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Why Women Need Collagen (skin + stretch marks) – Thomas DeLauer
Collagen protein makes up 30% of the total protein in the body, and 70% of the protein in the skin
Our body’s collagen production naturally begins to slow down as we age – that is the reason behind wrinkles, sagging skin, and weaker cartilage in your joints
Collagen is special because it contains an abundance of four amino acids that you won’t find in meaningful amounts in many other foods (glycine, proline, and hydroxyproline)
Tissues are made of more than just cells – most of the volume within a tissue is comprised of the extracellular matrix (ECM), a diverse mesh of proteins and sugars produced by certain cells, which acts as the mortar binding our cells together
The ECM is composed of two components, proteoglycans, and fibrous proteins – collagens, elastins, fibronectins, and laminins are all fibrous proteins making up the scaffolding in the ECM; the proteoglycans fill in space in between
Collagen is one of the many proteins embedded in the ECM – in fact, it is the most abundant protein in animal tissues
Collagen proteins are produced by animal connective tissue cells called fibroblasts – for a protein to be classified as a collagen, it must form the collagen-like triple helix and provide structural support in the ECM
Tropocollagen is the basic building block of collagen – it is made from three peptides (groups of amino acids) strands that are coiled together in the form of a helix; these strands are known as alpha chains (α-chains)
Collagenous region: This region is a series of three amino acids. The first amino acid, glycine, is the most important – the next two can be any amino acid but are usually proline and hydroxyproline, and the repeating amino acid sequence is responsible for the helix structure of tropocollagen
A study, published in Skin Pharmacology and Physiology, had 114 women aged 45-65 years were randomized to receive 2.5 g of collagen or placebo, once daily for 8 weeks, with 57 subjects being allocated to each treatment group
Found that women who took collagen regularly for 8 weeks saw a 20% reduction in wrinkles
Additionally, after 8 weeks of intake a statistically significantly higher content of procollagen type I (65%) and elastin (18%) in the collagen-treated volunteers compared to the placebo-treated patients was detected
For fibrillin, a 6% increase could be determined after collagen treatment compared to the placebo
Study – Journal of Agricultural and Food Chemistry
Joint pain in the subjects (80) had been present for 3 months or longer at enrollment
Subjects were divided into two groups and administered either 2 g of collagen or placebo for 70 days
The tolerability profile of the treatment group was comparable to that of the placebo. Intent-to-treat analysis showed that the treatment group, as compared to placebo, had a significant reduction of pain on day 70
The collagen group experienced a significant improvement in physical activities compared to the placebo group on days 35 and 70
Collagen is made up of building blocks called amino acids, which are properly structured with the help of vitamin C
When the body makes collagen, it joins amino acids (like glycine, proline and hydroxyproline from collagen peptides) with vitamin C, which adds a hydroxyl group (oxygen and hydrogen) to the amino acids, allowing the acids to turn into a well-formed, strong helix shape.
Essentially, vitamin C helps to strengthen the formation of collagen
Our body is genetically coded to form collagen from these precursors, so using building peptides is a more natural way of getting collagen
Silica and biotin are both required for the formation of collagen, alongside hyaluronic acid & vitamin c