Where is trypsinogen produced?

The proenzyme trypsinogen is roughly formulated in the pancreas. This lies transversely in the upper abdomen on the left side of the stomach. The pancreas can also be divided into two parts:

The endocrine part produces hormones like insulin for the regulation of the sugar balance, which act within the body.
The exocrine part, which makes up the main part of the pancreas, produces pancreatic saliva, which contains the proenzyme trypsinogen and has an important function in digestion.

What are the standard values?

Since trypsinogen is normally passed on directly into the small intestine via the ducts of the pancreas, there is usually no trypsinogen in the blood, i.e. the normal values approach zero. Should it be the case that trypsinogen is detected in the blood, the findings definitely indicate a pathological process. Acute pancreatitis and cystic fibrosis, for example, are possible. Newborn screening tests for trypsin.

What does trypsinogen have to do with cystic fibrosis?

In cystic fibrosis, also known as cystic fibrosis, a mutation in the genome leads to an altered composition of the secretion of glands, which release their secretion to the body surface such as the intestine. This makes the secretion much more viscous, allowing it to be released more slowly. This is particularly critical in the case of the pancreas.Due to the longer retention time in the ducts of the pancreas, the secretion has an increased effect within the organ. As more trypsinogen is thus also activated to trypsin, the body digests its own substances, which can result in acute pancreatitis.

What is trypsin?

Trypsin is an enzyme that is formed from an inactive precursor, the proenzyme trypsinogen, and plays an important role in the digestion of proteins. The proenzyme trypsinogen originates from the exocrine part of the pancreas. This proenzyme is activated in two different ways.

Firstly, an amino acid chain consisting of six amino acids is split off with the aid of the enzyme enteropeptidase. Secondly, trypsin can activate itself. In this process, an amino acid chain of six amino acids is also split off.

Active trypsin can also convert the three pro-enzymes procarboxypeptidases, proaminopeptidases and chymotrypsinogen 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 categorized as an enzyme under the category of hydrolases.

This means that they can reversibly split compounds between amino acids by consuming water. The ability to split amino acid chains reaches a maximum in slightly basic pancreas with pH values between 7 and 8. This property is essential for the process of digestion.

After the enzymes of oral saliva, trypsin represents the second step in the cleavage of proteins. The enzyme does not split the amino acid chain of the proteins from the outside, but divides the entire chain into several small fragments, which are subsequently shortened by other enzymes so that they can be absorbed into the body through the intestinal mucosa. If trypsin is deficient, the digestion of proteins is disturbed.

In the following, fewer amino acids are absorbed into the body. Since some amino acids are essential for the human body, as they cannot be produced either by modifying existing amino acids or by their own synthesis, deficiency symptoms occur after some time, which can have serious consequences if left untreated. In addition, it can happen that the amino acid stores present in the body, such as the proteins of the muscles, are used, resulting in weight loss and reduced resilience.