Representing 75%1 of the skin’s dry weight, the quantity and quality of Collagen plays a major role in the skin’s appearance.

Collagen is an important element of human skin; in fact it is the principle structural protein holding skin together. Representing 75%1 of the skin’s dry weight, the quantity and quality of Collagen plays a major role in the skin’s appearance.

Sandwiched between the epidermis and hypodermis lies one the skin’s lifeblood area, the dermis. The dermis contains blood vessels that nourish the skin, and structural proteins like collagen that keep the skin firm, plump, and wrinkle-free. As we age our bodies struggle to replenish stores of collagen, and some people are genetically primed to break down collagen faster than others.

It is well established that collagen is an important element of human skin1; in fact it is the principle structural protein holding the skin together. Representing 75% of the skin’s dry weight2 it keeps the skin firm, plump and wrinkle-free. The quantity and quality of the Collagen plays a major role in the skin’s appearance. Like many components of the body, Collagen undergoes continuous turnover: new Collagen is continually produced and recycled throughout life. At a younger age, the synthesis of Collagen predominates, whereas after about the age of 40, the degradation of Collagen picks up speed .4 This degradation process is precipitated by a protein called Matrix Metallopeptidase-1 (MMPs) or Collagenase.

In healthy, youthful skin, the synthesis and degradation of Collagen is in balance: damaged or redundant Collagen is degraded while the deficit is replenished by the ongoing synthesis4. Unfortunately, this intricate balance gets disrupted when there is an oversupply of MMP1: too little of the matrix is synthesized and too much is degraded .1,3 The more this occurs the more winkles, roughness and sagginess one tends to have. MMP levels are known to increase with age as a result of photo aging5 as well as natural aging .3,4

The genes in this category are involved in slowing the breakdown and degradation of Collagen Fibers found in the extracellular matrix of human tissue. Key variations tested in this category can identify if the synthesis and degradation process of Collagen is in balance, or if the degradation predominates (increased MMP levels) that can result in the appearance of premature wrinkling, loss of youthful looks and other ageing skin traits.

Did you know? 1 in 3 people have a genetic variation that predisposes their skin to accelerated wrinkling.

Collagen: Collagen is the principle structural protein that holds the skin together.1 Collagen is just one of thousands of different proteins in the body. Most proteins occur only in small amounts. But by far the most abundant protein is collagen. In fact, collagen makes up more than one third of all protein in the body and about 75% of the skin.2

Protein: Protein are the building blocks of life. They are essential in helping to build the human body including muscle, bone, blood and collagen. Protein enables the body to function properly. They are used in all sorts of ways: to transport nutrients and oxygen to vital organs including the skin, and are essential tools needed for cellular repair.

The Function of MMPs: Proteins of the Matrix Metalloproteinases (MMP) family are critical players in the skin’s physiology.1,3,4 Being part of this group of zinc dependant enzymes (endopeptidases) the MMP1 gene is involved in the breakdown and degradation of the collagen fibrils found in the extracellular matrix of human tissue .1,3,5

MMP’s form an important part of the body’s natural physiological process: they break down damaged or worn out structural proteins, facilitate the second phase of wound healing, clear pathways for movement of immune cells to infected areas, and so forth.

1. Varani. J., et al., (2006). ”Decreased Collagen Production in Chronologically Aged Skin” American Journal of Pathology 168: 1861-1868.

2. Available at: http://www.biospecifics.com/collagendefined.html. Accessed October 22, 2008.

3. Varani. J., et al., (2001).”Inhibition of Type I Procollagen Synthesis by Damaged Collagen in Photoaged Skin and by Collagenase-Degraded Collagen in Vitro.” American Journal of Pathology 158: 931-942.

4. Ho Chung. J., et al., (2001). ”Modulation of Skin Collagen Metabolism in Aged and Photoaged Human Skin In Vivo.” Journal of Investigative Dermatology 117: 1218–1224.

5. Fisher. G., et al., (1997). "Pathophysiology of Premature Skin Aging Induced by Ultraviolet Light." The New England Journal of Medicine 337(20): 1419-1429