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(kŏl`əjən), any of a group of proteins found in skin, ligaments, tendons, bone and cartilage, and other connective tissueconnective tissue,
supportive tissue widely distributed in the body, characterized by large amounts of intercellular substance and relatively few cells. The intercellular material, or matrix, is produced by the cells and gives the tissue its particular character.
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. Cells called fibroblasts form the various fibers in connective tissue in the body. The fibroblasts produce three types of fibers to form the ground substance: collagen, elatin, and the reticulum. Collagen consists of groups of white inelastic fibers with great tensile strength. These fibers include fine fibrils, which are composed of even finer filaments, visible only through the electron microscope. Collagen protein contains an unusually high percentage of the amino acids prolineproline
, organic compound, one of the 20 amino acids commonly found in animal proteins. Only the l-stereoisomer appears in mammalian protein.
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 and hydroxyproline. X-ray diffraction studies provide evidence that the protein forms a wavy band, a coiled chain with periodic, i.e., repeating, arrangement of its amino acids. Cartilage is composed of fibrous collagen in an amorphous gel. The organic (nonmineral) content of bone is made up largely of collagen fibers with calcium salt crystals lying adjacent to each segment of the fiber; the fibers and salt crystals combined form a structure with compressional and tensile strength comparable to that of reinforced concrete. A group of diseases, often termed collagen, or connective tissue, diseases, involve a variety of alterations in the connective tissue fibers; rheumatoid arthritis, rheumatic fever, lupus, and scleroderma are included in this group. Some of these diseases may involve an autoimmune response, in which the immune mechanism injures or destroys the individual's own tissues (see immunityimmunity,
ability of an organism to resist disease by identifying and destroying foreign substances or organisms. Although all animals have some immune capabilities, little is known about nonmammalian immunity.
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). Collagen dissolved in boiling water becomes denatured to form gelatingelatin
or animal jelly,
foodstuff obtained from connective tissue (found in hoofs, bones, tendons, ligaments, and cartilage) of vertebrate animals by the action of boiling water or dilute acid.
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The major fibrous protein in animals, present in all types of multicellular animals and probably the most abundant animal protein in nature. It is estimated that collagen accounts for about 30% of the total human body protein. Collagen is located in the extracellular matrix of connective tissues. It is part of the interacting network of proteoglycans and proteins that provides a structural framework for both soft and calcified connective tissues. By self-associating into fibrils and by binding to proteoglycans and other matrix components, collagen contributes to tissue integrity and mechanical properties. Collagen interacts with cells through the integrin cell receptors and mediates cellular adhesion and migration. Important roles for collagen have been identified in development, wound healing, platelet aggregation, and aging. Its commercial importance in leather and the production of gelatin and glue have long been recognized. More recently, it is being used as a basis for biomaterials. Examples of its biomedical applications include injectable collagen to lessen facial wrinkles and defects; surgical collagen sponges to increase blood clotting; and artificial skin for the treatment of burns.

The classification of an extracellular matrix protein as a collagen is based on the presence of a domain with a distinctive triple-helical conformation. The collagen triple helix consists of three polypeptide chains supercoiled about a common axis and linked by hydrogen bonds. At least 19 distinct molecules have been classified as collagens, and specific types are associated with particular tissues. The most prevalent and well-studied collagens belong to the fibril-forming or interstitial collagen family. The molecules in a fibril are covalently cross-linked by an enzymatic mechanism to strengthen and stabilize them. Inhibition of the enzyme involved in cross-linking results in a dramatic decrease in the tensile strength of tissues, a condition known as lathyrism.

Type I is the most common fibril-forming collagen. Its fibrils make up the mineralized matrix in bone, the strong parallel bundles of fibers in tendon, and the plywoodlike alternating layers in the transparent cornea. Type II is the major fibril-forming collagen in cartilage, while type III is found in blood vessels and skin, together with type I. Basement membranes, which serve to separate cell layers and act as filtration barriers, contain a distinctive group of collagens, denoted as type IV collagens, which are organized into a network or meshlike sheet structure. In the kidney glomerulus, the network based on type IV collagen acts as a filter to determine which molecules will pass from the blood into the urine. See Bone, Connective tissue

An orderly breakdown of collagen is necessary during development and tissue remodeling. For instance, following childbirth, the uterus reduces in size, which involves a massive degradation of collagen. An abnormal increase in the degradation of cartilage collagen is seen in osteoarthritis. Collagen breakdown also appears to be essential for tumor metastases. A number of hereditary diseases have been shown to be due to mutations in specific collagen genes. Osteogenesis imperfecta (brittle bone) disease is characterized by fragile bones and is due to mutations in type I collagen. Some cartilage disorders are caused by mutations in type II collagen. Ruptured arteries are found in Ehlers-Danlos syndrome type IV, which arises from mutations in type III collagen.



a fibrillar protein of the scleroprotein group; the principal component of the collagenous fibers of the connective tissues in animals.

Collagen molecules (length, approximately 3,000 Å; width, 15 Å) consist of three interwined helical polypeptide chains. The primary structure of the collagen molecule is characterized by frequent repetition of a glycyl-prolyl-oxyprolyl sequence (about one-third of all amino acid residues), which influences the configuration of the chains. The collagen in mature fibers is insoluble in water and organic solvents and soluble in 10-percent alkaline solution. A part of the collagen of immature fibers (procollagen, or tropocollagen) is soluble in weak acid. Collagen fibers undergo marked contraction when heated in water; with prolonged heating, they are denatured and turn to gelatin.

Collagen constitutes about a third of all protein in the body. It is an important structural component of connective tissue, tendons, ligaments, cartilage, skin, bones, and fish scales; its function is chiefly supportive. There is no collagen in plants. Tannins increase the resistance of collagen fibers to chemical, physical, and bacterial influences—the basis for tanning hides and furs.


Finean, J. Biologicheskie ul’trastruktury. Moscow, 1970. (Translated from English.)
Treatise on Collagen, vols. 1–2. Edited by G. N. Ramachandran and B. Gould. New York, 1967–68.



A fibrous protein found in all multicellular animals, especially in connective tissue.


a fibrous scleroprotein of connective tissue and bones that is rich in glycine and proline and yields gelatine on boiling
References in periodicals archive ?
The increased secretion of IL-1[alpha] from KM stimulated MMP-3 secretion from FM and promoted degradation of type I collagen and type III collagen from FM.
Among various types of collagen, type I and type III collagen are primarily implicated in the dermal wound healing process, especially during the late stages.
The remodeling phase is the last phase in the healing process which is characterized by an increase in the biomechanical resistance tissue due to the replacement of granulation tissue rich in type III collagen by the stronger tissue rich in type I collagen [45, 72].
Type I and type III collagen interactions during fibrillogenesis.
The repaired tendon is composed of a fibrovascular scar with a large proportion of type III collagen. A number of causes have been identified as to why the repaired tendon is disorganized, including disorganized expression of cytokines in the healing response, presence of inflammatory cells at the tendon-bone interface, slow and limited bony ingrowth between the tendon and prepared tuberosity, and insufficient number of undifferentiated stem cells at the healing tendon-bone interface.
In some tissues Type I and Type III collagen molecules are present within the same collagen fibril, covalently bound between the N-terminal regions (as discussed in [35]).
During initial inflammatory phase erythrocytes and inflammatory cells enter the site of injury and later tenocytes gradually migrate to the wound and Type III collagen synthesis is initiated.
Initially type III collagen appears but by the end of first week collagen type I dominate and it becomes the major collagen of mature scar tissue.5
Increased content of type III collagen at the rupture site of human Achilles tendon.
They are poorly organised initially and consist mainly of type III collagen, fibronectin and the glycosaminoglycans (GAGs), such as heparan sulphate and hyaluronic acid.
Assembly of human prolyl 4-hydroxylase and type III collagen in the yeast pichia pastoris: formation of a stable enzyme tetramer requires coexpression with collagen and assembly of a stable collagen requires coexpression with prolyl 4-hydroxylase.
The recombinant human type III collagen used to make the cornea uses a proprietary technology developed by a company called Fibro- Gen Inc.