What activates the enterokinase
Definition - What is Trypsinogen?
Trypsinogen is the inactive one Prepress, a so called Proenzyme, of an enzymemade in the pancreas, the pancreas. Together with the remaining pancreatic secretion, the so-called Pancreas, the proenzyme trypsinogen is released through the pancreatic ducts into the duodenum, part of the small intestine. This is where the activation to the enzyme trypsin takes place.
This enzyme is called "Hydrolase"categorized, that is, it is to able to cleave connections between individual amino acids. This process takes place in the Small intestine instead, which breaks the proteins that are ingested through food into smaller fragments of amino acids, which enables them to be absorbed into the body.
How is activation to trypsin done?
The activation from trypsinogen to trypsin can be done in two different ways. In both ways, activation does not take place in the area of the pancreas or its ducts, but only in the area of the duodenum, part of the Small intestine.
- For the one way in activation to trypsin is a further enzyme needed. This enzyme is produced in the brush border, i.e. the superficial cells, of the duodenum. It's called Enteropeptidase or Enterokinase. The enzyme is among the Hydrolases categorized. This means that they can reversibly cleave the compounds of individual amino acids that give the proenzyme trypsinogen its structure while consuming water molecules. In the Activation of trypsinogen to trypsin a chain of six amino acids, a so-called hexapeptide, is split off from the proenzyme trypsinogen while consuming water. This results in a shortened amino acid chain compared to before. The process is called limited proteolysis. However, the enzyme is now in his active form before and can split further amino acid chainsto order below To be able to break down and digest proteins.
- The second variant of activating trypsinogen to trypsin is by the already active enzyme trypsin shown. Trypsin can not only split exogenous proteins into smaller amino acid chains, it can too the body's own proenzymes like trypsinogen shorten by several amino acids. Trypsin particularly likes to split after the sixth amino acid of the trypsinogen. This means that a hexapeptide is split off, which converts the trypsinogen into its active form, trypsin. In addition to trypsinogen, active trypsin can convert three other enzymes that are important for digestion into their active form. Two factors that are not initially obvious are also important for activation. On the one hand, the effect of trypsin is particularly good at a slightly basic pH value of 7 to 8, which means that trypsinogen is increasingly activated. On the other hand, it becomes trypsinogen in the pancreas with a Trypsin inhibitor submitted. This prevents premature activation inside the pancreas and is only broken down in the duodenum.
Where is trypsinogen made?
The proenzyme trypsinogen is roughly formulated in the pancreas educated. This lies across the upper abdomen to the left of the stomach. The pancreas can still be divided into two parts:
- The endocrine partproduces hormones how insulin for the regulation of the sugar balance that work within the body.
- The exocrine partwhich makes up the major part of the pancreas, produces the pancreas, which is the proenzyme Trypsinogen and has an important function in digestion.
You might also be interested in: Functions of the pancreas
What are the normal values?
Because trypsinogen normally passes through the ducts of the pancreas forwarded directly to the small intestine is usually found no trypsinogen in the blood, that is, the standard values are approaching zero.
Should it be the case that trypsinogen detected in the blood is, the finding speaks in any case for one pathological process. Here, for example, comes an acute one Pancreatitis and a Cystic fibrosis in question. Trypsin tests are carried out as part of the newborn screening.
What does trypsinogen have to do with cystic fibrosis?
In the cystic fibrosis, also Cystic fibrosis called, a mutation in the genome leads to a changed composition of secretions from glandsthat release their secretions to the surface of the body such as the intestines. The secretion becomes clear more viscousmaking it released slowly can be.
This is particularly critical in the case of the pancreas. Due to the longer time it remains in the passages of the pancreas the secretion acts more within the organ. Since trypsinogen is thus also increasingly activated to trypsin, one occurs Digestion of your own bodywhat in a acute pancreatitis can end.
Further information on the topic can be found here:Cystic fibrosis
What is trypsin?
Trypsin is an enzyme that arises from an inactive precursor, the proenzyme trypsinogen important role in the digestion of proteins plays. The proenzyme trypsinogen comes from the exocrine part of the pancreas. This proenzyme is activated in two different ways. On the one hand, an amino acid chain made up of six amino acids is split off with the aid of the enzyme enteropeptidase. On the other hand, trypsin can activate itself. Here, too, an amino acid chain made up of six amino acids is split off. Active trypsin can also do the three proenzymes Procarboxypeptidases, Proaminopeptidases and Chymotrypsinogen convert to their three active enzymes by splitting off an amino acid chain. These three enzymes are also involved in the digestion of proteins.
Trypsin is classified as an enzyme under the category of Hydrolases categorized. That means they can reversibly cleave connections between amino acids with consumption of water. The ability to split amino acid chains reaches a maximum in the slightly basic pancreas with pH values between 7 and 8. This property is essential for the digestive process.
After the enzymes in the saliva of the mouth, trypsin is the second step in the cleavage of proteins. The enzyme does not cleave the amino acid chain of the proteins from the outside, but rather divides the entire chain into several small fragments, which are then reduced by further enzymes so that they absorbed into the body through the intestinal mucosa can be.
More information can be found here: Trypsin
What happens with a trypsin deficiency?
With a lack of trypsin, the digestion of proteins is disturbed. The following are fewer amino acids absorbed into the body. Since some amino acids are essential for the human body, as they can neither be produced by modification of existing amino acids nor by their own synthesis, it happens after some time Deficiency symptomswhich, if left untreated, can have serious consequences.
It can also happen that made use of the amino acid stores present in the body, such as the proteins of the muscles becomes, making it a Weight reduction and to decreasing resilience comes.
Alpha-1 antitrypsin deficiency
Alpha-1 antitrypsin deficiency is often caused by one Genetic defect. Alpha-1 antitrypsin is one enzyme, the other Inhibits enzymes in their function. The enzymes that are inhibited normally have the task of breaking down proteins, which causes them to lose their function. Thus, Alpha-1-Antitrypsin can also be used as Proteinase inhibitor are designated.
The enzymes that go through Alpha-1 antitrypsin are inhibited, especially join inflammatory processes on and are mainly Chymotrypsin, trypsin, plasmin, elastase and Thrombin.
Here comes the inhibition of the Elastase special meaning to it. The elastase usually breaks down elastin, which is mainly in the lung occurs. Elastin is a structural protein that is essential for the Elasticity of the lungs responsible for. At a insufficient supply of elastase inhibitors such as alpha-1-antitrypsin it can lead to an increased activity of elastase in the lungs. Here, like everywhere else in the body, elastase breaks down proteins, but this affects the body's own tissue in the lungs. This leads to massive damage to the lung tissue, causing a Impairment of lung function is inevitable. Symptoms that develop from it include Cough, shortness of breath and a narrowing of the airways. In addition, the liver, which is mainly responsible for the production of elastase, can show elevated liver values and can be further damaged by biliary congestion.
More information can be found here: Alpha-1 antitrypsin deficiency
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