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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). Gradual calcium deposition within collagen occurs as a natural function of aging. Individual cardiac valvular leaflets are folded into shape by specialized collagen under variable pressure. The mass, distribution, age and density of collagen all contribute to the compliance required to move blood back and forth. Collagen is layered in variable densities with smooth muscle mass. With support from collagen, atrial fibrillation never deteriorates to ventricular fibrillation. 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. 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 cardiac skeleton also includes the separating septa of the heart chambers – the interventricular septum and the atrioventricular septum. The collagenous cardiac skeleton which includes the four heart valve rings, is histologically, elastically and uniquely bound to cardiac muscle.

Type V: cell surfaces, hair, and placenta.

Type IV: forms basal lamina, the epithelium-secreted layer of the basement membrane.

Type III: reticulate (main component of reticular fibers), commonly found alongside type I.

Type II: cartilage (main collagenous component of cartilage).

Type I: skin, tendon, vasculature, organs, bone (main component of the organic part of bone).

MACIT (Membrane Associated Collagens with Interrupted Triple Helices) (Type XIII, XVII).

Multiplexin (Multiple Triple Helix domains with Interruptions) (Type XV, XVIII).

FACIT (Fibril Associated Collagens with Interrupted Triple Helices) (Type IX, XII, XIV, XIX, XXI).

The number of types shows collagen's diverse functionality. All of the types contain at least one triple helix. However, as of 2011, 28 types of human collagen have been identified, described, and divided into several groups according to the structure they form. Over 90% of the collagen in the human body is type I collagen. The name collagen comes from the Greek κόλλα ( kólla), meaning " glue", and suffix -γέν, -gen, denoting "producing". Gelatin, which is used in food and industry, is collagen that has been irreversibly hydrolyzed. The fibroblast is the most common cell that creates collagen. Collagen constitutes one to two percent of muscle tissue and accounts for 6% of the weight of the skeletal muscle tissue. In muscle tissue, it serves as a major component of the endomysium. Collagen is also abundant in corneas, blood vessels, the gut, intervertebral discs, and the dentin in teeth. It is mostly found in connective tissue such as cartilage, bones, tendons, ligaments, and skin.ĭepending upon the degree of mineralization, collagen tissues may be rigid (bone) or compliant (tendon) or have a gradient from rigid to compliant (cartilage).

Collagen consists of amino acids bound together to form a triple helix of elongated fibril known as a collagen helix. As the main component of connective tissue, it is the most abundant protein in mammals, making up from 25% to 35% of the whole-body protein content. Tropocollagen molecule: three left-handed procollagens (red, green, blue) join to form a right-handed triple helical tropocollagen.Ĭollagen ( / ˈ k ɒ l ə dʒ ə n/) is the main structural protein in the extracellular matrix found in the body's various connective tissues.