Temporal and Spatial Distribution of Collagen Types I and III during Experimental Wound Healing An Immunohistochemical Study
Introduction:
Collagen is a structural protein of connective tissues (cartilage, tendons, ligaments) and organs (skin, heart, liver, kidney, lungs, blood vessels, bones). Collagen is a family of fibrous protein that is a component of the extracellular matrix (ECM). It is made up of three alpha chains that wrap around each other to form the collagen fibers. The overall architecture of the collagen and its type depend on the amino acid sequence of the chain. Collagen can be divided into interstitial collagen, basement membrane collagen, and peripheral collagen according to its location in the body. There are over 30 types of collagen identified. Three left hand helices (proline II), wound together and linked to each other to form a long, strong right hand helix, is the normal collagen molecule, the triple helix. In distensible connective tissues such as skin, lung, and vasculature, collagen type I (Col I) is typically found together with type III collagen (Col III). The major collagens in ECM are collagen type I and III, but collagen type IV, V, VI, and VIII are also found in ECM. Collagen type I forms a scaffold with thick fibers and low turnover. Collagen type I maturation, however, is dependent on collagen type III, which forms thin, weak fibers with rapid turnover. Also, collagen types I, II, and III are the most abundant fibrillar collagens. Collagen type I is found in skin, tendons, blood vessels, lungs, heart, and other organs, and it is the major organic component of the calcified tissue of bones and teeth. But reticular fibers are collagen type III which are usually found with collagen type I ) Khalaf et al.,2019).
Download pdf:
