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The root of the word “collagen” is very apt in two ways. Collagen means, “glue producer” (kola = glue in Greek) – as glue was derived from early times by boiling animal hooves and sinew to make glue.
But for us in the beauty industry the “glue” idea is also applicable, as collagen is the “glue” that keeps the connective tissue together and healthy collagen is needed for keeping that ageless face.
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Also look at fibroblast and elastin.
Collagen is a protein and is found in all body parts, including the largest organ of the body - the skin – and is made up of three strands of repeating amino acids coils coiling into the unique collagen triple helix.
Various types of collagen are found in the body and are required to build new cellular structures – like skin – and to repair any damage caused.
Types I, III and V are specific collagen types involved in the health of your skin.
Together with soft keratin, the collagen and elastin fibers are responsible for the strength and elasticity of the skin – and degradation of the collagen leads to aging and accompanying wrinkles.
With the onslaught of normal aging, the collagen in our skin is under attack and various factors hasten the degradation of collagen.
Sun tanning and sun exposure is one of the main culprits of collagen deterioration in our skin and inflammation also destroys collagen.
Large amounts of free radicals – which are formed during normal body functions (oxidation), can also destroy collagen – and here a person can specifically look at pollution and toxins in your environment, fat filled diet as well as cigarette smoking and consuming alcohol.
While on the point of cigarette smoking, it is important to note that the body requires vitamin C in order to make collagen – and without it, many things in your body will deteriorate at a hastened pace. Smoking kills off the ascorbic acid molecule – so if you cannot quit smoking, then maybe look at taking a supplement of vitamin C.
An excellent example of vitamin C shortage and its effect on collagen is the old English sailors that suffered scurvy, a shortage of vitamin C, which resulted first in loose teeth and ultimately death – since collagen could not be formed to keep the body together.
Although it may sound flippant to talk about physical appearance in the face of death, it would have been interesting to note the skin condition of these sailors – as a shortage of vitamin C would have shown very quickly in the tone and health of their skin.
Although a Finnish study could not detect morphological changes in the skin of smokers, they did find that type I and III collagen synthesis is decreased and the regulation of ECM turnover is altered in smokers, which may lead to deterioration of the tensile strength and resiliency of skin in the long term.
During normal sugar metabolism (for instance glucose and fructose) binding can occur with a reactive aldehydes and/or ketones, which in turn, can attach itself to a free amino acid groups on proteins – collagen – and in degradation process is called non-enzymatic glycosylation.
This is also referred to as glycation or the Maillard reaction, which can reduce the skin’s elasticity. Studies have also found that diabetes contributes to chemical aging, which includes skin aging, via the Maillard reaction.
Inflammatory conditions also break down collagen – for instance, arthritis in joints and infections on the skin.
An enzyme found in the body, collagenase, causes the breakdown of collagen, and any systemic or topical help that will slow down the excessive action of collagenase should be used.
The body uses collagenase to remove excessive collagen build-up over a wound area – therefore collagenase in small quantities is required by the skin, but if present in excess, will hasten the destruction of healthy collagen.
Should excessive collagenase exist, mediation and balancing would have a positive effect on the skin.
Topical application of various compounds assists the collagen in the skin, and here we can look at:
The connective tissue of the dermis is made up of collagen and elastin fibers immersed in glycosaminoglycans. All three components have their origin in the fibroblasts.
Collagen is the most important integral component of the dermis connective tissue.
Study under electronic microscope reveals that collagen comprises fibers of highly variable diameters, from 2 to 15 Tm, which are set out either as a delicate weave or in thick bundles.
The network of collagen fibers lies in the papillary dermis, while the collagen fibers linked in thick bundles are to be found in the reticular dermis and run almost parallel to the surface of the skin in an intertwined fashion.
The biosynthesis of collagen begins in the fibroblasts with the union of three polypeptide alpha pro-chains in a triple helix pro-collagen molecule.
When they reach extracellular space, the chains are shortened by 30-40% through hydrolysis of the carboxi and amino terminal ends by two fibroblastic peptidases.
This determines the conversion of the pro-collagen into collagen. If the additional peptides keep the pro-collagen soluble and prevent its intracellular polymerization, the collagen is easily polymerized.
Collagen molecules are rigid cylinders in which each of the three-spiraled alpha chains carries almost 1000 amino acids. These molecules are 300 nm long and 1.5 nm wide.
Collagen micro-fibers are formed by lateral and longitudinal association of the molecules, nevertheless, diameters vary widely because of the differing degrees of polymerization; this is why young micro-fibers are thinner than older ones. Collagen fibers present characteristic transverse striae because the fibers line up in a parallel manner coinciding with the five charged areas in each molecule.
Seven types of collagen are described which differ in their composition and anti-genicity.
Type I, which predominates from birth, is found in the large bundles of fibers in the reticular dermis. Type III corresponds to the reticular fibers. Even in cases where this type is prevalent at the beginning of the life of the fetus, after birth it is restricted to basal zones and perivascular areas.
The collagen of the basal membrane is type I and of the cartilage, type II. Type V is observed in fetal membranes and vascular tissue. Type VII is found in different basal membranes and is an important structural component of the anchoring mini-fibers.
Compositions vary in the following ways: the type I collagen molecules have two alpha-1 (I) chains and one alpha-2; the three chains of type II collagen are alpha-1 (II); type III collagen also has three identical alpha chains; type IV is pro-collagen with three identical pro-alpha chains which retain their helicoidal extensions; the characterization of type V and VI is not yet suitable; in type VII three alpha chains with non collagen terminal regions can be made out.
Collagen has an amino acid composition, which differentiates it from other natural proteins. It contains around 25% glycine, 10% alanine, 12% proline and 10% hydroxyproline, which is the amino acids that characterizes collagen.
From all of the above, it is clear that healthy collagen is imperative for having a youthful looking skin and it is beneficial to try and increasing the volume and quality of collagen in your skin, should you wish to have a youthful, vital and healthy looking skin.
For this reason we use certain patented molecules to increase the amount of collagen in your skin. The effectiveness of these molecules have been clinically tested and proven to increase the collagen in the skin:
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