Breaking Down the Collagen

Collagen is a structural component of facial anatomy that serves as a framework to the skin providing substance tensile strength, regulation of cell adhesion and directs tissue development. The structural organization of collagen originates from functional fibers assembled via a complex process utilizing proteins and amino acids. Collagen’s fibrous protein are found in the extracellular matrix (ECM) and connective tissue of the skin.

The ECM is formed by unique protein families tasked with supplying structural integrity and several physiological functions forming a dense network throughout the dermis. The collagen family of proteins can be grouped into: fibril-forming collagens, fibril-associated collagens, network-forming collagens, anchoring fibrils, transmembrane collagens and basement membrane collagens.

The human body consists largely of the collagen fibril-forming types. Collagen fibrils are made of collagen I and III in the skin and are mainly determined by the existence of several amino acid chains with combined ratios of amino acids. Collagen is mainly produced by fibroblasts in the connective tissues, but numerous epithelial cells make certain types of collagens as well. With age, the ability to replenish collagen naturally decreases by about 1.5% per year. Collagen fibers in aged skin become thicker, shorter and result in a loss of type I collagen. As the density of collagen and elastin in the dermis declines, the structure and elasticity of the skin degrades, causing it to become thinner and more rigid.

The body contains 28 types of collagens and consists of approximately 80%-90% of collagen type I, II or III. The collagen helix is formed by a network of fibers bound by the amino acids: lysine, glycine, proline, hydroxylysine, hydroxyproline and along with keratin and elastin, give the skin its strength. The skin requires a balanced ratio of amino acids to provide this structural composition of protein. Without amino acids, protein molecules and the complex matrix of amino acids will not fabricate collagen. Hydroxyproline is created by a modification of proline amino acids and oxygen after the collagen chain is constructed. Several factors influence collagen production in one’s lifetime including, pregnancy, menopause, smoking, UV radiation, nutrient deficiencies and pollution.

By age 50, many women may lose up to half of the collagen from their skin, which is often compounded by not consuming enough protein for an extended period. Protein deficiency can also lead to muscle wasting (catabolism), poor wound healing, frequent infections, swelling under the eyes and ankles, hair breakage and hair loss.

Power to the Protein

Proteins are large molecules composed of complex chains of amino acids and are classified by the number of amino acids formed into a chain. The long polypeptide chains are joined in length by specific sequences, peptide bonds and sulfur amino acid (cysteine) bonds. More than 50 amino acids are supplied by proteins with typically 100 to 10,000 amino acids linked together to form structural units and fibrous proteins found in the skin, tendons, bone and muscle. Amino acids are essential for both dermal and epidermal structures and produce the extracellular proteins and enzymes needed for the synthesis of the epidermal barrier.

The essential amino acids for the body are: arginine, histidine, leucine, iso leucine, lysine, methionine, phenylalanine, threonine, tryptophan and valine. The non-essential amino acids are formed by essential amino acids carnitine, cysteine, glutamine, taurine and tyrosine.

Complete protein sources include proteins that provide all the essential amino acids, whereas incomplete protein sources are missing one or more essential amino acids. Essential amino acids must be included in the diet and consumed as food or supplements because the body cannot manufacture them. It is also necessary for dietary protein sources to offer both sufficient quality and quantity of amino acids to provide adequate ratio amounts for the amino acid profile.

Our protein levels are conserved during periods of total nutrient deprivation by mechanisms such as the recycling of amino acids, processing of proteins within the organelles, and cellular turnover of amino acids consuming tissues. A functional distinction cannot be made to differentiate between the impact of synthesized amino acid units because of tissue breakdown, and those that are utilized from a dietary source. The amino acid “pool” is influenced by the turnover of protein in the body, intake of dietary protein, synthesis of non-essential amino acids, and the collective status of the type of amino acids. Adequate protein intake is necessary to supply such indispensable amino acids in the body. It is also very important to note that it is not only the total protein gram count that substantiates the quality of protein intake, but also the total amino acid profile that is consumed.