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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 1% to 2% of muscle tissue and 6% by weight of skeletal muscle. [4] The fibroblast is the most common cell creating collagen in animals.
The presence of water (an aldehyde) has been shown to decrease the stiffness of collagen fibrils, as well as increase their rate of stress relaxation and strength. [4] From a biological standpoint, water content acts as a toughening mechanism for fibril structures, allowing for higher energy absorption and greater straining capabilities.
Fibrillogenesis is the development of fine fibrils normally present in collagen fibers of connective tissue.It is derived from the New Latin fibrilla (meaning fibrils, or pertaining to fibrils) and Greek genesis (to create, the process by which something is created).
FACIT collagen is found in various tissue areas to modulate the surface properties of collagen fibrils and generate tissue-specific three-dimensional patterns in the extracellular matrix. [3] For example, collagen XIV connects the fibrillar networks of the cartilage and skin, [ 3 ] and XII is found in connective tissues, particularly at the ...
Collagen, type I, alpha 1, also known as alpha-1 type I collagen, is a protein that in humans is encoded by the COL1A1 gene. COL1A1 encodes the major component of type I collagen , the fibrillar collagen found in most connective tissues , including cartilage .
Collagen IV (ColIV or Col4) is a type of collagen found primarily in the basal lamina. The collagen IV C4 domain at the C-terminus is not removed in post-translational processing, and the fibers link head-to-head, rather than in parallel. Also, collagen IV lacks the regular glycine in every third residue necessary for the tight, collagen helix ...
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Integrin α11β1 is expressed by mesenchymal cells in some parts of embryo during its development and also in muscles in adults: it preferably binds fibrillar collagen. Integrin receptors capable of collagen binding could, according to results of (Garnotel R et al. 2000), include integrin α10β2, which is situated on monocytes and binds type I ...
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