LDH (L-lactate-NAD-oxidoreductase, EC 1.1.1.27) is a zinc-containing enzyme that reversibly catalyzes the oxidation of lactate to pyruvate. LDH is a tetramer, contains subunits M and H. In the cytoplasm of cells and blood serum, LDH is represented by 5 isoenzymes, designated according to their mobility to the anode in the electric field: LDH-1 (NNNN), LDH-2 (NNNM), LDH-3 (NNMM), LDG-4 (NMMM) and LDG-5 (MMMM). LDH is present in almost all organs and tissues of the body, and the distribution of LDH isoenzymes is organ specific. LDH-4 and LDH-5 predominate in the liver and skeletal muscles, tissues with predominantly anaerobic metabolism, LDH-1 and LDH-2 - erythrocytes, leukocytes, myocardium, kidneys - tissues with aerobic metabolism, the highest content of LDH-3 is in lungs, lymphoid tissue, platelets and tumors.

MI is usually accompanied by a 3–4-fold increase in total LDH activity; A similar increase in LDH is observed in myocarditis and cardiac arrhythmias. During MI, an increase in total LDH activity in the blood serum is observed after 8–10 hours, and reaches maximum activity after 48–72 hours. The release of myocardial LDH isoenzymes into the blood during MI leads to an increase in the activity of LDH-1 and LDH-2. LDH-1 activity increases 12–24 hours after the onset of acute MI, coinciding in time with the maximum of CK-MB activity and ahead of the peak of total LDH activity (24 hours).

Identification of the spectrum of isoenzymes characteristic of MI is possible with blood stagnation in the liver and kidneys due to heart failure, with ischemic damage some organs due to a sharp decrease cardiac output. Currently, determination of the activity of LDH and its isoenzymes is not among the mandatory tests for diagnosing MI due to insufficient specificity.

Myopathies, liver diseases, megaloblastic and hemolytic anemias, acute and chronic diseases kidney An increase in LDH activity is observed with liver damage, but this increase is not as great as the increase in ALT and AST activity. Special boost (10 times higher upper limit norms) are noted when toxic hepatitis accompanied by jaundice.

A physiological increase in LDH levels in the blood occurs during pregnancy, in newborns, and also after intense physical activity.

Indications for the study:

• Liver diseases;
• detection of myocardial lesions;
• myopathies;
• hemolytic anemia;

Serum or plasma (EDTA, heparin) without signs of hemolysis. Store samples for no more than 2 days at 18–25°C. Storing samples at 4–8°C or freezing reduces enzyme activity.

Research methods. Method based on IFCC recommendations. LDH catalyzes the oxidation of lactate to pyruvate at alkaline pH, while NAD+ is reduced to NADH. The rate of increase in the optical density of the reaction mixture at 340 nm, reflecting an increase in the concentration of NADH, is proportional to the enzyme activity in the sample.

Increased values:

• Myocardial damage;
• liver damage;
• damage, inflammatory and degenerative diseases skeletal muscles;
• embolism and pulmonary infarction;
• kidney diseases;
• diseases and conditions accompanied by cell breakdown;
• malignant tumors of any location;
• reception anabolic steroids, ethanol, hepatotoxic drugs.

Reduced values:

Isoenzymes LDH-1 and LDH-2

LDH-1 and LDH-2 are isoenzymes with a high content of H-subunits that can use α-ketobutyrate as a substrate and catalyze its conversion to α-hydroxybutyrate; the LDH-1 isoenzyme, which has a high affinity for the named substrate, is called α-hydroxybutyrate dehydrogenase (α-HBDH). A parallel study of the activity of total LDH and α-HBDG can be used for the differential diagnosis of diseases of the liver and heart: with damage to the heart muscle, an increase in enzyme activity is due to an increase in LDH-1 (α-HBDG), with damage to the liver parenchyma - by the LDH-5 isoform, LDH activity -1 does not increase.

Indications for the study:

• Detection of myocardial lesions;
• hemolytic anemia;
• malignant neoplasms;
• pulmonary embolism (differential diagnosis with myocardial infarction).

Features of sampling and storage. Serum or plasma (EDTA, heparin) without signs of hemolysis. Store samples for no more than 2 days at 18–25°C. Storing samples at 4–8°C or freezing reduces enzyme activity.

Research methods. LDH catalyzes the conversion of α-ketobutyrate to α-hydroxybutyrate, which results in the oxidation of β-NADH2 to β-NAD. The rate of decrease in optical density at a wavelength of 340 nm is proportional to the enzyme activity in the sample.

Increased values:

• Myocardial damage;
• diseases and conditions accompanied by the breakdown of blood cells;
• acute diseases kidney

Reduced values:

• Genetic disorders or complete absence LDH subunits.

Biochemical analysis Blood testing as one of the methods for determining the state of the body has been used for quite a long time and has shown its effectiveness. A blood test can be called almost the most informative method establishing a diagnosis. A biochemical blood test and interpretation can show almost any changes in the patient’s condition. This method has a high level of reliability and accuracy. Moreover, this analysis blood not only shows clinical picture the state of a certain organ and the quality of its functioning, but also allows you to determine which vitamins, macro- and microelements are missing in the body. Even if nothing hurts and the organs are not bothered, any chemical changes in the body can be the consequences of a process that has already begun, so it is very important to go to the hospital in time and carry out a biochemical blood test if necessary. Most often, this method is used in the practice of urology, gynecology, cardiology, therapy, gastroenterology and other areas of medicine.

Biochemical blood test: preparation and process

In order to conduct a biochemical blood test, it is necessary to take 5-10 ml of blood from a vein on the elbow. In the process of studying the composition of the blood, its composition, quantity and specific gravity of all constituent elements are revealed. All results this study and their decoding is entered into special forms, which list the blood components and their quantitative content. Then, based on the data obtained in the analysis, the doctor will be able to determine the most accurate diagnosis, because the results obtained are compared with established standards for relatively healthy human donors. A blood test, or more precisely the values ​​obtained, can vary greatly in the same person in at different ages and at different condition health. Moreover, not only a person’s age, but also gender can significantly influence the data shown by biochemical analysis.

In most cases, all test indications and criteria cannot have exact reference values. Generally accepted norms fluctuate within a set range. The data obtained is already compared with them: the biochemical analysis showed the norm, or, conversely, whether changes can appear. Any hospital medical Center They use different devices and methods to determine tests, so each individual medical institution sets its own standards for each indicator. Biochemical analysis carried out approximately simultaneously in different structures, may differ. Each clinic that conducts biochemical analysis sets its own requirements and criteria. Therefore, the same analysis indicator, its decoding, is interpreted differently. A doctor with experience can easily cope with the task of conducting the analytical stage of biochemistry and will be able to determine the most accurate diagnosis. This method of determining the diagnosis is practiced in any medical institution cities.

First of all, you need to familiarize yourself with the procedure itself (blood test), the method of its implementation and the reason for the appointment. You need to prepare for the tests. It is prohibited to eat or drink anything. It is necessary to take a blood test on an empty stomach, which will further increase the level of accuracy of the results. Most often, it takes no more than one day to check all blood components. However, the operation can be speeded up. A blood test using this method involves the study of such important blood components as proteins, enzymes, pigments, vitamins, carbohydrates, nitrogenous substances and inorganic elements.

What is an enzyme?

A blood test often includes the determination of various enzymes and their activity. They are protein molecules that influence the development of biochemical reactions in the human body in order to speed them up. In other words, the enzyme is also called an enzyme. The scientific direction that studies these active protein molecules is called enzymology.

The structure of the enzyme is quite complex. It consists of two parts: the active main center and the protein element. The protein part is called the apoenzyme, and the main activating center is called the coenzyme. All together, i.e. apoenzyme and coenzyme are called holoenzyme. This is the complete structure of the enzyme. The coenzyme can be represented by various organic compounds: B vitamins, heme, flavin and others. It is this component that is responsible for accelerating processes and reactions in the body. And an apoenzyme can only be a protein with a tertiary structure. This means that it can then be transformed into a structure more complex than this.

An enzyme reacts on a specific substance, which before the reaction is called a substrate. After the enzyme has acted on it, the resulting element is called a product. Most often, the name of enzymes is formed by adding the ending “-ase” to the name of the substance that breaks down the enzyme. For example, the substrate is succinate, but the enzyme is called succinate dehydrogenase. Depending on how the reactions take place, enzymes are divided into several types. For example, some of them can carry out oxidation or reduction processes, and some direct their action to the cleavage of bonds between chemical elements.

All enzymes are involved in only one process, and this is their narrowly targeted action. Moreover, they can only work under certain prevailing conditions: at the required temperature, at a certain pressure, and acidity level. The enzyme has peculiar " family ties» with the substance that needs to be acted upon. If you imagine the process, the apoenzyme searches for and attaches to the substrate, and the coenzyme begins the process of accelerating the interaction. This connection is called the ligand-receptor or lock-and-key principle.

Special enzyme lactate dehydrogenase

Found in blood fluid and some tissues special enzyme- lactate dehydrogenase (LDH). This component includes 5 types of isoenzymes. The greatest activity of the enzyme is manifested in the kidneys and liver, in the muscles of the heart and skeleton, therefore, in the blood, LDH decoding is used more often in order to find out how well the listed organs and muscles work correctly and accurately. This indicator is quite difficult to establish; it is used infrequently, so not every medical institution allows such an analysis. It requires maximum precision. In addition, if decryption is made, there may be deviations from the norm. Great importance have professional skills in carrying out analysis with maximum accuracy medical personnel and quality of equipment.

A lactate dehydrogenase test is required if there is any suspicion of any disease. Main uses of LDH analysis:

• determination of the development of anemia (the indicator will be increased);
• diagnosing the body for the development of neoplasms, including tumors;
• if there was a myocardial infarction - for diagnosis, observation and control;
• diseases affecting the hepatobiliary complex;
• various diseases, the development process of which is associated with hemolysis.

The blood is analyzed for LDH using a special technique called the UV test. The analysis will only be carried out if it is indicated in the direction. This test does not simply perform calculations and provide results if decryption has been carried out. He does a little medical description the state of the body based on the activity of a given LDH. The blood test itself takes no more than one day, and the results are issued on the second day. It is strictly forbidden to falsify data, as this may negatively affect the course of the patient’s treatment.

LDH depends on age criterion. For an adult, this figure should not be less than 240 and more than 480 IU/l. For children of various ages the criterion will have very strong differences. So, a newborn baby will have more than 1327 IU/l on the first day after birth. In the first 5 days of life, the figure will decrease to 1732 IU/l. From the sixth day to the sixth month, the indicator will decrease to 975 IU/l. Up to 1 year it should be no more than 1100 IU/l. In a child under 3 years of age, LDH should not exceed the norm of 850 IU/L, and between the ages of 4 and 6 years this figure should decrease to approximately 620 IU/L. Later (up to 12 years), LDH decreases to 580 IU/l, and at 17 years - to 450 IU/l.

Normal values ​​and deviations from the norm LDH

The level of lactate dehydrogenase may increase as if physiological reasons, and with pathological deviations that are worth paying attention to. With normal for non-dangerous reasons Enzyme activity increases during pregnancy, in newborn babies, and in people who actively engage in sports.

The total level of lactate dehydrogenase may increase if there has been a myocardial infarction. In this case, the increase in the enzyme itself will be observed 8-11 hours after the heart attack. After 40-73 hours, enzyme activity reaches its maximum. The indicator increases by 2-5 times. Such critical level lasts for another 10 days, but the period may vary depending on the size of the area of ​​the heart muscle that was damaged. The entire increase in activity occurs due to parameters such as LDH2 and LDP. If a person suffers from angina pectoris, then this enzyme will not show an increase in activity.

A moderate level of increased LDH activity may occur in myocardium, heart failure, acute manifestations coronary insufficiency, but a heart attack will not manifest itself. In addition, an increase in activity is observed when congestion and problems occur in the liver. If a person has a heart arrhythmia disease, then LDH may be normal, but after electrical pulse therapy the indicator may increase.

Diseases such as:

• pulmonary insufficiency, pulmonary infarction;
• myopathy due to muscle damage due to injuries, inflammatory processes;
• viral hepatitis in acute form;
• jaundice (only the first stages of the disease);
• liver cancer;
• cirrhosis of the liver.

Testing for LDH helps to detect many diseases of the heart, liver, kidneys and muscles in a timely manner, but the analysis requires maximum accuracy.

LDH in the blood - what is it?

Almost every person experiences extreme stress when they receive the result of a test ordered by a doctor and do not know how to interpret it, and do not immediately get to see a doctor. We will analyze in detail what LDH or LDH is in a biochemical blood test, why the test is taken, what the LDH norm is in men and women, and an interpretation of the results.

LDH analysis - what is it?

Lactate dehydrogenase (LDH or LDH) is an enzyme that takes part in the breakdown of glucose in the absence of oxygen (under anaerobic conditions), converting pyruvic acid to the dairy and back.
IN normal conditions The cell takes energy from the breakdown of glucose into water and carbon dioxide with the participation of oxygen. Under unfavorable conditions, when for some reason the cell does not receive enough oxygen, for the purpose of self-preservation, glucose is also converted into lactic acid, in this reaction a significant amount is produced less energy. At this stage, lactate dehydrogenase is needed. LDH is normally present in small amounts in the cells of all tissues as an “insurance” to survive for some time in the absence of oxygen, but does not accumulate!
LDH enters the blood during the destruction of those cells in which it is most abundant, namely the myocardium, red blood cells, skeletal muscles, and liver.

The LDH molecule consists of 4 subunits, designated H (heard) and M (muscle). Depending on the combinatorial relationships of these subunits, 5 types of LDH are distinguished:

• LDH1 – HHHH - myocardium and erythrocytes
• LDH2 – HHHM - lymph nodes, spleen
• LDH3 – HHMM - lungs
• LDH4 – HMMM - skeletal muscles, placenta, pancreas, kidneys
• LDH5 – MMMM - skeletal muscles and liver.

It is important to note that LDH is an indicator of cell damage but is not specific to any organ or disease.
Determination of LDH enzyme activity is used in conditions associated with cell destruction - when tumor diseases, hemolysis - breakdown of red blood cells, for late diagnosis of myocardial infarction, etc.
Cancer cells consume a lot of glucose, but, unlike healthy cells, breakdown occurs anaerobically - without oxygen (even when there is plenty of it in the blood). Therefore, the amount of LDH is always increased in tumor cells. Also, in tumor diseases, malignant tissue destroys healthy tissue. Therefore, this analysis is prescribed when malignant tumors. It is not entirely correct to call it a tumor marker, since LDH also increases in a number of other conditions with cell damage. But changes in this indicator allow us to judge the dynamics malignant disease and the effectiveness of its treatment.
After myocardial infarction, LDH rises and reaches a peak after 24-48 hours and lasts for high level up to 10 days. This is important for confirming myocardial infarction 24 hours after a painful attack, while the determination of creatinine phosphokinase is valuable for its early diagnosis. During myocardial infarction, LDH increases mainly due to LDH-1 and 2. Normally, LDH-1 and 2 make up about 30-50% of the total amount of this enzyme.

LDH blood test - interpretation

The LDH level changes throughout life - in children the levels are higher and decrease with age:

• newborns in the first 4 days of life: less than 750 U/l;
• 4 – 10 days of life: less than 2000 U/l;
• up to 2 years: less than 430 U/l;
• from 2 to 12 years: less than 295 U/l;
• over 12 years: no more than 250 U/l.

Normal level of LDH in the blood of women

Normal values ​​of LDH in corvi in ​​women are less than 211 U/l.

Normal level of LDH in the blood of men

Normal LDH values ​​in corvi in ​​men are less than 226 U/l.

Increased LDH in the blood - reasons

As mentioned above, an increase in LDH occurs in a variety of conditions accompanied by cell destruction. In addition to diseases, LDH increases during pregnancy, after intense physical activity.

Reasons for increased LDH in the blood:

• myocardial infarction;
• hepatitis of various etiologies(viral, toxic);
• obstructive jaundice;
• cirrhosis of the liver;
• conditions accompanied by hemolysis of red blood cells ( hemolytic anemia, sickle cell, megaloblastic anemia, as a result of poisoning with certain poisons, spider and snake bites, transfusion of incompatible blood, etc.);
• acute leukemia;
• damage to skeletal muscles (extensive injuries, atrophy);
• kidney diseases: glomerulonephritis, pyelonephritis, kidney infarction;
• acute pancreatitis;
• malignant neoplasms;
• taking certain medications: cephalosporins, sulfonamides, NSAIDs (non-steroidal anti-inflammatory drugs), anesthetics, caffeine;
• any diseases accompanied by massive cell destruction: severe states of shock, severe hypoxia, extensive burns;
• pregnancy;

Lactate dehydrogenase (LDH) is one of the most abundant enzymes on Earth - suffice it to say that any cell that breathes oxygen and uses carbohydrates as an energy source must contain it. Therefore it is present in every cell human body, but in different quantities. Thus, its quantity is greatest in organs that are highly functionally loaded during a person’s life - in the liver, kidneys, myocardium, lymph nodes. There is also a lot of lactate dehydrogenase in cells that oxidize a large number of glucose is the most prominent representative in in this regard is nervous tissue.

It is this enzyme that serves as a kind of “bridge” between the oxygen-free and oxygen breakdown of glucose. In most cells, the first stage of carbohydrate oxidation is anaerobic, producing lactic acid and a small amount of energy. Despite the low energy release, the main advantage this process- speed. It provides rapid release of energy from glucose, which is spent on muscle contraction, biochemical and nervous processes. Muscle pain after increased exercise is caused precisely by the accumulation of lactic acid (lactate), formed during the rapid but oxygen-free breakdown of glucose.

Lactate dehydrogenase ensures the conversion of lactic acid into pyruvic acid, which can participate in a slower, but high-energy oxidation process. This pathway provides approximately 16 times more energy than the conversion of glucose to lactate. And him final products are easily removed from the body carbon dioxide and water. Since almost all cells receive energy through the processes described, LDH is found in varying amounts in all organs.

When cells are destroyed, this enzyme enters the blood - it is calculated that on average the concentration of LDH in cellular structures ah exceeds that in the blood by about 500 times. Since in the body against the background full health A small number of cells are constantly breaking down, the level of total lactate dehydrogenase in the blood is normally approximately 135 - 214 U/l in women and 135 - 225 U/l in men. In International units, the amount of LDH in the blood is 200-450 IU/l.

Any acceleration of cell breakdown caused by pathology will inevitably lead to an increase in blood LDH levels. Therefore, this indicator has extremely high sensitivity for a wide variety of pathologies accompanied by destruction of cellular structures. But at the same time, despite the high sensitivity, this indicator is not specific - severe damage connective tissue will give exactly the same picture biochemical research, as well as mild liver or myocardial damage.

For this reason in laboratory diagnostics a method was introduced for the determination of certain varieties of lactate dehydrogenase. In total, five different modifications of this enzyme have been identified in the human body, which are distributed differently in organs. Thus, LDH-1 and 2 are accumulated in the heart, kidneys, lymph nodes, LDH-3 is present in the lungs, LDH-4 is determined in the pancreas, LDH-5 - in the liver and muscle tissue. The most important clinically are the first and second fractions, which are localized in the heart - the study of their quantity in the blood allows us to characterize the state of the myocardium. The norm for LDH-1 and 2 is 72 - 182 IU/l or about 30-50% of the total amount of this enzyme.

As already mentioned, the immediate cause of an increase in LDH in the blood is the destruction of cellular structures. An increase in the amount of total lactate dehydrogenase (the totality of all its fractions) can be provoked by the following pathological conditions:

• Massive damage internal organs– polytrauma, long-term crush syndrome (crash syndrome);
• Destruction of tissues and organs due to the effects of malignant tumors.
• Destruction of blood cells - massive hemolysis of red blood cells during poisoning with certain poisons, spider and snake bites, and transfusion of incompatible blood.
• Damage to organs rich in lactate dehydrogenase - liver, kidneys, myocardium, brain.

Previously, the level of total LDH was recognized as a standard and a specific marker of such a condition as myocardial infarction. However, this was later abandoned in favor of other compounds. Currently, for chest pain, analysis of the total amount of all fractions of lactate dehydrogenase is used only when differential diagnosis myocardial damage.

Increased levels of LDH-1 and 2 are caused precisely by heart damage. Therefore they are still used as diagnostic criterion if myocardial infarction is suspected. Sometimes such a picture of research results is observed in diseases of the kidneys and liver, however, in this case, too, high values ​​of these enzymes are due to secondary damage to the myocardium.

IN in rare cases at clinical analysis a decrease in the amount of both total LDH and its fractions can be detected. But, as a rule, this does not matter diagnostic value and is due to errors in the execution of the study. Thus, the presence of high values ​​in the blood (with renal failure) helps neutralize the enzyme and it is not detected when. The same thing happens when there are certain medicinal substances– hydroxyurea, metronidazole. Objectively, such neutralization looks like a decrease in the amount of this enzyme, but it is not such.

What is LDH level testing used for?

The once popular and widespread method of diagnosing pathologies of the heart and other organs is now gradually losing its importance.

However, the markers and analysis methods that replaced it, although more accurate, are quite expensive and technically complex. Therefore, many doctors use this approach - by determining the level of lactate dehydrogenase or its fractions, they prove the presence of heart damage, and only then prescribe more highly specialized techniques laboratory research to assess the extent of damage.

Another popular use for determining LDH-1 and 2 levels is to monitor therapy with cardiac glycosides and other drugs that can affect the myocardium. Unlike treatment efficacy studies various organs with the help of other enzymes (for example, in the case of pancreatic treatment), the determination of LDH has a different purpose. Data medicines can have a cardiotoxic effect, therefore regular analysis of the level of lactate dehydrogenase makes it possible to detect incipient myocardial damage at early stage and stop taking the medication before irreversible processes occur.

Therefore, the level of LDH in the blood is overall indicator tissue and cellular damage. Sometimes the concentration of a substance is assessed using cerebrospinal or pulmonary fluid in the presence of certain diseases.

The importance of the enzyme in the body

Interest in what LDH is in a biochemical blood test is associated primarily with myocardial infarction. Previously, this test was used to diagnose and monitor damage to cardiac tissue, but now the troponin test is considered more accurate and informative. Lactate dehydrogenase (LDH) is not a specific indicator of cardiac cell damage and is no longer used for patients with suspected acute coronary syndrome. Typically, the transcript of a biochemical blood test contains this indicator. Lactate dehydrogenase in the blood - important enzyme involved in reactions:

production of lactic acid.

The peculiarity of the enzyme is that it does not accumulate in cells, but is completely broken down and excreted. LDH is essential for converting glucose into energy for the functioning of all cells in the body. The reaction is mediated by oxygen, which helps break down glucose into water, carbon dioxide and energy. Without oxygen, energy production decreases by 20 times and lactic acid accumulates. The enzyme LDH is necessary for its oxidation and return to glucose metabolism. Unlike healthy cells cancerous tumors feed without oxygen.

When is the test prescribed?

The test is used when acute and chronic tissue damage is suspected, as well as to evaluate progressive diseases. In rare cases, the test can help identify target organ damage.

The enzyme is detected in the sample venous blood. After injury, LDH is elevated, rises for 48 hours and reaches a maximum after 2-3 days, then gradually decreases. Normal indicator recovers in 10 days.

Research shows that the LDH blood chemistry test is an indicator of cancer development and progression. Even after taking into account the factor of age and stage of the disease in patients, a strong association with the risk of death remained. This relationship was true for all types of malignant tumors.

The blood LDH test can be used to detect and evaluate:

acute or chronic tissue damage;

progression of anemia and severe infection;

currents oncological diseases after chemotherapy for lymphoma, leukemia, melanoma, neuroblastoma. High values ​​indicate poor prognosis for patient survival.

The doctor prescribes determination of LDH levels in other body fluids:

To distinguish between bacterial and viral meningitis by analysis of cerebrospinal fluid.

To identify the cause of the accumulation of exudate in chest or abdomen (pleural, peritoneal and pericardial fluids) due to trauma and inflammation or due to pressure imbalance within blood vessels and the amount of protein in the blood.

A blood test for LDH (biochemistry) is taken on an empty stomach from a vein.

The last meal 8 hours before the examination should not contain too much fatty or protein foods.

Be sure to inform if you need to take medications regularly. Aspirin, hormonal agents contraception and antidepressants affect coagulation and may show elevated values.

Intense training the day before can lead to an increase in the enzyme, as it increases energy expenditure and the need for the breakdown of glucose.

Many factors influence the results of the analysis, and they are not always a cause for concern and further examination:

Hemolysis of blood samples leads to false positive results. Violation of the rules for storing samples and rough processing affect the accuracy.

With increased platelet count, serum LDH level also increases and does not show the real picture.

During hospitalization with suspected myocardial infarction and acute pancreatitis, LDH analysis is performed without taking into account the recommendations. Often, the LDH indicator is used to assess the dynamics of the disease and the patient’s recovery.

Norm of LDH in the body and interpretation of the analysis

When testing blood, the norm is usually indicated in units/l, which means one per liter. The interpretation of the analysis takes into account the age and gender of the patient. A relatively small amount of the enzyme is found in the blood of a healthy adult. In a child under two years of age, the norm is considered to be within 430 units/l.

An increase in lactate dehydrogenase occurs during pregnancy, in newborns, and in professional athletes.

Based on the identified marker, it is impossible to determine which cells were damaged. Therefore, when deciphering LDH, it is necessary to know what its isoenzymes are. Some laboratories conduct additional tests that determine several forms of the substance, starting with the most mobile:

the first indicates a problem with the heart, kidneys and red blood cells;

the second is found mainly in cardiomyocytes and erythrocytes;

the third was found in lung tissue, endocrine glands and adrenal glands;

the fourth is an enzyme in white blood cells, liver, placenta and male testicles and muscle tissue;

the fifth is found in all organs containing LDH-4, as well as skeletal muscles.

Deciphering biochemistry for increased LDH in the blood is now considered less informative.

High values ​​of all isoenzymes determine the pathology of several organs. Myocardial infarction with congestive heart failure causes lung damage and liver congestion. For oncological and autoimmune diseases, such as lupus, lactate dehydrogenase is elevated in general. Hypoxia, shock and burns are accompanied by cell death, which shows an increase in LDH. Caffeine also affects the amount of enzyme in the blood.

The dynamics of the first isoenzyme are more sensitive and specific than the increase in LDH in general. Usually the level of the second isoenzyme is higher than the first. If the concentration of LDH-1 increases relative to LDH-2, it is diagnosed heart attack. Typically, the LDH level in the blood exceeds an hour after damage to the heart tissue and for two days in 80% of cases. Normal ratio LDH-1/LDH-2 is reliable evidence that there was no attack. The ratio of total LDH to LDH-1 is called hydroxybutyrate dehydrogenase. Therefore, during a heart attack:

the LDH/GBDG figure is reduced (less than 1.30);

the LDH-1/LDG-2 ratio approaches 1 and sometimes exceeds this value.

On the first day, myocardial infarction is diagnosed by the creatine kinase indicator, and a day later - by the enzymatic study of LDH. The activity of the substance is directly related to the area of ​​damage to the heart muscle.

Other serious illnesses reflected in the ratio of isoenzymes and coefficients:

hemolytic anemia is characterized by a low LDH/GBDG figure - up to 1.3 and below;

in megaloblastic anemia, LDH-1 significantly exceeds LDH-2;

the general level increases during acute necrotic processes and cell death, such as damage to the kidney parenchyma;

tumors in the gonads (ovaries and testes) are accompanied by an isolated increase in LDH-1.

Most often, LDH is elevated due to the destruction of tissue of the liver and kidney parenchyma, and the death of platelets and red blood cells.

LDH in a blood test is considered in relation to other indicators:

With anemia, red blood cells are destroyed, which releases large amounts of LDH into the blood. The disease is diagnosed against the background of low hemoglobin. Weakness, pallor, shortness of breath may be indications for examination.

Blood cancer is associated with the production of abnormal blood cells, which is reflected in the levels of many indicators: LDH, aspartate aminotransferase, bilirubin, urea. At the same time, there is a decrease in the level of glucose and the blood clotting factor fibrinogen. A biochemical blood test allows one to suspect pathology and refer the patient to identify tumor markers.

Along with the LDH level in the blood, which indicates the death of pancreatic cells, bilirubin and glucose will increase. The primary indicator is the level of the pancreatic enzyme amylase.

Reasons for the increase

Elevated LDH levels can be caused by various diseases:

• stroke;
• some types of anemia (pernicious and hemolytic)
• kidney and liver diseases;
• muscular dystrophy;
• pancreatitis;
• Infectious mononucleosis;
• some forms of cancer.

The concentration of the enzyme increases after the administration of anesthetics and aspirin, as well as after intense physical activity. Normal and reduced levels LDHs are not pathological. A factor that reduces the indicator is consumption of a large dose ascorbic acid(vitamin C).

The reasons that lactate dehydrogenase is elevated are varied: HIV infection, sepsis, acute kidney disease, infarction of the intestines and lungs, bone fractures, rash on the body.

LDH is reduced when transudate accumulates in body cavities, for example, in abdominal cavity, which is usually caused by congestive heart failure or cirrhosis.

Why is LDH elevated in a child, what are the consequences?

If LDH is elevated in a child, doctors become wary. It is necessary to respond to any changes in the body, especially in childhood. This enzyme is present in almost all human organs. How smaller child, the higher this figure will be. It should decrease with age. Lactate dehydrogenase can increase in women during pregnancy, infants, and athletes.

Causes and consequences of increased LDH

The reasons why lactate dehydrogenase is elevated are varied.

LDH concentrations can be affected by various diseases. In most cases, the diagnosis is malnutrition muscle mass, pulmonary infarction or anemia.

Diseases in which LDH increases include:

• hepatitis;
• jaundice;
• liver pathologies (cirrhosis);
• blood diseases;
• leukemia;
• wasting of muscle fibers;
• kidney diseases;
• acute pancreatitis;
• some medications;
• burns.

An analysis to determine the level of LDH is carried out:

• To determine how affected the patient's tissues are.
• To find out the cause of pain in the chest area.

• In order to find the cause of the destruction of red blood cells.
• To monitor the course of cancer.
• To conduct an examination of the liver and kidneys.
• After receiving serious muscle injuries.

The resulting research material is stored for no more than 48 hours, the temperature should be from 18 to 25 o C. If the sample is placed in the cold or frozen, the concentration of LDH will begin to rapidly decrease, the result will be false.

Normal LDH in children

Let's look at the standard indicators of LDH levels in childhood:

• from 1 to 4 days of life -<750 единиц;
• from 4 to 10 days of life -<2000 единиц;
• in children under two years of age -<430 единиц;
• in children from two to twelve years old -<295 единиц.

In medicine, such a biochemical analysis is usually called a UV test. This method should be prescribed for each such patient. A prerequisite is not only a brief transcript of the results, but also a detailed description of each of the indicators.

Nowadays, you can already get the results in your hands in a couple of days, since the equipment is improving and improving every year, you don’t need to worry about the quality. It very rarely happens that the result of a test turns out to be false. But in this situation, further diagnosis and treatment will not give the expected results. The tests will have to be carried out again to verify the falsity/truth of the previous test.

The level of lactate dehydrogenase differs only according to age; gender in this case does not play any role. For adults, a single norm is established, and for children it is calculated by day, especially after birth.

Conducting research

When the lactate dehydrogenase level is elevated, you need to focus your attention on the reasons that caused this condition. This analysis is carried out exactly the same for both adults and children. The blood collection process does not cause pain, so parents should not worry. Blood is taken only from a vein, because it is the most concentrated, and for laboratory processing this is a very important indicator.

As soon as the blood is received, the laboratory assistant extracts serum from it; the remaining components are not needed for biochemical analysis. Further, after certain manipulations, you can find out whether the lactate in the baby’s blood is increased or decreased. Sometimes test results are not released immediately on the second day. The fact is that the material can be stored a little longer, the main thing is that certain conditions are met. Let’s say if the storage temperature is 20 degrees, then the whey can be stored for another month and a half.

Only the blood must be brought to the laboratory within the same two days in order to obtain serum from it in time. If all parameters are met, then the results obtained can be considered one hundred percent accurate.

To take the lactate dehydrogenase test, the patient does not need any special preparation.

But important rules should not be missed:

Otherwise, there are no special instructions. Despite the fact that the procedure is painless, it is still something unknown and unusual for children. So, before the upcoming procedure, it’s worth preparing him: talk to him calmly, tell him everything as it will happen. When the child is ready, then the procedure will seem normal.

The analysis for lactate dehydrogenase may exceed normal standards, be reduced, or be equal to normal. When LDH is elevated, we can talk about the presence of certain types of anemia, hepatitis, hypoxia, or carcinomatosis.

Also, the child has not yet had time to get used to all manifestations of the external environment. The body is just adapting to all kinds of changes. This is how many doctors explain the frequent illnesses of the younger generation. Over time, the immune system, knowing this or that irritant, is able to give its response, then infection will not occur. But preventive measures should not be forgotten; they will help increase immune defense.

Lactate dehydrogenase (LDH) in the blood: what is it, the norm in the analysis, reasons for the increase

The glycolytic intracellular (cytoplasmic) enzyme lactate dehydrogenase (LDH), which accelerates the reaction of converting lactic acid into pyruvic acid, and also catalyzes the reverse reaction (the reversible oxidation reaction of L-lactate to pyruvate), is present without exception in all tissues of the human body. The highest content of LDH is observed in the heart, liver and kidney parenchyma, skeletal muscles, red blood cells, where the enzyme is presented in the form of five isoenzymes (isoenzymes): LDH-1, LDH-2, LDH-3, LDH-4, LDH-5. The electrical mobility of these isoenzymes fully corresponds to that of globulins - α 1, β 1, γ 1, γ 2. The main concentration of LDH is concentrated inside the cells; serum is noticeably inferior in this regard.

In an adult who does not complain about his health, the total activity of lactate dehydrogenase in the blood serum normally ranges from 0.80 to 4.00 mmol/(h·l) or 38 to 62 U/l (at 30°C).

Distribution of fractions in plasma. Age and norm

The first fraction (LDH-1 or HHNN tetramer) originates primarily in the cardiac muscle and is significantly increased in the blood serum with myocardial damage.

The second, third, fourth fractions (LDG-2, LDH-3, LDH-4) begin to actively enter the plasma under pathological conditions accompanied by massive death of blood platelets - platelets, which occurs, for example, in the case of such a life-threatening condition as pulmonary embolism (PE).

The fifth isoenzyme (LDH-5 or MMMM tetramer) comes from the cells of the liver parenchyma and is released into the blood plasma in large quantities at the acute stage of viral hepatitis.

Due to the fact that different types of tissue accumulate and release different concentrations of LDH, fractions of lactate dehydrogenase isoenzymes are distributed unevenly in the blood plasma:

The activity of lactate dehydrogenase in red blood cells (erythrocytes) is 100 times higher than the levels of the enzyme contained in the blood plasma, and increased values ​​​​are observed not only in pathological conditions, but also in a number of physiological conditions, for example, pregnancy, the first months of life or excessive physical effort on their part also contribute to an increase in LDH activity. Significant differences in the normal levels of this indicator are also due to age and gender, as evidenced by the table below:

Meanwhile, the normal values ​​for blood LDH are always approximate; they should not be memorized once and for all for the reason that the analysis can be performed at a temperature of 30°C or 37°C, the level is calculated in different units (μkat/l, mmol/( h·l), U/l or U/l). But if there is an urgent need to independently compare your own results with the normal variants, then it will be useful to first inquire about the institution that performed the analysis, the methods of its implementation and the units of measurement used by this laboratory.

Excretion of lactate dehydrogenase isoenzymes (LDH-4, LDH-5) by the kidneys does not exceed the level of 35 mg/day (excretion rate).

Reasons for increased LDH

The level of LDH activity is increased in almost any pathological process that is accompanied by inflammation and death of cellular structures, therefore the reasons for the increase in this indicator are primarily considered to be:

• Acute phase of myocardial infarction (a more detailed description of changes in the LDH spectrum during necrotic myocardial damage will be presented below);
• Functional failure of the cardiac and vascular system, as well as the respiratory system (lungs). Involvement of lung tissue in the process and the development of circulatory failure in the pulmonary circulation (LDH levels are increased due to the activity of LDH-3 and, to some extent, due to LDH-4 and LDH-5). Weakening of cardiac activity leads to circulatory disorders, symptoms of congestion and an increase in the activity of LDH-4 and LDH-5 fractions;
• Damage to red blood cells (pernicious and hemolytic anemia), causing a state of tissue hypoxia;
• Inflammatory processes affecting the lungs, as well as the renal or hepatic parenchyma;
• Pulmonary embolism, pulmonary infarction;
• Acute period of viral hepatitis (in the chronic stage, LDH activity, as a rule, does not leave the normal range);
• Malignant tumors (especially those with metastasis), localized mainly in the liver tissue. Meanwhile, a strict correlation, in contrast to myocardial infarction (the larger the size of the lesion, the higher the activity of LDH) between the progression of the oncological process and changes in the spectrum of lactate dehydrogenase is not traced;
• Various hematological pathologies (polycythemia, acute leukemia, granulocytosis, chronic myeloblastic leukemia, anemia caused by vitamin B12 deficiency or lack of folic acid);
• Massive destruction of platelets, which is often caused by blood transfusions that are not provided with sufficient selection for individual blood systems (for example, HLA);
• Diseases of the musculoskeletal system, primarily damage to skeletal muscles (injuries, atrophic lesions, mainly at the initial stage of disease development).

LDH and cardiac muscle necrosis

The study of the glycolytic enzyme has a very important diagnostic value in case of damage to the heart muscle, therefore it is one of the main enzymatic tests that determine myocardial infarction on the first day of the development of a dangerous necrotic process localized in the heart muscle (8 - 12 hours from the onset of pain). The increase in enzyme activity occurs, first of all, due to the LDH-1 fraction and partly due to the second fraction (LDG-2).

After a day or two from a painful attack, the level of LDH in the blood reaches its maximum values ​​and in most cases remains highly active for up to 10 days. It should be noted that the activity is directly dependent on the area of ​​myocardial damage (the larger the size of the lesion, the higher the indicator values). Thus, myocardial infarction, initially diagnosed using laboratory tests such as determination of creatine kinase and the MB fraction of creatine kinase, can be confirmed within a day by this enzymatic test (LDG is elevated and increased significantly - 3 - 4 ... up to 10 times).

In addition to increasing the total activity of lactate dehydrogenase and increasing the activity of the LDH-1 fraction, the LDH/LDH-1 or HBDG (hydroxybutyrate dehydrogenase) ratio and the LDH-1/LDH-2 ratio are of particular value for detecting acute myocardial infarction. Considering that the GBDG values ​​in the acute period of the disease change significantly upward, and the total activity of lactate dehydrogenase will be reduced relative to the rather high LDH-1 values, the LDH/GBDG ratio will noticeably drop and will be below 1.30. At the same time, the LDH-1/LDG-2 ratio, on the contrary, will tend to increase, tending to reach 1.00 (and sometimes even cross this line).

Other reasons for changing odds

The above parameters, in addition to necrotic damage to the heart muscle, are also subject to changes in the case of other serious diseases:

• Hemolytic anemia of various origins (LDG/GBDG decreases and becomes below 1.3);
• Megaloblastic anemia (the content of the first fraction significantly exceeds the concentration of the second);
• Conditions accompanied by increased cell destruction (acute necrotic process);
• Neoplasms localized in the glands of the female and male reproductive system: ovarian dysgerminoma, testicular seminoma, teratoma (here only an increase in the concentration of LDH-1 is noted);
• Renal parenchyma lesions.

Thus, the main culprits, and therefore the main reasons for changes in the concentration of the described indicators in the blood serum, can be considered conditions associated with the destruction of liver and kidney parenchyma cells, as well as blood cells (platelets, erythrocytes).

Some nuances

To study LDH in the blood, 1 ml of serum is sufficient, which is obtained from blood donated, as for any other biochemical test, in the morning on an empty stomach (however, if there is a question about diagnosing acute MI, then these rules, of course, are neglected).

In a laboratory study of LDH, hemolysis leads to distortion of the analysis results (overestimates them). And when exposed to heparin and oxalate, the enzyme activity in the serum, on the contrary, will be reduced compared to the real blood LDH values. To prevent this from happening, you should start working with the material as early as possible, first of all separating the clot with formed elements from the serum.

Causes of increased lactate dehydrogenase (LDH) enzyme

Lactate dehydrogenase (LDH) is an enzyme that is involved in the oxidation of glucose and the formation of lactic acid. In the body of a healthy person, LDH does not accumulate, but is destroyed and eliminated naturally. However, there are a number of diseases and pathological conditions that are characterized by a moderate or significant increase in LDH in the blood.

What is LDH?

LDH is found in almost every organ, but the highest concentrations are present in the liver, skeletal muscle and myocardium. The enzyme has five isoenzymes (modifications), which differ from each other in structure, as well as in their specificity - each of them is concentrated in a specific organ.

• LDH-1 predominates in the tissues of the heart muscle and brain;
• LDH-1 and LDH-2 are found in blood cells (erythrocytes, platelets) and kidneys;
• LDH-3 is an enzyme in skeletal muscle, lungs, thyroid and pancreas, adrenal glands and spleen;
• LDH-4 is found in the same tissues as LDH-3, as well as in the liver, placenta, male germ cells and granulocytes;
• LDH-5 is characteristic of the liver and skeletal muscles, as well as organs containing LDH-4.

Due to the fact that the concentration of LDH in the blood increases in diseases that are accompanied by damage to tissues and cells, this enzyme is a very important diagnostic marker. An analysis that determines the concentration of LDH in the blood, in combination with other tests, is often used to identify a variety of disorders in the body. Such a study is prescribed to determine the following diseases and pathologies:

• Diagnosis of myocardial infarction, heart and lung diseases with complaints of severe chest pain;
• Diagnostics of malignant neoplasms;
• Diagnosis of muscle pathologies;
• Monitoring the treatment of cancer patients and the course of certain diseases;
• Comprehensive examination of patients.

Norm

The level of LDH in the body of a healthy person depends primarily on his age: thus, at the beginning of life, its concentration increases, and over the years it begins to decrease. Reference values:

Level up

The level of LDH may be elevated in the patient’s blood with the following diseases and pathological conditions:

• Myocardial infarction: an increase in the concentration of LDH in the blood during myocardial infarction is observed in the first hours, after which the enzyme level persists for 3-10 days
• Congestive heart failure
• Pulmonary infarction: an increase in lactate dehydrogenase is observed already in the first day after the onset of pain in the chest area
• Kidney pathologies (kidney infarction, pyelonephritis, etc.)
• Liver diseases: acute viral hepatitis, cirrhosis, changes in liver tissue due to alcoholism
• Oncological diseases: testicular cancer, liver, kidney tumors, etc.
• Intestinal infarction
• Stroke
• Leukemia
• Blood diseases that are accompanied by hemolysis (hemolytic, megaloblastic, pernicious anemia, erythremia)
• Lymphoma
• Acute pancreatitis
• Infectious mononucleosis
• Conditions accompanied by hypoxia, hypo- and hyperthermia
• Muscle pathologies: dystrophy, atrophy, injuries
• Bone fractures
• Acute pancreatitis
• Multiple burns
• Traumatic shock
• Delirium tremens
• Seizures
• Eclampsia
• During pregnancy, an increase in LDH may be normal or indicate placental abruption

What concentration of uric acid is considered normal for women, read here.

What values ​​of the Alt enzyme in the blood are considered normal? Find out about this at the link http://med-analyzes.ru/analizy-krovi/biohimiya/fermenty/alt.html

• Heavy physical activity prior to testing
• Alcohol consumption
• The patient has a prosthetic heart valve, which can cause hemolysis of red blood cells
• Use of electropulse therapy on the eve of the study
• Application of hemodialysis
• Some skin diseases
• Thrombocytosis
• Taking medications that can increase LDH levels: acetylsalicylic and valproic acid, anesthetics, anabolic steroids, codeine, nonspecific anti-inflammatory drugs, sulfonamides, penicillin, insulin, caffeine.

During myocardial infarction, the peak concentration of the enzyme is observed on days 3-4, and remains at the same level for 10 days. In addition, in this case, the patient experiences a significant increase in LDH-1 levels. If a person has suffered not a heart attack, but an attack of angina, the analysis will show the absence of destruction of heart cells.

The main difference between a pulmonary embolism and a heart attack is that in the first case, an increase in LDH is accompanied by an increase in bilirubin levels and normal AST levels.

With inflammation of the membranes of the brain (viral meningitis), an increase in LDH is negative and indicates the development of encephalitis.

With serious liver pathologies, the concentration of LDH increases and remains unchanged for a long time.

When diagnosing any disease, it is very important to determine the activity of a particular isoenzyme in order to determine the localization of the pathological process. In particular, in patients with acute leukemia, an increase in the activity of LDH-2 and LDH-3 is observed, and in liver diseases, the concentration of LDH-4 and LDH-5 increases. Malignant neoplasms are characterized by a significant increase in the concentration of isoenzymes LDH-3, LDH-4 and LDH-5.

The level of LDH in the blood of cancer patients decreases with effective therapy, so this marker is used to monitor the dynamics of treatment.

Downgrade

A decrease in LDH levels is typical for the following conditions:

• Increased levels of urea (uremia) and oxalates in the patient's body
• Taking certain medications: ascorbic acid, dofibrate, amikacin, naltrexone, anticonvulsants, etc.
• Specific reaction to cystotic chemotherapy.

Taking LDH in a blood test for biochemistry and interpreting the results

General lactate dehydrogenase (LDH) is a zinc-containing intracellular enzyme that plays a role in lactate synthesis. It is found almost throughout the body, most commonly in the liver, muscle tissue and heart. LDH has 5 variations, differing in structure and localization:

1. LDH-1 is mostly located in brain tissue and heart muscle;
2. LDH-1 and LDH-2 are localized in blood cells and kidneys;
3. LDH-3 is present in muscles, spleen, adrenal glands, lungs, pancreas;
4. LDH-4 has the same locations as LDH-3, in addition it is found in the placenta, granulocytes, liver and sperm;
5. LDH-5 is found in muscles, in liver cells and in all organs where LDH-4 is localized.

What is LDH

When cells are fully supplied with oxygen, Lactate dehydrogenase is not stored in the body, but breaks down into neutral substances and is released naturally. But with certain disorders leading to cell splitting, its amount may increase. An increase in the concentration of lactate dehydrogenase may be evidence of various pathologies.

Norm of LDH in the blood

There are specific limits for normal LDH concentrations. Immediately after birth (up to 4 days), an LDH level of up to 775 U/l is considered normal. In newborns, the normal level of enzyme in the blood will not exceed 2000 units per liter of blood. In children under 2 years of age, the enzyme level should not exceed 430 U/l, from 2 to 12 years of age U/l. In adults, the amount of LDH decreases significantly and has gender differences: in women, the number of units/l is taken as the norm, and in men, units/l.

When is an LDH test required?

As a rule, doctors refer for an analysis of the concentration of LDH in the blood if they suspect many diseases caused by hypoxia or cell breakdown: anemia, myocardial destruction, tumors, pathologies in the liver, and others. With the help of this study, it is possible to identify any abnormalities in the structure of tissues and recognize the disease in time.

Determination of LDH level

The blood is tested for LDH content using a special technique called the “UV test”. Blood is taken from a vein in the morning (before 10) and on an empty stomach. The resulting substance is then centrifuged to separate the serum from the plasma. It is very important that the serum is clean, without traces of red blood cell breakdown, otherwise the result may be incorrect. Attention! It is not advisable to smoke or drink alcohol on the eve of the test. In addition, you should not eat 6-8 hours before the test, and you should limit your intake of protein and fatty foods. Intense sports can also distort the results. The final indicator is also influenced by the medications taken, so it is worth postponing taking medications on the day of the study. Usually, the results of the analysis can be seen already on the 2nd day of the examination.

Important! An increase in LDH levels does not always indicate pathology. There are physiological reasons for an increase in enzyme levels, such as pregnancy, infancy or increased physical activity.

When LDH is elevated

An increase in LDH concentration occurs in the following pathologies:

• stroke
• myocardial, intestinal or lung infarction
• pulmonary failure
• hypoxia
• acute pancreatitis
• pancreatic diseases
• low blood pressure
• diseases that affect the hepatobiliary complex
• cancer of the blood, kidneys, testicles, etc.
• cirrhosis of the liver
• jaundice (in the first stages of the disease)
• iron deficiency or pernicious anemia
• eclampsia
• placental abruption
• some fungal diseases
• lymphoma
• hepatitis
• Infectious mononucleosis
• skeletal muscle injuries, traumatic shock
• dystrophic condition
• glomerulonephritis
• leukemia
• oxygen deficiency

To accurately determine where the pathological process occurs, it is necessary to analyze which LDH isoenzyme is elevated.

An increase in LDH-1 or LDH-2 levels most often indicates a heart attack. If the concentration of LDH-1 and LDH-3 is increased, then it can be assumed that the patient is developing muscle tissue atrophy. Excessive activity of LDH-4 and 5 isoenzymes often indicates liver dysfunction, as well as muscle and bone damage. If cancer is suspected, then the greatest attention is paid to the amount of LDH-3, 4 and 5.

Important! Elevated LDH levels can be found in conditions such as:

• alcohol consumption
• psychological stress or increased physical activity
• certain skin diseases
• use of certain medications (most often aspirin, anesthetics, fluorides, oral contraceptives and insulin)
• thrombocytosis

When LDH is low

A decrease in the concentration of lactate dehydrogenase in the blood is typical in the following situations:

• consumption of large amounts of ascorbic acid;
• high levels of oxalic acid salts (oxalates) in urine
• a peculiar reaction to cystotic chemotherapy.

A decrease in LDH is very rare and is not always interpreted as evidence of the presence of disorders in the body.

Ways to lower LDH levels

To reduce the lactate dehydrogenase level, it is necessary to accurately diagnose the cause of its increase and eliminate it. A qualified specialist must be involved in deciphering the analysis results. Treatment of the identified disease will help lower the level of LDH in the blood. Monitoring of lactate dehydrogenase is required when the following diagnoses are detected:

If the patient is diagnosed with anemia, he will be prescribed systematic therapy, including taking iron supplements and a special diet. In this case, it is necessary to periodically conduct a biochemical blood test for LDH in order to ensure the effectiveness of treatment.

It is also necessary to regularly donate blood for LDH during the treatment of acute pancreatitis, since it is by the lactate dehydrogenase indicator that the success of therapy can be monitored.

As a rule, qualified doctors eliminate an attack of inflammation of the pancreas without surgery, and only in the most serious cases is its removal prescribed.

In case of myocardial infarction, it is imperative to start treatment on time. First of all, drug therapy is prescribed to help quickly relieve the attack and normalize blood circulation. During treatment, LDH levels should be strictly monitored.

If cancer is suspected, additional examinations of the patient are required. If this diagnosis is confirmed, emergency measures must be taken. As a rule, preference is given to complex therapy, including surgery, chemotherapy and radiation treatment.

Thus, a biochemical blood test for the content of lactate dehydrogenase will help to timely detect various diseases and pathologies in the human body in the early stages, before symptoms of the disease appear. Fortunately, modern methods of examining the body make it possible to avoid dangerous complications. Moreover, comprehensive diagnostics makes it possible to monitor the course of chronic diseases.

How to get rid of varicose veins

The World Health Organization has officially declared varicose veins one of the most dangerous mass diseases of our time. According to statistics for the last 20 years, 57% of patients with varicose veins die in the first 7 years after the disease, of which 29% die in the first 3.5 years. The causes of death vary - from thrombophlebitis to trophic ulcers and the cancerous tumors caused by them.

The head of the Phlebology Research Institute and academician of the Russian Academy of Medical Sciences spoke in an interview about how to save your life if you have been diagnosed with varicose veins. Watch the full interview here.