Fibrinfasern

Fibrinfasern, also known as fibrillar collagen fibers, are a type of collagen fiber found in the bodies of vertebrates. They are composed of a triple-helix structure made up of collagen type I molecules, which are cross-linked together to form a single fiber.

Fibrinfasern are the primary component of skin, bones, tendons, and ligaments, making up approximately 25-35% of the total collagen in the body. They are also found in other connective tissues, such as cartilage, fascia, and blood vessels. The unique structure of fibrinfasern gives them high tensile strength and elasticity, allowing them to withstand mechanical stress and pressure.

The fibrinfasern network is composed of microfibrils, which are electrostatically charged and repel each other to form a lattice structure. The hydroxyproline content is higher in fibrinfasern compared to other collagen fibers, which increases the strength and stability of the fiber. Through the secretion of enzymes and growth factors, fibrinfasern can be influenced in terms of development, organization, and degradation.

Disease or damage to fibrinfasern can affect the body's structural integrity and result in various conditions, such as fibrosis, joint disease, and dental decay. Conversely, the role of fibrinfasern in the body is also significant to the development and repair of tissues. Their ability to reform or regenerate plays a key role in connective tissue survival.

More research is needed into fibrinfasern's therapy and clinical applications, the interaction with ligands, and their reliability as a disease marker.