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Collagen (/ˈkɒlədʒən/) is the main structural protein in the extracellular matrix found in the body's various connective tissues. As the main component of connective tissue, it is the most abundant protein in mammals,[1] making up from 25% to 35% of the whole-body protein content. Collagen consists of amino acids bound together to form a triple helix of elongated fibril[2] known as a collagen helix. It is mostly found in connective tissue such as cartilage, bones, tendons, ligaments, and skin. Vitamin C is vital for collagen synthesis, and Vitamin E improves the production of collagen.
Depending upon the degree of mineralization, collagen tissues may be rigid (bone) or compliant (tendon) or have a gradient from rigid to compliant (cartilage). Collagen is also abundant in corneas, blood vessels, the gut, intervertebral discs, and the dentin in teeth.[3] In muscle tissue, it serves as a major component of the endomysium. Collagen constitutes one to two percent of muscle tissue and accounts for 6% of the weight of the skeletal muscle tissue.[4] The fibroblast is the most common cell that creates collagen. Gelatin, which is used in food and industry, is collagen that has been irreversibly hydrolyzed using heat, basic solutions or weak acids.[5]
- ^ Di Lullo GA, Sweeney SM, Korkko J, Ala-Kokko L, San Antonio JD (February 2002). "Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen". The Journal of Biological Chemistry. 277 (6): 4223–4231. doi:10.1074/jbc.M110709200. PMID 11704682.
- ^ "Leather grown using biotechnology is about to hit the catwalk". The Economist. 26 August 2017. Archived from the original on 1 September 2017. Retrieved 2 September 2017.
- ^ Britannica Concise Encyclopedia 2007
- ^ Sikorski ZE (2001). Chemical and Functional Properties of Food Proteins. Boca Raton, Florida: CRC Press. p. 242. ISBN 978-1-56676-960-0.
- ^ Bogue RH (1923). "Conditions Affecting the Hydrolysis of Collagen to Gelatin". Industrial and Engineering Chemistry. 15 (11): 1154–59. doi:10.1021/ie50167a018.