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FrançaisA still incomplete vision of the articulation
When talking about joint disorders, we always come back to the same concepts:
- cartilage that wears out
- inflammation
- the lack of collagen
All this is right.
But it is insufficient to explain what we observe on a daily basis.
Two patients may have:
- the same age
- the same constraints
- sometimes even similar radios and MRIs </ul
and yet, a completely different evolution.
Why?
Because there is a piece missing in the reasoning: the body’s ability to repair what has been damaged.
Micro-traumas: a daily reality
We often tend to associate an injury with a 'big shock'.
A fall.
An accident.
A violent movement.
These "big shocks" are rather rare. And yet micro-traumas are created every day. Because joint tissues do not only damage during a violent shock.
They are damaged... all the time.
Every step.
Every move.
Each constraint.
On a small scale, this creates permanent micro-lesions. It’s completely normal. It’s even the physiological functioning of the tissue.
The problem is therefore not the micro-trauma itself. The problem is the ability to repair the lesions behind.
What the body actually does after a trauma or micro-trauma
After each micro-lesion, fortunately the body does not reconstruct everything from scratch. He starts by doing something much smarter: he sorts out.
We can summarize it in three situations:
- 1 - What is too damaged is eliminated,
- 2 - What can be recovered is repaired,
- 3 - What is missing is rebuilt.
It is precisely in the second category that everything takes place.
Chaperone proteins: the 'restorers' of the living
This is where the chaperone proteins, also known as HSP (Heat Shock Proteins), come in.
Their role is not to make collagen. It is much more subtle: they restore damaged proteins.
Concretely, what do they do?
To function, a protein must have a very precise shape. A three-dimensional structure.
During stress (mechanical, oxidative...), this structure can deform.
The protein is not necessarily destroyed. But it becomes ineffective.
The HSPs will then intervene as a kind of "maintenance service".
They will:
- attach to the altered protein,
- stabilize it,
- prevent it from clumping or degrade,
- help it regain its functional form. </ul
This is called protein folding
If the protein is really too damaged: they direct it towards its degradation..
And in articulation?
In joint tissues, this repair mechanism mainly concerns collagen.
Collagen is everywhere.
In:
- the ligaments,
- the tendons,
- the articular capsule.
And it is constantly subjected to micro-lesions.
Some chaperone proteins, like HSP47, are specialized in collagen repair.
They allow :
- a coherent structure,
- an adapted mechanical resistance.
In other words: they condition the quality of the fabric.
A key point often forgotten: the activation of HSPs
Contrary to what their name suggests, HSPs are not activated solely by heat.
They respond to a simple principle: moderate stress activates repair.
Concretely:
- a physical activity
- of controlled mechanical stresses
- a mild oxidative stress. Conversely: absence of slightly active system stimulation excess system stresses exceeded. It is an equilibrium.
Another way to see the articulation
We often talk about: «feeding the cartilage» or «making collagen». But as we have seen, this is only part of the story. The other part, known to me, is: the body’s ability to repair what is already there.
And this is precisely the role of chaperone proteins.
Conclusion
With each micro-trauma, the organism must decide whether to: throw away, repair... or rebuild.
Chaperone proteins are involved in this process.
They allow for the restoration of altered proteins, rather than relying solely on their renewal.
And it is this ability to repair that largely determines the quality and durability of joint tissues.
Article written by the scientific team Cellula Pharm. Expert laboratory in cellular health and micronutrition.
