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Collagen Enzyme Collagen is a complex protein whose main role is to provide flexibility to the skin, ligaments, joints, bones, nails, eyes and hair (Artmann & Chien 163). It makes up 30% of all proteins available in humans and all mammals (Artmann & Chien 163). The body produces this due to the intake of provisions enriched with nutrients such as proteins. However, its level reduces with age resulting to shrinking of the skin, pain in joints and ligaments, lesser hair elasticity, fragile nails and lip thinning (Lynch 161).
Decrease in the level of collagen also leads to complications like Oesteogenesis Imperfecta, commonly known as brittle bone disease (Artmann & Chien 183). Apart from aging, collagen can also be lost through malfunctioning of the structure. This study will seek to relay more information about Collagen enzyme that comprises human beings’ stature especially its importance. It comprises of glycine, proline and hydroxyproline, which are amino acids whereby the latter is usually a product of proline’s reaction with oxygen (Artmann & Chien 163).
The three amino acids are what give it a triple helical configuration (Mecham 80). Although there are 28 types of its Collagen usually detonated using Roman numbers ranging from I to XXVII, the most common ones are I-V. Type I is quite evident in bones, ligaments, dermis and tendons whereby its core role encompasses resisting tension in these respective areas. Type II is present in stretchy cartilage together with hyaline responsible in resisting pressure. Type III is quite rampant in cardiovascular systems, spleen, lungs and the lymphatic system (Keeley & Mecham 40).
Type IV its location is in the basement membrane where it filters glomeruli and blood capillaries, whereas type V comprises placenta, cell surfaces and hair (Keeley & Mecham 40).Figure 1: Collagen structure made up of Hydroxyproline and proline. Accessed on 5Th March. 2014.glycine.intranet.tdmu.edu.ua/data/kafedra/internal/chemistry/classes_stud/en/nurse/BSN/ptn/2/2.Biochemistry of muscle, muscle contraction.files/image051.jpg Type I is the most profuse in humans because it is present in body organs such as the skin, ligaments and tendons (Artmann & Chien 165).
The skin’s middle section commonly referred as dermis is usually made of collagen. Some roles of collagen include strengthening of bones hence enhance them provide structural support to the body and act as lever for attachment of muscles, which aid in mobility (Artmann & Chien 165). It is essential to humans because it provides sturdy and flexible tendons and cartilages. It also improves the state of human teeth and nails. Apart from strengthening of bones, it also plays a big role in enhancing human health via controlling skin, tendons, bones and connective tissues (Artmann & Chien 170).
Alongside Keratin, it is also mandated to ensure elasticity and sturdiness of the skin by keeping it hydrated (Artmann & Chien 170). Lack of collagen is evident during old age whereby the skin becomes dry and wrinkled. This is due to the gradual diminution of types I and II (Artmann & Chien 170). It is also essential in helping healing of wounds when one is hurt. This is by repairing the wound with a scar (Artmann & Chien 170). Bones apart from acting as levers where muscles attach themselves to allow varied body movements, they also offer structural support and protect internal organs (Lynch 160).
Due to the roles performed by bones, it is appropriate for them to be healthy and strong. Collagen mesh combines with water to form a slippery pad to act as a cushion in joints, hence easing movement. In conclusion, collagen is a complex protein comprising both humans and other mammal creatures. There are 28 types in the human body arranged in roman numbers but the common ones include I-V. Type I is the largest located in the skin, ligaments, tendons and bones (Artmann & Chien 165). Some of the roles performed by collagen include strengthening of bones and hydration of the skin.
Work CitedArtmann, Gerhard M. & Chien, Shu. Bioengineering in Cell and Tissue Research. New York: Springer, 2008.PrintKeeley, Fred, W. & Mecham, Robert, P. Evolution of Extracellular Matrix. Berlin ; New York : Springer, 2013.PrintLynch, Gordon S. Sarcopenia- Age-Related Muscle Wasting and Weakness: Mechanisms and Treatments. Dordrecht. New York: Springer Science+ Business Media B.V., 2011.PrintMecham, Robert P. The Extracellular Matrix : An Overview. Berlin; New York: Springer Verlag, 2011.Print
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