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Collagen is an essential part of the framework of the design of our various body tissues. is the major insoluble fibrous protein in the extracellular matrix and in connective tissue.
- It is the single most abundant protein in the animal kingdom.
- There are at least 16 types of collagen, but 80 – 90 percent of the collagen in the body consists of types I, II, and III
- It is responsible for performing a variety of important biological functions.
- It is most well-known for the structural role it plays in the body.
- It is present in large quantities in connective tissue and provides bone, tendons and ligaments with tensile strength and skin with elasticity. It often works in conjuction with other important proteins such as keratin and elastin.
- Collagen production declines with age and exposure to factors such as smoking and UV light.
- Collagen can be used in collagen dressings, to attract new skin cells to wound sites.
- Cosmetic lotions that claim to increase collagen levels are unlikely to do so, as collagen molecules are too large to be absorbed through the skin.
- Collagen is a hard, insoluble, and fibrous protein that makes up one-third of the protein in the human body.
- In most collagens, the molecules are packed together to form long, thin fibrils.
- These act as supporting structures and anchor cells to each other. They give the skin strength and elasticity.
- The collagens in the human body are strong and flexible.
- Type 1 collagen fibrils are particularly capable of being stretched. Gram-for-gram, they are stronger than steel.
There are close to 30 different types of collagen that have been identified so far. The most abundant type of collagen present in the human body is that of Type I with significant amounts of Type II,III and IV also accounted for.
- Collagen I- found in bones, tendons, organs
- Collagen II- found mainly in cartilage
- Collagen III- found mainly in reticular fibres ( fine fibrous connective tissue occurring in networks to make up the supporting tissue of many organs).
- Collagen IV- found in the basement membrane of cell membranes (a thin noncellular layer located between epithelial cells and the connective tissue that underlies them, composed of collagen and other proteins and having a variety of functions including support and filtration)
- Collagen V- found in hair, nails
Collagen Synthesis and structure
- The production of collagen starts with procollagen—the substance secreted by your cells. It goes through processing in two parts of your cell, the endoplasmic reticulum and Golgi body.
- This whole process needs vitamin C.
- The structure of a collagen protein is what gives it the unique strength your body needs. It’s a triple helix—three chains twisting around each other.
- There are 1,050 amino acids in each of the three chains that make up collagen. And they’re held together with hydrogens—the smallest atom.
- Glycine is amino acid that takes up the middle of the triple helix structure because it’s the only one that can fit. Glycine is an amino acid that has a single hydrogen atom as its side chain. It is the simplest amino acid.
- These long fibers don’t just exist as single protein ropes. Collagen can come together to form striated horizontal sheets.
NB The older you get, the less collagen you make. And what you do make is not as high-quality as the collagen of your youth. This impacts the appearance of skin, the maintenance of joint health, and much more.
There are many types of disorders associated with collagen.These disorders typically occur as a result of improper folding of these molecules and occasionally due to a particular amino acid substitution. These include:
- Alport Syndrome (IV)
- Osteogenesis imperfecta (I) -more commonly known as Brittle Bone disease
- Chondrodysplasias (II) eg achondroplasia
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- Medical news today What is collage and why do people use it. Available from:https://www.medicalnewstoday.com/articles/262881.php (last accessed 13.2.2020)
- Your dictionary Basement Membrane Available from:https://www.yourdictionary.com/basement-membrane (last accessed 12.2.2020)
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