an individual needs specific treatment for their disease.

Therefore, the principles of dietary therapy in humans have significance only in terms of a normal nutrition. The diet is established only when there is a specific disease that can be solved by understanding what it means normal nutrition and metabolism.

The establishment of a diet needs, therefore, accommodate the following questions:
Disease. How the disease affects the body and its normal metabolic functioning?
How dietary therapy and why the diet should be modified in terms of nutritional components to meet the needs caused by that particular disease?
How these dietary guidelines necessary nutritional changes affect daily food choice?.

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Congenital metabolic defects leading to a wide range of diseases, relatively rare, occurring as a consequence of inherited deficiencies of particular proteins with enzymatic function, transport, structural, receiver, etc..

Many patients suffering from congenital metabolic disorders can receive various treatments helpful. In some cases the benefit is relatively insignificant, but many others can be achieved very favorable results. The basis of many treatments is essentially nutritional.

According to Aquino Sanjurjo P and L (Nutrition and inborn errors of metabolism, in: Diagnosis and Treatment of Inherited Metabolic Disease. Eds Sanjurjo P and A Baldellou, Ed Ergon, 2001), “Nutrition is the most important therapeutic tool for this type pathology, waiting for gene therapy, and that in a poetic way, these real biological models, which are inborn errors of metabolism will return the favor to the general nutrition, giving important insights achieved through both empiricism as binomial nutrition research / EIM. “

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Most organic diseases in which nutritional factors play an important role, have genetic and environmental determinants. But at present, are not clearly characterized all environmental risk factors, and not yet identified the most susceptible genotypes. Moreover, not yet fully aware of the possible relationships between genetic and environmental mechanisms, in the development of disease. It is clear that dietary factors are important in the etiology of various organic diseases and that dietary modifications can reduce the risk. However, for most diseases is not yet possible to estimate quantitatively, not only the total risk, but also the benefits.

It is well known that many diseases negatively alter the nutritional status of an individual. The facts known and most studied are those observed in infections, or surgical observed in body mass loss of certain nutrients, as well as redistribution of the components relative to other elements. In the case of an early cure, the mass of nutrients lost, consisting of proteins, sugars, fats., Electrolytes, etc.. normality can be restored with organic deposits and reserves are filled up to the normal values, a solution that can last, sometimes weeks or even months.

In processes of chronic or progressive, the facts do not happen the same way and so favorable. Body composition is altered significantly and need a new equilibrium on the balance sheets of the various components of an organism, often cachectic and devoid of sufficient amounts of nutrients that can restore the lost material. In a number of diseases, the facts are further complicated by the actions antinutritional with some types of treatment, as the disease itself that creates in the patient decreased appetite, digestive and absorptive intestinal difficulties, along with metabolic and hormonal .

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Arginine

Is a basic amino acid. It is synthesized from glutamate, after passing through by ornithine.

The main features of arginine are
a) Participate in the reactions called the urea cycle, designed to pack ammonium ions generated during the fractionation normal body protein. The ammonium ion is excreted as an element toxic to the nervous system.
b) A small fraction of arginine in the formation of nitric oxide (NO), a product that acts in controlling blood pressure and other arterial functions.
c) Arginine can be synthesized de novo in the liver and to a lesser extent in the kidney and lymphocytes.
d) arginine requirements are high in conditions of high protein degradation (sepsis, trauma).
e) Arginine plays a pivotal role in maintaining the immune response.
f) Solutions arginine-free parenteral nutrition originate hyperammonemia, metabolic acidosis and coma.
g) arginine supplementation increases the weight of the thymus and of lymphocytes and delayed hypersensitivity reactions.
h) Dietary supplements of arginine inhibit tumor growth in experimental animals.
i) Arginine accelerates the healing of wounds and enhances energy expenditure in hypermetabolic states.
j) Arginine causes the secretion of HGH and insulin action shared with ornithine.

Carnitine

It is a necessary cofactor for the transport of long chain fatty acids in mitochondria, and hence play an essential role in oxidative metabolism, and ketone body formation.
Unlike other cofactors, carnitine is a vitamin derivative.
Free carnitine concentrations in muscle is about 4.0 mmol / kg.

Some features of carnitine:
a) carnitine requirements are satisfied by endogenous synthesis in the liver and kidney from lysine and methionine, and the diet.
b) The typical Western diet provides about 100 mg of carnitine per day. Meat and milk are good sources, beef contains about 500 mg / kg and cow’s milk 5-40 mg / kg. Eggs and vegetables contain little or no carnitine.
c) There is concern about the temporary deficiency of carnitine in infants fed carnitine-free diet (eg, soybeans). woman’s milk contains high concentrations of carnitine (50-100 nmol / mL). Newborns have a low deposit
d) Infants fed on formula milk free carnitine, have elevated plasma free fatty acids.
e) Carnitine was first detected in 1973, have since been described several cases of genetic deficiency.
f) carnitine deficiency syndromes comprising a series of:
· Progressive muscle weakness with skeletal muscle lipid infiltration, and decreased levels of muscle carnitine.
· Cardiomyopathy
· Severe hypoglycemia
· Elevated blood ammonia
· Diminished capacity of production of ketone bodies
· Association with metabolic disorders with organic aciduria or medical treatment (renal dialysis, long-term parenteral nutrition)

Glycine

Simple amino acids are glycine and alanine.
The R group of glycine is a hydrogen atom, the alanine, a methyl group.

Characteristics of glycine:
a) It is in the most abundant protein in mammals, collagen.
b) conjugated bile salts to form the bulk of modified bile salts glycine or taurine joining before being excreted by the liver.
c) It is an important precursor of creatine, porphyrins, glutathione and nucleotides.
Glycine deficiency may be responsible for poor growth of preterm infants fed breast milk supplemented with protein (ratio assessment of the state of glycine by urinary excretion of 5-oxoproline).

Glutamine

Acidic amino acids are glutamic acid and aspartic acid. These amino acids are also presented in form amides, such as glutamine and asparagine.

Some characteristics of glutamine are:
· Glutamine is the most abundant amino acid in blood (650 mmol / L).
· Except for taurine, is the largest concentration of intracellular amino acid.
· It is 61% of the amino acids of skeletal muscle.
· The concentrations of glutamine in skeletal muscle and decrease in blood diseases with high metabolism (metabolic stress, multiple trauma).
· The decline in plasma glutamine levels favors the appearance of villous atrophy and intestinal necrosis.
· The absence of total parenteral nutrition of this amino acid can cause atrophy of intestinal villi.

Taurine

Taurine is the 2-aminoethane sulfonic acid, which is synthesized from cysteine. The molecule contains one amino group and other acidic. No protein was detected, although there may in certain polypeptides.

Features:
· It is a component of bile salts and plays an important role in the transport and absorption of lipids.
· It is found in animal foods and milk, but not in plants.
· The human newborn has a limited capacity to synthesize taurine, formulas based on cow’s milk contains much less of this amino acid to human milk (25-35 mmol / dL).
· Levels were found in plasma and urinary taurine low in preterm infants.

Polyamines

Polyamines are derived from ornithine and methionine, which act as cell growth factors. Involved in the stabilization of cells, organelles and membranes as well as in protein synthesis.
· The most important polyamines: spermidine and spermine.
· Humans synthesize approximately 0.5 mmol spermine day.
· We detected high amounts of polyamines in human breast milk are undetectable in infant formula.
· The polyamines of human milk or preformed polyamines promote the development of the microflora of the large intestine.

Nucleotides

Nucleotides are products that have three distinctive components:
a) a nitrogenous base components derived from two heterocyclic
· Purines adenine (A), guanine (G)
· Pyrimidines: thymine (T), cytosine (C), uracil (U)
b) a pentose
c) one or more phosphate groups

Nucleosides: contain glycosidic bond between
pentose (ribose or deoxyribose)
Nitrogen Base

Nucleotide: phosphate esters of nucleosides
RNA and DNA (nucleic acids) constituted by nucleotide
ATP: transport of chemical energy
CAMP and cGMP: effectors of hormones in the cells
NAD, NADP, FAD, and Coenzyme A (adenine derivatives): coenzyme components.

Hill

Choline (trimetiletanolamina) is a compound of 2 carbon atoms in the body is shaped structural lipid phosphatidylcholine (lecithin).
Fosfafidilcolina and phosphatidylethanolamine are major phospholipids in cell membranes.

Features:
a) The hill is also in animal and vegetable foods.
The eggs, liver and soybeans are rich in lecithin, cauliflower and lettuce on the hill is in free form.
The daily intake of choline is about 400-900 mg (in adults).
b) Choline is part of complex molecules: in the cell membranes, lipoproteins, in the pulmonary surfactant, sphingomyelin in the nervous system and in the neurotransmitter acetylcholine.
c) The human placenta can synthesize choline de novo.
The premature infant requires a minimum contribution of choline.
Human milk provides choline as lecithin and sphingomyelin.
Infant formulas should contain choline (7 mg colina/100 kcal.)
d) may be established choline needs for patients with prolonged parenteral nutrition.
Can liver cirrhosis due to inadequate intake of choline?

Food content (mmol / kg food)
free and bound choline

SEE ANNEX 1

Myoinositol

Inositol is a cyclic alcohol, ciclohexanohexol, chemically related to glucose.
Isomers of inositol alone 9 myoinositol (inositol-1 ,2,5-triphosphate) is important in the metabolism of animals and plants.
In vegetables such as phytic acid found in animal tissues and as a constituent of cell membrane phospholipids.

Features:
a) The myoinositol is supported as an important nutrient to consider a second messenger of hormone receptor-mediated stimuli and its role in intracellular calcium mobilization.
b) myo-inositol content of the tissues derived from diet and endogenously synthesized.
c) has not been shown to be essential for humans, but some animals need to be provided in their diets.
d) Its deficiency leads to alterations in lipid metabolism.

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Previous concepts
Nucleic acids. Are complex molecules of high molecular weight containing nitrogenous bases (purines and pyrimidines), five-carbon sugar (ribose and deoxyribose) and phosphate.

Base. Can be defined as a substance which combines with acids to form neutral salts. Also, as a substance which increases the ion concentration on the contrary hidroxilo.o decreasing concentration of hydrogen ions when dissolved in water.

Purines
Are nitrogenous bases: adenine, guanine and hypoxanthine have a double structure comprising a ring of six carbon and other five-carbon ring.
Nucleosides
Purines can exist as free bases or a pentose sugar, usually ribose or deoxyribose, linked by the N9 position to form a nucleoside. For example, adenine is the free base and adenosine, the nucleoside is the free base guanine and guanosine, the nucleoside. The nucleoside of hypoxanthine called inosine.
Sugar phosphorylation C5 position results in the formation of mono-, di-and trinucleotides.
The phosphate groups make these molecules are negatively charged.

Pyrimidines
Are compounds containing heterocyclic nitrogen ring structures. Are pyrimidines: thymine, cytosine and uracil.
In pyrimidines, a carbamyl molecule in which glutamine is the donor of the amimo group, binds to an aspartic acid molecule. Orotic acid, product from these reactions is transferred to a molecule of phospho-ribosyl pyrophosphate to give rise to uridylic acid.
Nucleosides. Pyrimidines are mostly associated with five-carbon sugars to form united in N1 nucleosides

Nucleotides
Molecules composed of a phosphate group, a five-carbon sugar (ribose or deoxyribose and a nitrogenous base (flavin, purine, pyrimidine or pyridine).
Examples of nucleotides are: flavin adenine dinucleotide, adenosine triphosphate, cytosine triphosphate and nicotinamide adenine difosfosfato.

Nucleotides. Synthesis
The nucleotides are formed de novo in the cell from amino acids, ribose, phosphate and CO2. Novo route for the synthesis of nucleotides requires a relatively large supply of energy. To compensate, many cells have very efficient recovery route by which purine bases are reused or preformed pyrimidine.

Because of the way in which are synthesized or recovered nucleotides, purines and pyrimidines in the cell are mainly in the form of nucleotides. Under normal conditions, the concentrations of free bases or nucleosides are extremely small. Nucleotide levels in the cell is regulated by a series of enzymes allosterically controlled on the route.

Metabolic functions of nucleotides

All types of cells contain a variety of nucleotide derivatives. Its main functions are:

a) Participation in energy metabolism. ATP (adenosine triphosphate) is generated by phosphorylation in cells, oxidative and substrate level. Is used to activate the metabolic reactions, and is involved in processes such as muscle contraction, active transport, and maintenance of the integrity of cell membranes. ATP is a phosphate donor for the generation of other nucleoside 5′-triphosphates.
b) presence of nucleic acid monomeric units. DNA and RNA, are composed of nucleotide units. Reactions in nucleic acid synthesis, the nucleoside 5′-triphosphates are substrates which bind to the polymer by phosphodiester bonds 3′-5 ‘, releasing pyrophosphate.
c) physiological mediators of key metabolic processes. CAMP (cyclic adenine monophosphate) acts as a second messenger in the control of glycogenolysis and gluconeogenesis processes mediated by epinephrine and glucagon.
d) Components of coenzymes. NAD (nicotinamide adenine dinucleotide), FAD (flavin adenine dinucleotide) and CoA (coenzyme A) are metabolic constituents involved in many metabolic pathways.
e) activated intermediates necessary for various reactions. UDP-glucose is a key intermediate in the synthesis of glycogen and glycoproteins. GDP-mannose, GDP-fucose, UDP-galactose and CMP-sialic acid are key intermediates of reactions in which sugars are transferred to the synthesis of glycoproteins. CTP is used to generate CDP-choline, CDP-ethanolamine and CDP-diacylglycerol, compounds involved in phospholipid metabolism.
f) allosteric effectors. Intracellular concentrations of nucleotide control the regulated steps in metabolic pathways.

Alterations in the metabolism of purine

Alterations in the purine metabolism may lead to a variety of diseases:

a) drop syndrome. Produced by accumulation of uric acid crystals in joints and kidneys
b) immunodeficiencies caused by the absence of adenosine deaminase activity and nucleoside phosphorylase.
c) Lesch-Nyhan syndrome. Caused by lack the enzyme hypoxanthine-guanine-phosphoryl Transfera, the catabolic pathway of purine nucleosides.
d) gout syndrome. Deficiencies caused by glucose-6-phosphatase, and glutamate dehydrogenase, or by increasing the activity of the enzyme.

Drop

It is a disorder associated with an inborn error of uric acid metabolism that increases production or excretion queinterfiere. Excess uric acid is converted to sodium urate crsitales, which precipitate and are deposited in joints and other tissues. Process extremely painful and sometimes disabling

Gout can be primary or secondary
Primary drop is due to the absence of enzyme activity that causes overproduction of uric acid, or also to a deficit in its mechanism of excretion
Secondary drop is the result of an acquired condition in which gouty arthritis develops as a complication of hyperuricemia accompanying disease (leukemia, chronic nephritis, polycythemia, etc.).

Metabolism of pyrimidines

The catabolism of pyrimidines produces methyl-malonyl-CoA, which are broken down to carbon dioxide. Among the changes the metabolism of these nucleotides is the orotic aciduria

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In general, the physiological effects of a complete plant food are higher than those with each of the individual compounds, doubts arise when you are aware of phytochemicals or combinations thereof having a Preventica action on humans. However, certain compounds are known to provide specific health benefits, including certain antioxidant properties that protect against the effects of aging and some chronic diseases such as cancer and cardiovascular diseases.

These bioactive compounds include carotenoids, phenolics such as flavonoids and catechins, phytoestrogens such as isoflavones and lignans, glucosinolates, phytosterols, terpenoids, and saponins. For most of the phytochemicals, not yet well known, molecular, and their interactions with other dietary components.

Carotenoids

Carotenoids are the pigments responsible for color, from yellow to red, fruits and vegetables. Sources of these plants are yellow / orange of carrots, peppers and sweet potatoes, red and yellow / orange tomatoes, oranges, strawberries, apricots. The carotenoids beta-carotene, lycopene, lutein and zeaxanthin are antioxidant that protects DNA against free radical damage, and is thought to also contribute to cancer prevention, as well as providing other health benefits. Xantofílicos carotenoids, lutein and zeaxanthin appears that reduce the risk of developing certain eye conditions, especially in older people.

Epidemiological studies suggest a relationship between diet rich in lycopene and decreased occurrence of coronary heart disease and certain cancers of the prostate, stomach, uterus and lung. Of all the carotenoids, lycopene from tomato (provides the red color), is the most efficient scavenger of reactive oxygen species. This plant can serve as an example of those foods that have been observed to have more actions to those conventionally accepted nutritional.

Flavonoids

Flavonoids are a group of phenolic compounds based on the core flavone. They are found especially in fruits and vegetables, and are present mainly as glycosides. Different classes of flavonoids have potential beneficial properties, including anthocyanins, flavones, luteolin and for artichokes, flavonols, including quercetin, and flavans / tannins, catechins and proanthocyanidins as. In addition to the antioxidant capacity, some flavonoids inhibit platelet aggregation and show anti-viral, anti-bacterial, anti-inflammatory, anti-mutagenic and immuno-stimulants, which derive their beneficial effects.

Significant amounts of flavonols, catechins and tannins found in tea and wine, as well as apples, onions and broccoli. The preparation and processing of fresh fruits and vegetables can cause losses of up to 50% of the flavonoid content. At present there is known about the intestinal absorption of flavonoids from the diet.

Glucosinolates

Brassica vegetables are the main source of glucosinolates, a series of more than 100 sulfur-containing glycosides. Glucosinolates are degraded in plants by the enzyme myrosinase, giving a series of derivatives containing sulfur among which include isothiocyanates, thiocyanates and nitriles, some with potential health benefits. Foods rich in glucosinolates are the buds of Brussels sprouts and other sprouts containing mainly sinigrin, glucoiberina, progoitrina and glucobrassicin and broccoli, turnips and cauliflower. The cooking process unfavorably affects the levels of glucosinolates in food.
We have detected that diets rich in Brassica vegetables reduce the incidence of certain cancers, especially lung and digestive tract.

Phytoestrogens

Phytoestrogens are plant compounds that are structurally similar to the mammalian estrogen hormone 17-b-estradiol. It has been observed in vitro and in animal models, that phytoestrogens compete with estradiol in its cellular receptors and suppress responses that stimulate estrogen, an effect that is recognized to be important in preventing breast cancer, bowel, prostate and other. The estrogenic activity of these compounds may also have beneficial effects on bone, heart disease and symptoms of female menopause.

The major classes of phytoestrogens found in plants are isoflavones, lignans, coumestans. Isoflavones and lignans have been most studied for their potential health effects.

Isoflavones are found in high concentrations in soybeans, as well as glycosides or as free as aglycones. Women from Eastern countries who eat soy are apparently less menopausal symptoms and lower incidence of osteoporosis than western countries. Soy diet helps to reduce serum cholesterol levels, helping to reduce the risk of developing cardiovascular disease also can help reduce the development of cancers of the uterus, breast and colon

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