How is collagen synthesized?
Collagen synthesis
Previous sections have anticipated the autonomous ability of the human body to synthesize its own collagen and how that capacity is suffering a slow and irreversible deterioration with the passage of time, to the point of becoming half of the original at the approximate age 30 years old
Likewise, it has been apostilled about certain situations that accentuate this deterioration, being the most relevant the one that happens with the arrival of the climacteric in the female sex, something that is explained by the strong dependence of the intervention of the estrogens that characterizes the synthesis of collagen .
If we propose to select a truly key factor in accentuating this deceleration in the ability to synthesize collagen, perhaps we should point to what is known as " oxidative stress " derived from the accumulation of free radicals in cellular metabolism, among whose causes, to its Psychological stress, environmental pollution, excessive exposure to sunlight, a deficit of restful sleep, or the intake of medicines and stimulants , all of which can be enhanced with a diet lacking in vitamins, minerals and sources natural collagen (which will be discussed in detail in later sections).
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oxidative stress
Avoid degradation of collagen synthesis
In this order of things, we must bear in mind that the available weapons to stop the degradation of collagen synthesis point to two complementary fronts: on the one hand, to reduce oxidative stress and, on the other, to try to ingest the greatest amount of nutrients that contain principles favoring the synthesis of this capital protein structure. It is evident the advisability of eating a diet rich in collagen precursor foods, such as those that will be pointed out later, a diet in which the consumption of those foods that produce, albeit transiently, hyperglycemia, should be postponed, since This is the so-called glycation, a process by which surplus sugar molecules adhere to the collagen fibers to the detriment of their strength and flexibility.
Collagen synthesis
Let's go on to describe in detail how the synthesis of collagen develops in the bowels of the organism. This has its beginning in the cellular cytosol , where chains of isolated amino acids are made that are transported to the rough endoplasmic reticulum, that ribosome rich organelle where the remains of lysine and proline undergo the necessary hydroxylation to transform into the two main amino acids, together with glycine, from the collagen molecule: hydroxyproline and hydroxylysine. For this chemical reaction to take place it is essential that there is a sufficient amount of iron in its reduced form (+3) and vitamin C, both cofactors strictly necessary for two enzymes, prolyl-4-hydroxylase and lysyl-hydroxylase, trigger the reaction.
What is the importance of hydroxylation of both amino acids?
proline
Specifically, as far as proline is concerned, it is responsible for making collagen a more thermostable protein than most, while that of lysine is what makes the formation of the triple helical characteristics that collagen adopts as a structure high school.
After the hydroxylation arrives another determinant phase carried out by enzymes present in the endoplasmic reticulum, the glycosyl transferases , responsible for glycosylation, that is, to join a molecule of glucose, hydroxylysine residues so that this triple helical figure is perfectly assembled with the ends occupied by free polypeptides, which constitute the starting point of the classic folding in globular form that characterizes the quaternary structure of collagen.
Golgi apparatus Finally, the triple helices are transported to another prominent organelle of the cellular cytoplasm, the Golgi apparatus , in which they are subjected to a sulfation reaction involving the amino acid cysteine rich in sulfur, to which is added the phosphorylation of its homolog serine.
At the end of these stages, the resulting metabolite is the procollagen or immature form of collagen, whose fate is its evacuation by the fibroblast to the intercellular matrix using its secretory vesicles. In this extracellular fluid, procollagen becomes the substrate of new enzymes, peptidases and proteases, which give rise to the tropocollagen molecule, the stage immediately prior to the definitive collagen fiber. The dimensions of the tropocollagen are 300 nanometers in length and 1.4 in diameter and are formed by three polypeptide chains, of about 100,000 daltons of molecular weight each, called non-helical α-chains, of levorotatory configuration and each of which is composed of a polypeptide containing a tandem replica of three amino acids.
Defects of collagen synthesis
In all described above can be given a series of Defects of collagen synthesis .