What is a collagenase?
A collagenase is an enzyme that is able to break down collagen. Since collagenases break bonds, they belong to the group of proteases. Like every enzyme, collagenase also consists of a series of amino acids. These amino acid chains are folded and ultimately always have a specific function.
The job of collagenase is to break bonds between two amino acids. One of these amino acids is always proline, while the second can vary. Since collagen is made up of a lot of proline, it is broken down by the collagenases and finally broken down.
There are a total of five different collagenases in humans, each specializing in different types of collagen.
What are the tasks and functions of collagenase?
The function of collagenases is to break bonds between the amino acid proline and various other amino acids. So they belong to the proteases, rather than to enzymes that break bonds with the help of water.
The collagenases in the human organism are so-called matrix metalloproteases. This means that they are not only made up of amino acids, but also have a metal ion in the center. In the case of collagenases, this is a zinc ion in the center. With the help of this metal ion and a water molecule, the bond between proline and the second amino acid is split.
Proline occurs in large proportions in collagen, which makes up the main part of our connective tissue. It is the most important fiber component of various structures, such as skin, bones and cartilage.
Due to the collagen-degrading function of the collagenases, they are of great importance in wound healing. Damaged or dead tissue is split down by the collagenase and finally broken down. This guarantees optimal healing of the wound by removing the dead tissue.
In humans there are a total of five collagenases that specifically split different collagens. These are mainly located in the lysosomes, which are responsible for the breakdown of various molecules.
However, collagenases are not only found in humans, but also in bacteria. They are extremely important for the clostridia. These bacteria use their collagenases to destroy connective tissue so that they can spread better in the organism.
If you have any further interest in this topic, check out our next article below: Role of enzymes in the human body
Where is collagenase made?
Like most enzymes, the production of collagenase begins in the cell nucleus. During the transcription, a copy of a certain DNA segment is made that contains the information for this enzyme.
This mRNA leaves the cell nucleus through the nuclear pores and reaches the ribosome. This is where translation takes place and the enzyme is assembled by linking different amino acids.
However, the active collagenase is not created immediately, but an inactive precursor. This so-called procollagenase has to be activated before it can be used.
This activation takes place after translation and only when the collagenase is required. In order to convert the procollagenase into an active collagenase, a short amino acid sequence has to be cut off.
This inactive precursor guarantees a controlled use of the collagenases, otherwise they would immediately fulfill their function of breaking down connective tissue, even if the tissue is healthy.
What are the normal collagenase levels?
There is currently no standard value for collagenase in the human organism. This enzyme is found in many different human organs, such as the exocrine part of the pancreas. Here the collagenase has the task of shrinking food.
If such cells perish, as in the case of an inflammation of the pancreas, for example, more collagenases are secreted into the blood. However, one does not measure the concentration of collagenase, but uses other enzymes, such as lipase in this case.
One reason for this is the widespread occurrence of collagenase. This fact makes the enzyme unspecific and is therefore not suitable for laboratory analysis.
How does it work in Dupuytren's disease?
Dupuytren's disease is a disease associated with an increase in tissue in the area of the palmar aponeurosis of the hand. As a result, it is no longer possible for the patient to fully stretch their fingers.
The little finger is particularly affected. This can often no longer be stretched at all and lies completely in the palm of the hand. In this case one speaks of a flexion contracture.
How this disease develops is not known. However, there is a familial accumulation and there are also suspected risk factors, such as smoking cigarettes or the consumption of alcohol.
Patients suffer from a lack of mobility of the hands and both vessels and nerves can be damaged by Dupuytren's disease.
Various surgical procedures are available as forms of therapy, such as the removal of the palmar aponeurosis (Aponeurectomy) or the splitting of fascia.
However, one can also try to counteract the disease with so-called collagenase injections. The injected collagenases are supposed to break down the excess connective tissue.
These enzymes are injected directly into the thickened palmar fascia, which consists largely of collagen fibers. This loosens the tissue and then the affected finger can be stretched as far as possible.
When the collagenase injection is successful, the tissue is softened to such an extent that the thickened cord of the palmar aponeurosis tears through the finger extension and the patient can move the hand normally again.
Are you interested in other treatment options for Dupuytren's disease? Read our next article below: Therapy of Dupuytren's disease
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Further general information may also be of interest to you:
- Pancreatic enzymes
- connective tissue
- The alpha amylase
- Dupuytren's disease