keratinproteiner

Keratinproteiner are a family of fibrous structural proteins that form the cytoskeletal intermediate filaments in epithelial cells. They provide mechanical support to tissues such as skin, hair, nails, and horn-like structures in various animals.

In mammals, keratinproteiner are broadly categorized as hard keratins, which dominate hair, nails, and horns, and soft keratins, found in most epithelial surfaces. Most keratins belong to two types: type I keratins (acidic) and type II keratins (basic to neutral). They function as obligate heterodimers, pairing one type I with one type II. These dimers assemble into tetramers and then into long, rope-like intermediate filaments that anchor cells to each other and to the surrounding matrix.

Keratinproteiner are produced by keratinocytes in stratified squamous epithelia. During differentiation, keratin expression patterns shift as cells keratinize, producing the durable filaments that give epithelial tissues their resilience. In specialized structures such as hair and nails, extensive cross-linking by disulfide bonds further strengthens the material.

Genetic information for keratinproteiner is carried by a large family of KRT genes. Mutations in keratin genes can lead to skin diseases, including epidermolysis bullosa simplex and various keratodermas, reflecting the essential role of these proteins in tissue integrity.

Beyond biology, keratinproteiner have practical uses. Keratin derived from hair and other sources is employed in cosmetics and biomaterials, where keratin-based films, fibers, and hydrogels are explored for wound healing and tissue engineering.