Biochemical analysis of blood, blood enzymes. Amylase, lipase, ALT, AST, lactate dehydrogenase, alkaline phosphatase - increase, decrease in indicators. Causes of violations, decoding of the analysis. Serum total amylase Site of amylase formation

Amylase - what is it and what function does it perform in the body? This term is understood as a whole group of enzymes, which are united under the general name - "amylase". There are three varieties of this substance: alpha, beta and gamma. For the human body, alpha-amylase is of particular importance. We will talk about it now.

Where is it synthesized?

Amylase - what is it? The name of this enzyme comes from the Greek word "amylon", which means "starch" in Russian. In the human body, amylase is found in a number of tissues and organs. It is an enzyme (hydrolase) that breaks down. The concentration of this enzyme is quite high in the pancreas. It is synthesized by the acinar cells of this organ and is secreted through the pancreatic ducts into the digestive tract, more precisely into the duodenum. In addition to the pancreas, they are also capable of synthesizing amylase. The enzyme contained in saliva initiates the hydrolysis of starch while food is still in the mouth. Thus, the process of digestion begins as soon as food enters the mouth.

Amylase level: analysis

Amylase - what is it? How to determine its level in the human body? The fact is that where this enzyme is produced, it is very well supplied with blood. Normally, part of the enzyme (its minimum amount) enters the bloodstream. Further, this hydrolase, passing through the kidneys, is excreted along with the urine.

Blood alpha amylase - what is it? We'll talk about this in more detail below.

When is an analysis scheduled?

Helps to assess the condition of the body blood test. Amylase - what is it, in what diseases does it increase in the blood? The level of alpha-amylase in can increase several times with the following pathologies:

  1. Acute or chronic pancreatitis during an exacerbation.
  2. Pancreatic necrosis is focal.
  3. Oncology of the pancreas.
  4. (in the presence of separate stones in the ductal system).
  5. Acute appendicitis.
  6. Renal failure.
  7. Stomach bleeding.
  8. Intestinal obstruction.
  9. Alcoholism and alcohol intoxication.
  10. AIDS.
  11. Viral hepatitis.
  12. Mumps.
  13. Sarcoidosis.
  14. Typhoid fever.
  15. Injuries of the abdominal cavity (upper section).

The level of alpha-amylase is lowered or not detected at all in cases of total oncology of this organ of the 4th stage, because gland tissue is replaced by tumor, as well as cystic fibrosis (congenital pathology). During surgical interventions, when a significant part of the gland is removed, the level of amylase can also be sharply reduced.

Under what conditions amylase in the blood increases?

Blood amylase - what is it and how does this indicator change in pancreatic pathologies? In acute pancreatitis, it increases sharply within 4-6 hours after the onset of an attack and continues to be at a high level for up to five days. An increase in the enzymatic activity of amylase in the blood plasma usually does not depend on the severity of the disease. More often the opposite. During destruction, a significant increase in concentration is not observed. And an increase in its level may indicate an increased release of amylase into the general circulation.

In what cases is it possible to increase its concentration in the blood? This can usually be observed under the following conditions:

  1. Hypersecretion of pancreatic juice.
  2. Violation of the full outflow of pancreatic secretions through the pancreatic ducts into the duodenum.
  3. Inflammation of the pancreas itself or organs close to it. The temperature of the inflamed organs rises and the blood flow in them increases, so there is an increased release of the enzyme into the blood.
  4. Injuries of the pancreas.
  5. Violation of the diet and alcohol abuse.

Urine diastasis

During glomerular filtration, amylase is excreted, half of it is reabsorbed by the tubules. The remaining half is excreted in the urine. An increase in urine diastase is observed under the same conditions as an increase in its concentration in the blood. It should be noted that the activity of amylase in the urine is approximately 10 times higher than its activity in the blood.

Amylase - what is it and what are the permissible norms for this indicator in the blood and urine? This will be discussed further.

Alpha amylase - what is it? Normal values ​​in blood and urine

When reading the results of the analysis for amylase, you should pay attention to the units in which it is expressed. It is customary to use "u/l" - units of amylase per liter of blood and "mkkatal/l" - microkatal in one liter. It should be clarified here that "katal" is a unit for measuring the activity of a catalyst.

Also, in different laboratories, the methods and reagents for determining amylase may differ slightly, so you should pay attention to the norms of this indicator, which are always indicated next to the result of the study. The first digit is the minimum value, the second is the maximum.

The norms of blood alpha-amylase and urine diastase are shown in the table below:

In cases where there is a slight increase in performance (by several units) and the person feels good, this is not a pathology. You need to worry when increasing the values ​​of amylase several times. Attacks of acute pancreatitis can give an increase in urine diastase and blood amylase by 100 times or more. Usually these attacks are accompanied by nausea, vomiting and severe pain. This condition requires immediate hospitalization.

How to take a blood and urine amylase test?

Blood for this analysis is taken from a vein. Usually it is taken in the morning on an empty stomach, but if you need to determine the level of amylase urgently, for example, during an exacerbation of chronic pancreatitis, this can be done at any time. Such an analysis can be performed by any biochemical laboratory. As a rule, enzymatic methods for diagnosing amylase activity are used in modern laboratories. This is a specific and precise method. The analysis is performed quite quickly.

It is also better to take an analysis of urine diastasis in the morning. An average portion of urine is taken and immediately delivered to the laboratory. Studies of this indicator are of great importance in the diagnosis of various diseases.

The amylase enzyme is the first enzyme discovered by scientists. In 1833, this enzyme was described by the French scientist Payat, who discovered it in connection with the breakdown of starch in the digestive tract. If you chew foods containing starch in your mouth for a long time ( potatoes, rice), thanks to amylase, they begin to acquire a sweetish taste. This indicates the beginning of the processing of carbohydrates in the mouth.

This enzyme is of three types: alpha, beta, and gamma. Calcium is required for the production and action of this enzyme. Different types of enzyme are similar to each other: they are all perfectly diluted with water or in a weak salt solution. And if you introduce a concentrated saline solution into the enzyme, the enzyme will precipitate. Alcohol has a similar effect on enzymes. With the introduction of it in a concentration of more than sixty percent, the enzymes also precipitate.

This enzyme is present not only in the human body, but also in animals, and even in a number of plants ( only beta-amylase, which is not present in animals). Ripe fruits have a pleasant sweet taste, often due to the presence of this enzyme.
In wheat, for example, gamma-amylase is present, which is the main substance for the production of malt. This type of enzyme works best when the acid content is high.

During the fermentation of yeast dough, fungi using amylase break down starch to the level of polysaccharides, which are then used by yeast fungi to form alcohols and carbon dioxide. It is thanks to these starch processing products that the yeast dough increases in volume, which has such a specific pleasant aroma and taste.

To date, in order for the yeast dough to ferment faster, amylase is added to it as a food additive ( E1100). Moreover, a different form of this enzyme is even added to washing powders to better wash starchy stains.

The amylase level is detected during a biochemical analysis. To make the results as objective as possible, biological materials ( more often blood) are taken after a night's sleep and preferably not earlier than eight hours after eating. The normal rate of this enzyme does not differ in people of different sexes and ranges from 25 to 125 units per liter.

Why is amylase elevated?
An increase in the amount of the enzyme indicates that the organs that include this enzyme are sick. The main reasons for the increase in the amount of amylase are:
1. Pancreatitis in acute form is an inflammatory process of the pancreas that proceeds in an acute form and passes with the destruction of the tissues of the gland, as a result of which the enzyme penetrates into the blood. The symptoms of this disease are: vomiting, nausea, pain around the navel, which shoots in the lower back, fever.

2. Chronic pancreatitis is an inflammatory process of the pancreas that takes place over a long period of time and is characterized by temporary relief and exacerbations. The signs of this disease in the acute phase are the same as in the acute form.

3. Neoplasms or stones in the pancreatic ducts - they interfere with the removal of the enzyme from the gland, which provokes its penetration into the blood.

The patient should not restrict himself in food or fluids. The only thing to refrain from is the use of alcoholic beverages. A blood test is taken from a vein. Before performing the procedure, the patient should be explained that pinching the hand with a tourniquet can cause some discomfort, but they quickly pass.
A few days before taking blood, you should talk with the patient about what medications he is using. Some may need to be temporarily cancelled.

After blood sampling, it is poured into a clean test tube, a piece of cotton wool soaked in alcohol is applied to the injection site. If a group of scientists from the University of Pennsylvania is formed at the injection site ( USA) conducted studies, as a result of which it was found that the amount of alpha-amylase in the blood and urine of a child ( and an adult) is different depending on the influence of external conditions. Scientists believe that by measuring the amount of this enzyme in a child's saliva, it is possible to determine the level of stress in which the child is.

Children of eight to nine years old took part in the experiment. Scientists have found a clear relationship between the amount of the enzyme and the difficulties in the process of mastering knowledge, communicating with peers, aggressive behavior, conflicts in the family.
Also, American scientists found that with an increase in the level of amylase in saliva in four-year-old babies, one can suspect poor social contacts with peers and teachers, as well as susceptibility to infectious diseases.

The data obtained make it possible to determine personal characteristics in the formation of reactions to stressful situations, to explain some violations of the behavior of children. To date, tests have been developed to easily determine the level of this enzyme in saliva. Despite the ease of use of the tests, it is undesirable to independently try to determine the level of enzymes in the child's saliva and interpret the results. It is preferable to visit a kidney failure pediatrician's consultation.
In the case of a chronic form of inflammation of the pancreas in the remission phase, the amount of enzyme in the urine is most often close to normal. And during an exacerbation, the amount of the enzyme in the blood increases slightly, while in the urine it can remain unchanged.

In addition to the above diseases, an increase in the level of amylase in the urine is characteristic of chronic renal failure, diseases of the digestive system ( with damage to the pancreas), disorders of the salivary glands ( caused by various reasons).

In a biochemical blood test, enzyme activity is often used. What are enzymes? Enzyme is a protein molecule that accelerates the course of biochemical reactions in the human body. The term enzyme is synonymous with enzyme. Currently, both of these terms are used in the same sense as synonyms. However, the science that studies the properties, structure and functions of enzymes is called enzymology.

Consider what this complex structure is - an enzyme. The enzyme consists of two parts - the actual protein part and the active center of the enzyme. The protein part is called apoenzyme, and the active center coenzyme. The whole enzyme molecule, that is, the apoenzyme plus the coenzyme, is called holoenzyme. The apoenzyme is always represented exclusively by a protein of a tertiary structure. The tertiary structure means that a linear chain of amino acids is transformed into a structure of a complex spatial configuration. The coenzyme can be represented by organic substances (vitamin B6, B1, B12, flavin, heme, etc.) or inorganic (metal ions - Cu, Co, Zn, etc.). Actually, the acceleration of the biochemical reaction is produced precisely by the coenzyme.

What is an enzyme? How do enzymes work?

The substance on which the enzyme acts is called substrate, and the substance resulting from the reaction is called product. Often the names of enzymes are formed by adding the ending - aza to the name of the substrate. For example, succinate dehydrogen aza- breaks down succinate (succinic acid), lactate dehydrogenase - breaks down lactate (lactic acid), etc. Enzymes are divided into several types depending on the type of reaction they accelerate. For example, dehydrogenases carry out oxidation or reduction, hydrolases carry out the cleavage of chemical bonds (trypsin, pepsin - digestive enzymes), etc.

Each enzyme accelerates only one specific reaction and works under certain conditions (temperature, acidity of the environment). The enzyme has an affinity for its substrate, that is, it can only work with this substance. Recognition of "one's own" substrate is provided by apoenzyme. That is, the process of the enzyme can be represented as follows: the apoenzyme recognizes the substrate, and the coenzyme accelerates the reaction of the recognized substance. This principle of interaction was called ligand - receptor or key-lock interaction.That is, just as an individual key fits a lock, so an individual substrate fits an enzyme.

Blood amylase

Amylase is produced by the pancreas and is involved in the breakdown of starch and glycogen to glucose. Amylase is one of the enzymes involved in digestion. The highest content of amylase is determined in the pancreas and salivary glands.

There are several types of amylase - α-amylase, β-amylase, γ-amylase, of which the determination of α-amylase activity is most widely used. It is the concentration of this type of amylase that is determined in the blood in the laboratory.

Human blood contains two types of α-amylase - P-type and S-type. In the urine, 65% of the P-type of α-amylase is present, and in the blood up to 60% is the S-type. The p-type of urinary α-amylase is called diastasis in biochemical studies to avoid confusion.

The activity of α-amylase in urine is 10 times higher than the activity of α-amylase in the blood. Determination of the activity of α-amylase and diastase is used to diagnose pancreatitis and some other diseases of the pancreas. In chronic and subacute pancreatitis, the determination of α-amylase activity in duodenal juice is used.

Blood amylase rate

Increase in blood amylase

An increase in the activity of α-amylase in the blood is called hyperamylasemia, and an increase in the activity of urine diastase - hyperamilasuria.

An increase in blood amylase is detected in the following conditions:

  • at the beginning of acute pancreatitis, the maximum is reached after 4 hours from the onset of the attack, and decreases to normal on days 2-6 from the onset of the attack (an increase in α-amylase activity is possible by 8 times)
  • with exacerbation of chronic pancreatitis (in this case, the activity of α-amylase increases by 3-5 times)
  • in the presence of tumors or stones in the pancreas
  • acute viral infection - mumps
  • alcohol intoxication
  • ectopic pregnancy
When is urine amylase elevated?
An increase in the concentration of amylase in the urine develops in the following cases:
  • in acute pancreatitis, there is an increase in diastase activity by 10-30 times
  • with exacerbation of chronic pancreatitis, diastase activity increases by 3-5 times
  • with inflammatory liver diseases, a moderate increase in diastase activity by 1.5-2 times is observed
  • acute appendicitis
  • intestinal obstruction
  • alcohol intoxication
  • bleeding from gastrointestinal ulcers
  • in the treatment of sulfa drugs, morphine, diuretics and oral contraceptives
With the development of total pancreatic necrosis, pancreatic cancer and chronic pancreatitis, α-amylase activity may not increase.

Decreased blood and urine amylase

There are body conditions in which the activity of α-amylase may decrease. Low diastase activity urine is detected in a severe hereditary disease - cystic fibrosis.

In blood decreased α-amylase activity possible after an attack of acute pancreatitis, with pancreatic necrosis, as well as with cystic fibrosis.

Although α-amylase is present in the kidneys, liver and pancreas, the determination of its activity is mainly used in the diagnosis of pancreatic diseases.

How to take an amylase test?

To determine the activity of amylase, blood is taken from a vein, in the morning, on an empty stomach or an average portion of morning urine. The day before the test, you should avoid fatty and spicy foods. In an acute attack of pancreatitis, blood from a vein and urine are given regardless of the time of day. Currently, most laboratories use enzymatic methods for determining amylase activity. This method is quite accurate, highly specific and takes a short period of time.

Lipase

Structure, types and functions of lipase
Lipase is one of the digestive enzymes involved in the breakdown of fats. This enzyme requires the presence of bile acids and a coenzyme called colipase to function. Lipase is produced by various human organs - the pancreas, lungs, leukocytes.

The greatest diagnostic value is lipase, which is synthesized in the pancreas. Therefore, the determination of lipase activity is used mainly in the diagnosis of pancreatic diseases.

The norm of blood lipase

In the urine of a healthy person, lipase is absent!


Lipase in the diagnosis of pancreatic diseases
For the diagnosis of pancreatic disease, lipase is a more specific test than amylase because its activity remains normal in ectopic pregnancy, acute appendicitis, mumps, and liver disease. Therefore, if there is a suspicion of the presence of pancreatitis, it is advisable to determine the activity of lipase and amylase at the same time. An increase in the activity of blood serum lipase in acute pancreatitis is possible from 2 to 50 times relative to the norm. To identify acute alcoholic pancreatitis, the ratio of lipase and amylase activity is used, and if this ratio is greater than 2, then this case of pancreatitis is undoubtedly of alcoholic origin. An increase in blood amylase activity occurs 4-5 hours after an attack of acute pancreatitis, reaches a maximum after 12 -24 hours and remains elevated for 8-12 days. With the development of acute pancreatitis, the activity of lipase in the blood serum may increase earlier and more significantly than the activity of amylase.

When is blood lipase elevated?

Under what conditions does the activity of lipase in the blood serum increase:
  • acute pancreatitis
  • various tumors and tumor-like formations of the pancreas
  • cholestasis
  • ulcer perforation
  • metabolic diseases - diabetes, gout, obesity
  • medication (heparin, narcotic painkillers, barbituric hypnotics, indomethacin)
Also, an increase in lipase activity is possible with injuries, wounds, operations, fractures and acute renal failure. However, the increased activity of lipase in these conditions is not specific for them, therefore, it is not used in the diagnosis of these diseases.

When is the level of blood lipase low?

A decrease in lipase activity in the blood serum is observed with tumors of various localization (except for the pancreas), a removed pancreas, malnutrition, or hereditary triglyceridemia.

How do I prepare for a lipase test?

To determine the activity of lipase, blood is taken from a vein, in the morning, on an empty stomach. The night before the test, you should not take fatty, spicy and spicy foods. In case of emergency, blood from a vein is donated, regardless of the time of day and previous preparation. Currently, an immunochemical or enzymatic method is most often used to determine the activity of lipase. The enzymatic method is faster and requires less staff qualification.

Lactate dehydrogenase (LDH)

Lactate dehydrogenase (LDH) is an enzyme found in the cytoplasm of kidney, heart, liver, muscle, spleen, and pancreas cells. The coenzyme of LDH is zinc ions and nicotinamide adenine dinucleotide (NAD). LDH is involved in glucose metabolism by catalyzing the conversion of lactate (lactic acid) to pyruvate (pyruvic acid). There are five isoforms of this enzyme in the blood serum. LDH1 and LDH2 are isoforms of cardiac origin, that is, they are found mainly in the heart. LDH3, LDH4 and LDH5 are of hepatic origin.

Norm of lactate dehydrogenase (LDH) blood


Diagnostic value of LDH isoforms

For the diagnosis of various diseases, the determination of the activity of LDH isoforms is more informative. For example, in myocardial infarction, there is a significant increase in LDH1. For laboratory confirmation of myocardial infarction, the LDH1 / LDH2 ratio is determined, and if this ratio is greater than 1, then the person had a myocardial infarction. However, such tests are not widely used due to their high cost and complexity. Usually, the total activity of LDH is determined, which is the sum of the total activity of all LDH isoforms.

LDH in the diagnosis of myocardial infarction
Consider the diagnostic value of determining the total activity of LDH. Determination of LDH activity is used for late diagnosis of myocardial infarction, since an increase in its activity develops 12-24 hours after an attack and can remain at a high level for up to 10-12 days. This is a very important circumstance when examining patients admitted to a medical institution after an attack. If the increase in LDH activity is insignificant, then we are dealing with a small-focal infarction, if, on the contrary, the increase in activity is prolonged, then we are talking about an extensive heart attack. In patients with angina pectoris, LDH activity is increased in the first 2-3 days after an attack.

LDH in the diagnosis of hepatitis
The activity of total LDH may increase in acute hepatitis (due to an increase in the activity of LDH4 and LDH5). At the same time, the activity of LDH in the blood serum increases in the first weeks of the icteric period, that is, in the first 10 days.

LDH norm in healthy people:

May increase LDH activity in healthy individuals ( physiological) after physical exertion, during pregnancy and after drinking alcohol. Caffeine, insulin, aspirin, acebutolol, cephalosporins, heparin, interferon, penicillin, sulfonamides also cause an increase in LDH activity. Therefore, when taking these drugs, it is necessary to take into account the possibility of increased LDH activity, which does not indicate the presence of pathological processes in the body.

Causes of increased blood LDH

In general, an increase in LDH activity in the blood serum can be detected in the following pathological conditions:
  • myocardial infarction
  • acute hepatitis (viral, toxic)
  • cancerous tumors of various localization (teratomas, ovarian dysgerminomas)
  • muscle injuries (ruptures, fractures, etc.)
  • acute pancreatitis
  • kidney pathology (pyelonephritis, glomerulonephritis)
  • hemolytic anemia, B12 deficiency and folate deficiency anemia
LDH may have reduced activity against the background of uremia (increased urea concentration).

How to take an analysis for LDH?

To determine the activity of LDH, blood is taken from a vein, in the morning, on an empty stomach. There are no special diets or restrictions before taking the test. LDH is present in erythrocytes, so the serum for the study must be fresh, without signs of hemolysis. Currently, the activity of LDH is most often determined by the enzymatic method, which is reliable, specific and fairly fast.

Alanine aminotransferase (ALT, ALT)

Alanine aminotransferase (ALT, AlAT) is an enzyme belonging to aminotransferases (transaminases), that is, carrying out the transfer of amino acids from one biological molecule to another. Since the name of the enzyme contains the amino acid alanine, this means that this enzyme transfers the amino acid alanine. The coenzyme of AST is vitamin B6. ALT is synthesized in cells, so normally its activity in the blood is low. It is predominantly synthesized in the cells of the liver, but is also found in the cells of the kidneys, heart, muscles and pancreas.

Alanine aminotransferase (ALT / ALT) blood norm

Increased ALT activity in healthy people ( physiological) can be caused by taking certain medications (antibiotics, barbiturates, drugs, anticancer drugs, oral contraceptives, non-steroidal anti-inflammatory drugs, dicoumarins, echinacea, valerian), strong physical exertion, injuries. Also, high ALT activity is observed in adolescents during a period of intensive growth.

ALT in the diagnosis of liver diseases
When diagnosing pathological conditions of the body, an increase in ALT activity is a specific sign of acute liver disease. An increase in the activity of ALT in the blood is detected 1-4 weeks before the onset of symptoms of the disease and 7-10 days before the appearance of the maximum level of bilirubin in the blood. The increase in ALT activity in acute liver disease is 5-10 times. Increased activity of ALT for a long time or its increase in the late stages of the disease indicates the onset of massive liver necrosis.

Causes of high ALT (ALAT)

High ALT activity in the blood is detected in the presence of such pathologies:
  • acute hepatitis
  • obstructive jaundice
  • administration of hepatotoxic drugs (eg, some antibiotics, lead poisoning)
  • collapse of a large tumor
  • liver cancer or liver metastases
  • extensive myocardial infarction
  • traumatic muscle injury
Patients with mononucleosis, alcoholism, steatosis (hepatosis) who underwent heart surgery may also experience a slight increase in ALT activity.

In severe liver diseases (severe cirrhosis, liver necrosis), when the number of active liver cells is reduced, as well as with a deficiency vitamin A B6, observed in the blood decrease in ALT activity.

How to take an analysis for ALT (AlAT)?

Blood to determine the activity of ALT is taken from a vein, in the morning, on an empty stomach. No special diet is required. However, you should consult with your doctor and stop taking medications that cause a change in ALT activity for several days. ALT activity is assessed by an enzymatic method, which is specific, quite simple to use and does not require long and special sample preparation.

Aspartate aminotransferase (AST, ASAT)

AST - the structure and function of the enzyme
Aspartate aminotransferase (AST, AST) is an enzyme from the group of transaminases that transfers the amino acid aspartate from one biological molecule to another. The coenzyme AST is vitamin B6. AST is an intracellular enzyme, that is, it is normally found in cells. In cells, the enzyme may be present in the cytoplasm and mitochondria. The highest activity of AST was found in the heart, liver, muscles and kidneys. The blood contains mainly the cytoplasmic fraction of AST.

Aspartate aminotransferase (AST / AST) norm

Higher values ​​of AST activity in healthy people are possible (physiological) with excessive muscle exertion, taking certain medications, such as echinacea, valerian, alcohol, large doses of vitamin A, paracetamol, barbiturates, antibiotics, etc.

The activity of AST in the blood serum increases 4-5 times in myocardial infarction and remains so for 5 days. If AST activity is kept at a high level and does not decrease within 5 days after an attack, then this indicates an unfavorable prognosis for a patient with myocardial infarction. If there are still increases in the activity of the enzyme in the blood, then this fact indicates an expansion of the infarct zone.

With necrosis or damage to the liver cells, AST activity also increases. Moreover, the higher the activity of the enzyme, the greater the degree of damage.

Why is Aspartate aminotransferase (AST, AST) increased?

An increase in blood AST activity is present in the following cases:
  • hepatitis
  • liver necrosis
  • cirrhosis
  • liver cancer and liver metastases
  • myocardial infarction
  • hereditary and autoimmune diseases of the muscular system (Duchenne's myodystrophy)
  • hepatosis
  • cholestasis
There are a number of pathological conditions in which an increase in AST activity also occurs. These conditions include - burns, injuries, heat stroke, poisoning with poisonous mushrooms.

Low AST activity observed with a deficiency of vitamin B6 and the presence of extensive liver damage (necrosis, cirrhosis).

However, the clinic uses the determination of AST activity mainly for diagnosing damage to the heart and liver. In other pathological conditions, the activity of the enzyme also changes, but its change is not specific, therefore, it is not of high diagnostic value.

De Ritis coefficient. How to distinguish a heart attack from liver damage

For differential diagnosis of damage to the liver or heart, the de Ritis coefficient is used. The de Ritis coefficient is the ratio of AST/ALT activity, which is normally 1.3. An increase in the de Ritis coefficient above 1.3 is characteristic of myocardial infarction, and a decrease below 1.3 is detected in liver diseases.

Alkaline phosphatase (AP)

Alkaline phosphatase (AP) is a membrane enzyme that is localized in the brush border of the bile ducts. ALP can be intestinal, placental and non-specific (in the tissues of the liver, kidneys and bones). This enzyme is key in the metabolism of phosphoric acid.

Normal blood alkaline phosphatase

The activity of alkaline phosphatase in the blood of healthy people increases ( physiological enhancement) with an overdose of vitamin C, calcium and phosphorus deficiency in the diet, oral contraceptives, hormonal preparations of estrogens and progesterones, antibiotics, sulfonamides, magnesia, omeprazole, ranitidine, and so on.

Alkaline phosphatase in the diagnosis of diseases of the liver and biliary tract
Determination of ALP activity in case of suspected liver disease has a high specificity and diagnostic value. With obstructive jaundice, there is an increase in blood alkaline phosphatase activity by 10 times relative to the norm. The definition of this indicator is used for laboratory confirmation of this particular form of jaundice. To a lesser extent, an increase in the activity of alkaline phosphatase occurs in hepatitis, cholangitis, ulcerative colitis. In addition to the high activity of alkaline phosphatase in the blood, there are conditions in which the activity of the enzyme is reduced. First of all, this phenomenon develops with a lack of zinc, magnesium, vitamins B12 or C (scurvy) in the diet nutrition. Low blood alkaline phosphatase activity also accompanies the following pathological conditions of the human body - anemia, insufficiency of placental formation in pregnancy, hyperthyroidism and disorders of growth and bone formation.

How to take an alkaline phosphatase test?

To determine the activity of alkaline phosphatase, blood is taken from a vein, in the morning, on an empty stomach. Compliance with a special diet is not required. You need to pay attention to the fact that some drugs can reduce or increase the activity of alkaline phosphatase, so you should consult your doctor if you should stop taking these drugs for a short period of time. In modern laboratories, enzyme activity is assessed by the rate of the enzymatic reaction. This method has high specificity, simplicity, reliability and does not require large time expenditures for analysis.

So, we examined the main enzymes, the activity of which is determined in a biochemical blood test. It should be remembered that the diagnosis cannot be based only on laboratory data, it is necessary to take into account the anamnesis, clinic and data from other examinations. Therefore, it is advisable to use the given data for consultation, but if any deviations from the norm are detected, you should consult a doctor.

Amylase is a biologically active enzyme produced mainly by the pancreas and, to a lesser extent, by the salivary glands. Role in the body - participation in metabolic processes associated with carbohydrates. Amylase is divided into two types - pancreatic amylase, which is produced by the pancreas, and alpha-amylase, or total body amylase. It breaks down starch into simple saccharides. Without alpha-amylase, the normal functioning of the digestive system of the body is impossible.

The norm of amylase in the blood. Result interpretation (table)

Before talking about the rate of amylase in the body, you need to understand what kind of amylase we are talking about. Alpha-amylase is a digestive enzyme necessary for the body, without which the breakdown of carbohydrates is impossible. Normally, its content is:

  • in young children, up to 2 years - 5 - 65 U / l,
  • older than 2 years and up to 70 - 25 - 125 U / l,
  • in older people - 20 - 160 U / l.

Pancreatic amylase is a component of alpha-amylase. Usually its level is highlighted on a separate line. This enzyme is actively produced by the pancreas in the presence of some inflammatory processes in it. Therefore, the normal content of pancreatic amylase should be as follows:

  • in newborns up to six months - less than 8 U / ml,
  • from six months to 12 months - less than 23 U / ml,
  • in persons older than 1 year - less than 50 U / ml.

Blood testing for amylase is usually ordered if a patient is suspected of having chronic or acute pancreatitis. Although changes in the concentration of this enzyme are quite characteristic of some other diseases. The rate of amylase in the blood is determined by biochemical analysis. Blood sampling for him is made from a vein, in the morning and on an empty stomach.


If amylase is elevated, what does it mean?

A smooth increase in the level of amylase in the blood occurs within a few hours from the onset of an attack of acute pancreatitis. After the attack ends, this indicator returns to normal again, but this takes several days. Acute pancreatitis can cause amylase levels to be as high as 5 or 6 times normal. However, if amylase is elevated, this does not always indicate pancreatitis, moreover, sometimes even during an attack and after it, amylase can remain within the normal range. Therefore, to make an accurate diagnosis, it is necessary to take into account other markers, for example, the level of lipase.

Other diseases that can cause an increase in the level of amylase in the blood:

  • pancreatic cyst,
  • malignant tumor of the pancreas,
  • diseases of the biliary tract and gallbladder,
  • chronic renal failure,
  • inflammatory processes in other organs of the abdominal cavity,
  • cystic fibrosis,
  • alcohol intoxication,
  • ectopic pregnancy,
  • diabetes,
  • parotitis,
  • insufficient activity of the salivary glands, for example, if they are damaged.

Taking certain medications can also lead to a similar effect. Therefore, before taking a blood or urine test for amylase levels, be sure to tell your doctor about all the medicines that you have taken recently. Including hormones and oral contraceptives.

If amylase is lowered, what does it mean?

A low amylase level is considered if less than 100 U / l of serum is found in the results of the analysis. This may be due to various reasons. For example, decreased amylase may result from acute or chronic hepatitis. With this disease, there is a violation of carbohydrate metabolism in the body, because of which all enzymes, and especially amylase, experience increased stress. And although the synthesis of amylase occurs uninterruptedly, much more is consumed. Therefore, a blood test shows an insufficient amount of this enzyme.

The rate of amylase in the blood may decrease as a result of a malignant tumor of the pancreas - tissue degeneration occurs here, and the production of the enzyme is disrupted. This phenomenon is called pancreatic insufficiency. It can also be caused by trauma or if the pancreas has been removed by surgery.

If amylase is lowered, this may be due to severe cystic fibrosis.

Remember that it is impossible to establish an accurate diagnosis based on the results of a single analysis. To clarify and confirm it, the specialist must take into account all the cumulative factors, and, if necessary, appoint an additional examination.

Participates in the breakdown of polysaccharides (starch, glycogen, etc.) to glucose, maltose and dextrins.

Synonyms:
Diastasis
1,4-a-D-glucan hydrolase
Serum amylase
Blood amylase
Amylase total
Total alpha amylase

Designation in analyzes:
Amy
alpha-amylase
AML
diastase
serum amylase
blood amylase

Main producers alpha-amylases:

  • Pancreas
  • Salivary glands (parotid, sublingual, submandibular, minor)

In a smaller amount this enzyme is found in the appendages of the uterus, intestines, lungs, muscle and adipose tissue, kidneys and liver.

Alpha-amylase functions in the oral cavity and intestinal tract.

In a healthy person, it enters the blood in very small quantities, as a result of the normal physiological renewal of the cells of the organs listed above.

Total or serum alpha-amylase in the blood is represented by two isoenzymes:

  • Pancreatic alpha-amylase (P-type) ≈40%
  • Salivary alpha-amylase (S-type) ≈60%

In pathological conditions associated with damage to the tissues of the pancreas, the total amylase in the blood increases due to an increase in
pancreatic P-alpha-amylase.

In diseases of the salivary glands, total serum amylase increases due to the fraction of salivary S-alpha-amylase.

In the vast majority of cases, an increase in the activity of total amylase in the blood is associated with pancreatic disease. Therefore, the analysis of amylase isoenzymes (P- or S-) is carried out according to special indications: to confirm the diagnosis of "pancreatitis"; for differential diagnosis of pathology of the pancreas, salivary glands, ovaries, fallopian tubes, lungs, etc.

The alpha-amylase molecule is small, so it is well filtered from the blood by the kidneys. With an increase in the enzyme in the blood, its content in the urine also increases.

Alpha-amylase in the blood - the norm in women and men


The average rate of total alpha-amylase in the blood of adult women and men is the same

Amylase in the blood - the norm in women and men by age
/table/

In newborns, children under one year old, the synthesis of a-amylase is insignificant, therefore the content of the enzyme in the blood is 2-5 times less than in adults. As complementary foods are introduced and the digestive system develops, amylase synthesis increases, and the level of the enzyme in the blood gradually reaches “adult” values.

The norm of total amylase in the blood in women and men by age Pancreatic amylase - the norm in women by age

/ For a more accurate interpretation, refer to local laboratory standards. Methods for determining the activity of amylase in the blood are different /

When is an amylase test needed?

Indications for carrying out
blood test for a-amylase:

  • Sharp pain in the abdomen.
  • Diagnosis of acute diseases of the pancreas.
  • Evaluation of the effectiveness of the treatment of pancreatic pathology (including cancer).
  • Differential diagnosis of diseases of the gastrointestinal tract.
  • Parotitis (inflammation of the parotid salivary glands).
  • Cystic fibrosis.
Greatest value blood test for total amylase - diagnosis of the cause of acute abdominal pain.

Clinical Significance Serum amylase analysis – detection and management of acute pancreatic disease. The main reasons for the increase
total alpha-amylase in the blood:

– Acute pancreatitis
- Abdominal injury
- Peritonitis
- Chronic pancreatitis
Tumor, cyst or cancer of the pancreas
- Acute cholecystitis, including calculous
- Acute infectious hepatitis
- Perforation of gastric ulcer
- Acute circulatory disorders of the abdominal organs, intestinal infarction
- Intestinal obstruction, intestinal perforation
- kidney failure
- Crohn's disease
- Mumps
– Macroamylasemia
- Ectopic pregnancy
- Ovarian pathology, salpingitis
- Diabetic ketoacidosis

It is obvious that an increase in the activity of total α-amylase in the blood is observed not only in the pathology of the pancreas. But an increase in the indicator by 3-5 times almost always has a pancreatic origin.

A marked elevation of 10-fold or more in serum alpha-amylase with severe abdominal pain suggests acute pancreatitis*. * Pancreatitis - inflammation of the pancreas

Pancreatitis - why does alpha-amylase increase in the blood?

The pancreas (pancreas) is a small organ of the abdominal cavity, pale yellow in color, up to 15 cm in length, weighing approximately 100 g. It is located behind the stomach.


Up to 10% of pancreatic tissue produces pancreatic hormones (insulin, glucagon, and somatostatin).

Up to 90% of the organ mass is represented by acinar tissue producing pancreatic juice. It includes: electrolytes dissolved in water and three groups of digestive enzymes:

  • Amylases (active) - break down carbohydrates.
  • Lipases (active) - digest fats.
  • Proteolytic enzymes or proteases (in an inactive form) - normally, proteases are activated only in the intestine, where digestion (proteolysis) of food proteins occurs.

Pancreatic juice is collected in the central (Wirsung) duct of the pancreas. Then it flows into the common bile duct and (together with bile) is collected in the hepatic-pancreas (Vater) ampoule. The entry of the "digestive mixture" into the duodenum regulates the sphincter of Oddi.


Normally, pancreatic proteases are activated (trypsinogen to trypsin, etc.) and exhibit their aggressive "digesting" properties exclusively in the cavity of the small intestine.

As a result of mechanical injury, blockage of the excretory ducts or under the influence of alcohol, the pancreatic tissue is damaged, inflamed, and swollen. The membranes of acinar cells become hyper-permeable. Pancreatic enzymes “leak out”, are immediately activated and evade into the blood, destroying (self-digesting) pancreatic tissue.

  • Acute pancreatitis- this is an inflammatory-destructive lesion of the pancreas as a result of the activation of pancreatic proteases within the pancreas itself.

Acute pancreatitis is accompanied by a massive release into the bloodstream of all "pancreatic" enzymes, including lipase.

It is lipase that is a strictly specific indicator of the destruction of the pancreas: if its level is elevated, the diagnosis of "pancreatitis" is beyond doubt.



The main causes of acute pancreatitis:
1. Alcohol abuse
2. Gallstone disease

Other reasons:
- Infections (viral, bacterial).
- Injuries to the pancreas as a result of a strong blow to the stomach (during a fall, fight, etc.)
- Pathological changes in the area of ​​the common bile duct, the papilla of Vater, the sphincter of Oddi (reflux of bile into the pancreatic ducts).
– Diseases of the duodenum (duodenitis, etc.)
- Helminthiasis.
- Inflammatory diseases of the liver and biliary tract.
- Acute circulatory disorders in the vessels of the pancreas: thromboembolism, prolonged spasm, blockage with fat droplets or atherosclerotic plaques, etc.
- Toxic poisoning (mercury, arsenic, phosphorus, etc.) or drug damage to pancreatic tissues.

The first symptoms of acute pancreatitis are
sudden sharp pain in the upper abdomen (epigastrium) or in the navel. The pain may radiate to the back, left hypochondrium, left shoulder and shoulder blade. Sometimes the pain captures a wide strip from the hypochondrium to the hypochondrium, it is girdle. The pain may be accompanied by repeated vomiting that does not bring relief, distension in the abdomen, flatulence, belching, fever. Appetite is absent, the chair is more often detained.


The pain subsides somewhat in the sitting position, lying on the stomach or bending over on the left side.

How does the level of a-amylase in the blood change in acute pancreatitis

If the levels of serum a-amylase after an acute attack of pancreatitis do not return to normal for a long time, the development of a pancreatic pseudocyst is assumed.



An increase and then a rapid decrease in high levels of a-amylase and other digestive enzymes in the blood in acute pancreatitis is a poor prognostic sign. In 20% of cases, acute pancreatitis is very severe and is a life-threatening condition.

Increased alpha-amylase in the blood in chronic pancreatitis

Chronic pancreatitis- This is a gradually developing, long-term inflammation of the pancreas. Sometimes it proceeds without acute attacks, almost asymptomatically.

In chronic pancreatitis, the activity of a-amylase in the blood and urine can be normal, increased, or even low. Therefore, in this situation, the analysis of serum amylase activity is uninformative.

Used to diagnose chronic pancreatic diseases provocative tests(with prozerin, with glucose):
Normally, after the introduction of prozerin (or glucose intake), the level of a-amylase in the blood rises to 60% of the original.
In the pathology of the pancreas with severe secretory insufficiency, amylase in the blood increases by 30% of the initial value.

Increased a-amylase in pancreatic cancer

The activity of a-amylase in the blood and urine in malignant tumors of the pancreas may be slightly increased, may remain normal. This test is not used to diagnose pancreatic cancer.

Increased a-amylase in macroamylasemia

An isolated rise in serum α-amylase is an important diagnostic feature of rare benign macroamylasemia.

This condition is due to the binding of several molecules of a-amylase to plasma proteins. Due to their large size, macroamylase aggregates cannot pass through the glomerular membranes of the kidneys, and therefore accumulate in the blood.

Alpha-amylase in the blood of pregnant women

During pregnancy, blood amylase may be slightly increased. This does not contradict the permissible physiological norm.

Medicines that increase alpha-amylase in the blood:

Blood alpha-amylase is lowered - causes

An abnormal decrease in alpha-amylase in the blood is very rare and indicates a decrease in pancreatic function or damage to other external secretion glands associated with hereditary or infectious diseases.

A low blood amylase level has no clinical significance. In practice, it is important to interpret the high levels of the enzyme.

What is the danger of increasing a-amylase in the blood?

By itself, an increase in alpha-amylase in the blood is safe. But it is associated with inflammation of the pancreas and the entry of active proteases into the blood, which damage both the pancreas and, as a result, other organs.

Exceeding the normal values ​​of alpha-amylase in the blood more than 3 times- a marker of inflammation of the pancreas

As a result of evasion of active proteases, the level of kinins, histamine, and other bioactive substances in the blood increases. General microcirculatory disorders develop, collapse is possible.

What to do if pancreatic amylase is elevated

A significant increase in pancreatic amylase in the blood is an indication for hospitalization.

Prehospital activities aimed at eliminating pain and suppressing the activity of pancreatic enzymes.

Painkillers: Baralgin, Analgin, Tramal.

To eliminate spasm: Papaverine, Galidor, No-Shpa.

Antispasmodic anticholinergics: Buscopan, Metacin.

Normalization of the tone of the sphincter of Oddi: Duspatalin.

Inhibition of the activity of pancreatic enzymes: Kvamatel (famotidine).

Antihistamine, antiserotonin, edema-reducing drugs: Tavegil, Suprastin, Dimedro, Peritol.

In severe forms of acute pancreatitis, measures are taken in the intensive care unit. To reduce enzymatic toxemia on the first day of the disease, Kontrykal or other inhibitors of proteolysis are administered intravenously. Antibacterial therapy is prescribed.

After the acute situation subsides, pancreatic enzymes that do not contain bile are prescribed in an intermittent course of up to 3 months (2 weeks of admission, 10 days of withdrawal): Pancreatin, Mezim-forte, Creon, Pancitrate (1 tablet 3 times a day with meals) .

Diet to lower pancreatic amylase

In the first 1-2-3 days acute condition - hunger.

Then gradually introduce into the diet:
- pureed cereals on the water;
- slimy pureed soups on the water;
- milk;
- weak tea with crackers;
- omelette;
- cottage cheese;
- low-mineralized water without gas, 50-100 ml 5-6 times a day: Slavyanovskaya, Essentuki No. 4, Borjomi, Naftusya.

From the 7th day it is allowed:
- vegetable, potato puree;
- steam cutlets, boiled fish;
- White bread;
- baked apples, fruit puree.

During the recovery period, phytotherapy can be used (after consultation with the doctor).

Herbal remedy for pancreatitis
Potentilla goose - 1 tablespoon
Celandine - 1 tbsp. l.
Calendula - 1 tbsp. l.
Marshmallow root - 1 tbsp. l.

Brew 1 tablespoon of the collection with 1 cup of boiling water, heat in a water bath for 15 minutes. Sue. Take 1/3 cup 3 times a day 15 minutes before meals. Reception course: 1 month.

Diet No. 5P with increased amylase and pancreatitis

Basic principles supply:

  • Avoid alcohol completely.
  • Cook food for a couple or boil, chop.
  • Meal mode: in small portions, 4-6 times a day.

What is prohibited?
Rich broths: meat, chicken, fish, vegetable, especially mushroom.
Hard boiled eggs, fried eggs.
Fatty meats, poultry, fish, game.
Pork fat, beef and mutton fat.
Raw: cabbage, radish, radish, sorrel, spinach, green onion.
Smoked meats, spices, spicy snacks, canned food, mushrooms, sausages.
Muffin, fresh pastries, black bread, ice cream, fatty desserts, cocoa, chocolate.
Alcohol in any form.

What to limit?
Fats: butter - 30 g, vegetable - 20 g per day.
Fast carbohydrates, sugar.
Coarse fiber, boiled (stewed) cabbage.
Too sour, sweet raw fruits.
Pastries, confectionery, coffee, strong tea.

What is allowed?
Dried white bread.
Boiled, stewed vegetables.
Any porridge, pasta.
Lean meat, poultry, fish (steam cutlets, meatballs, soufflés, rolls, etc.)
Eggs in the form of a protein omelet. Soft-boiled 1 piece per day.
Milk, non-sour cottage cheese, Dutch, Adyghe cheese.
Baked apples, fruit puree.
Rosehip broth, weak tea, kissels and compotes on xylitol.

The therapeutic diet is observed for at least 6 months. In the future, you should adhere to diet No. 5 according to Pevzner (watch the video).

How to donate blood for alpha-amylase

To determine the activity of alpha-amylase, blood is taken from a vein (5 ml)

In an acute condition, blood can be donated at any time.

With a planned analysis, blood is given in the morning, strictly on an empty stomach: do not eat, do not drink.

Do not smoke before donating blood.

Falsely elevated the results of a blood test for alpha-amylase may be in chronic renal failure, while taking the medications listed above.

Falsely low- Against the background of hypercholesterolemia (high cholesterol in the blood).

A slight isolated increase in alpha-amylase in the blood
is not sufficient reason to make a diagnosis.

  • Tags:

Save the article!

VKontakte Google+ Twitter Facebook Cool! To bookmarks

Random articles

Up