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Collagen
Collagen (/ˈkɒlədʒən/) is the main structural protein in the extracellular matrix of the connective tissues of many animals. It is the most abundant protein in mammals, making up 25% to 35% of protein content. Amino acids are bound together to form a triple helix of elongated fibril known as a collagen helix. It is mostly found in cartilage, bones, tendons, ligaments, and skin. Vitamin C is vital for collagen synthesis.
Depending on 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 dentin. 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. The fibroblast is the most common cell creating collagen in animals. Gelatin, which is used in food and industry, is collagen that was irreversibly hydrolyzed using heat, basic solutions, or weak acids.
The name collagen comes from the Greek κόλλα (kólla), meaning "glue", and suffix -γέν, -gen, denoting "producing".
As of 2011, 28 types of human collagen have been identified, described, and classified according to their structure. This diversity shows collagen's diverse functionality. All of the types contain at least one triple helix. Over 90% of the collagen in humans is Type I and Type III collagen.
The five most common types are:
The collagenous cardiac skeleton, which includes the four heart valve rings, is histologically, elastically and uniquely bound to cardiac muscle. The cardiac skeleton also includes the separating septa of the heart chambers – the interventricular septum and the atrioventricular septum. Collagen contribution to the measure of cardiac performance summarily represents a continuous torsional force opposed to the fluid mechanics of blood pressure emitted from the heart. The collagenous structure that divides the upper chambers of the heart from the lower chambers is an impermeable membrane that excludes both blood and electrical impulses through typical physiological means. With support from collagen, atrial fibrillation never deteriorates to ventricular fibrillation. Collagen is layered in variable densities with smooth muscle mass. The mass, distribution, age, and density of collagen all contribute to the compliance required to move blood back and forth. Individual cardiac valvular leaflets are folded into shape by specialized collagen under variable pressure. Gradual calcium deposition within collagen occurs as a natural function of aging. Calcified points within collagen matrices show contrast in a moving display of blood and muscle, enabling methods of cardiac imaging technology to arrive at ratios essentially stating blood in (cardiac input) and blood out (cardiac output). Pathology of the collagen underpinning of the heart is understood within the category of connective tissue disease.[citation needed]
As the skeleton forms the structure of the body, it is vital that it maintains its strength and its structure, even after breaks and injuries. Collagen is used in bone grafting because its triple-helix structure makes it a very strong molecule. It is ideal for use in bones, as it does not compromise the structural integrity of the skeleton. The triple helical structure prevents collagen from being broken down by enzymes, it enables adhesiveness of cells and it is important for the proper assembly of the extracellular matrix.
Collagen scaffolds are used in tissue regeneration, whether in sponges, thin sheets, gels, or fibers. Collagen has favorable properties for tissue regeneration, such as pore structure, permeability, hydrophilicity, and stability in vivo. Collagen scaffolds also support deposition of cells, such as osteoblasts and fibroblasts, and once inserted, facilitate growth to proceed normally.
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Collagen AI simulator
(@Collagen_simulator)
Collagen
Collagen (/ˈkɒlədʒən/) is the main structural protein in the extracellular matrix of the connective tissues of many animals. It is the most abundant protein in mammals, making up 25% to 35% of protein content. Amino acids are bound together to form a triple helix of elongated fibril known as a collagen helix. It is mostly found in cartilage, bones, tendons, ligaments, and skin. Vitamin C is vital for collagen synthesis.
Depending on 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 dentin. 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. The fibroblast is the most common cell creating collagen in animals. Gelatin, which is used in food and industry, is collagen that was irreversibly hydrolyzed using heat, basic solutions, or weak acids.
The name collagen comes from the Greek κόλλα (kólla), meaning "glue", and suffix -γέν, -gen, denoting "producing".
As of 2011, 28 types of human collagen have been identified, described, and classified according to their structure. This diversity shows collagen's diverse functionality. All of the types contain at least one triple helix. Over 90% of the collagen in humans is Type I and Type III collagen.
The five most common types are:
The collagenous cardiac skeleton, which includes the four heart valve rings, is histologically, elastically and uniquely bound to cardiac muscle. The cardiac skeleton also includes the separating septa of the heart chambers – the interventricular septum and the atrioventricular septum. Collagen contribution to the measure of cardiac performance summarily represents a continuous torsional force opposed to the fluid mechanics of blood pressure emitted from the heart. The collagenous structure that divides the upper chambers of the heart from the lower chambers is an impermeable membrane that excludes both blood and electrical impulses through typical physiological means. With support from collagen, atrial fibrillation never deteriorates to ventricular fibrillation. Collagen is layered in variable densities with smooth muscle mass. The mass, distribution, age, and density of collagen all contribute to the compliance required to move blood back and forth. Individual cardiac valvular leaflets are folded into shape by specialized collagen under variable pressure. Gradual calcium deposition within collagen occurs as a natural function of aging. Calcified points within collagen matrices show contrast in a moving display of blood and muscle, enabling methods of cardiac imaging technology to arrive at ratios essentially stating blood in (cardiac input) and blood out (cardiac output). Pathology of the collagen underpinning of the heart is understood within the category of connective tissue disease.[citation needed]
As the skeleton forms the structure of the body, it is vital that it maintains its strength and its structure, even after breaks and injuries. Collagen is used in bone grafting because its triple-helix structure makes it a very strong molecule. It is ideal for use in bones, as it does not compromise the structural integrity of the skeleton. The triple helical structure prevents collagen from being broken down by enzymes, it enables adhesiveness of cells and it is important for the proper assembly of the extracellular matrix.
Collagen scaffolds are used in tissue regeneration, whether in sponges, thin sheets, gels, or fibers. Collagen has favorable properties for tissue regeneration, such as pore structure, permeability, hydrophilicity, and stability in vivo. Collagen scaffolds also support deposition of cells, such as osteoblasts and fibroblasts, and once inserted, facilitate growth to proceed normally.