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The term collagen comes from the Greek word κολλα (kolla, meaning “glue”), due to the use of animal skin and collagen-rich tissues a glue source. In a broader sense, collagen is in fact the “glue” of our body, holding it together by providing elasticity and strength to most tissues where mechanical function is essential, such as skin, cartilage, tendons and bones.
The collagen family of proteins is the most abundant in the human body – representing a basic building block within
nearly every tissue and organ. Collagen structures form largely by cell-mediated self-assembly of small collagen
molecules (300 nm in length; circumscribable with an approximate 1.5 nm diameter)4. During the process of collagen self-assembly, various types of inter-molecular crosslinks stabilize the helical supramolecular structures that form. Collagen crosslinks can be conceptually classed as either enzymatic or non-enzymatic, with enzymatic crosslinking representing an ess, sential step in the development and repair of collagen connective tissues. Whether in the early stages of embryonic tendon development or the late stages of connective tissue disease, collagen crosslinks play a key role in tissue mechanics, cell signaling, matrix damage accumulation, and tissue repair.
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