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Keratin is one of a family of structural fibrous proteins also known as scleroproteins. Alpha-keratin (α-keratin) is a type of keratin found in vertebrates. It is the key structural material making up scales, hair, nails, feathers, horns, claws, hooves, and the outer layer of skin among vertebrates. Keratin also protects epithelial cells from damage or stress. Keratin is extremely insoluble in water and organic solvents. Keratin monomers assemble into bundles to form intermediate filaments, which are tough and form strong unmineralized epidermal appendages found in reptiles, birds, amphibians, and mammals. Excessive keratinization participate in fortification of certain tissues such as in horns of cattle and rhinos, and armadillos' osteoderm. The only other biological matter known to approximate the toughness of keratinized tissue is chitin. Keratin comes in two types, the primitive, softer forms found in all vertebrates and harder, derived forms found only among sauropsids.
Keratin 6A is one of the 27 different type II keratins expressed in humans. Keratin 6A was the first type II keratin sequence determined. Analysis of the sequence of this keratin together with that of the first type I keratin led to the discovery of the four helical domains in the central rod of keratins. In humans Keratin 6A is encoded by the KRT6A gene.
Keratin 2A also known as keratin 2E or keratin 2 is a protein that in humans is encoded by the KRT2A gene.
Keratin 12 is a protein that in humans is encoded by the KRT12 gene.
Keratin, type I cytoskeletal 10 also known as cytokeratin-10 (CK-10) or keratin-10 (K10) is a protein that in humans is encoded by the KRT10 gene. Keratin 10 is a type I keratin.
Keratin 18 is a type I cytokeratin. It is, together with its filament partner keratin 8, perhaps the most commonly found products of the intermediate filament gene family. They are expressed in single layer epithelial tissues of the body. Mutations in this gene have been linked to cryptogenic cirrhosis. Two transcript variants encoding the same protein have been found for this gene.
Hair keratin is a type of keratin found in hair and the nails.
Beta-keratin (β-keratin) is a member of a structural protein family found in the epidermis of reptiles and birds. Beta-keratins were named so because they are components of epidermal stratum corneum rich in stacked beta sheets, in contrast to alpha-keratins, intermediate-filament proteins also found in stratum corneum and rich in alpha helices. Because the accurate use of the term keratin is limited to the alpha-keratins, the term "beta-keratins" in recent works is replaced by "corneous beta-proteins" or "keratin-associated beta-proteins."
Keratin, type II cytoskeletal 8 also known as cytokeratin-8 (CK-8) or keratin-8 (K8) is a keratin protein that is encoded in humans by the KRT8 gene. It is often paired with keratin 18.
Keratin 6C, is a type II cytokeratin, one of a number of isoforms of keratin 6 encoded by separate genes located within the type II keratin gene cluster on human chromosome 12q. This gene was uncovered recently by the Human Genome Project and its expression patterns in humans remains unknown.
Keratin, type II cuticular Hb1 is a protein that in humans is encoded by the KRT81 gene.
Keratin, type I cuticular Ha1 is a protein that in humans is encoded by the KRT31 gene.
Keratin, type II cuticular Hb6 is a protein that in humans is encoded by the KRT86 gene.
Keratin, type II cytoskeletal 78 is a protein that in humans is encoded by the KRT78 gene.
Keratin, type I cuticular Ha2 is a protein that in humans is encoded by the KRT32 gene.
Keratin, type I cuticular Ha3-I is a protein that in humans is encoded by the KRT33A gene.
Keratin, type I cuticular Ha4 is a protein that in humans is encoded by the KRT34 gene.
Keratin, type II cuticular Hb5 is a protein that in humans is encoded by the KRT85 gene.
Keratin 83, also known as KRT83, is a protein which humans is encoded by the KRT83 gene.
A keratin disease is a genetic disorder of one of the keratin genes. An example is monilethrix. The first to be identified was epidermolysis bullosa simplex.
References
- ↑ Joseph CB, Mariniello M, Yoshifuji A, Schiano G, Lake J, Marten J, et al. (March 2022). "Meta-GWAS Reveals Novel Genetic Variants Associated with Urinary Excretion of Uromodulin". Journal of the American Society of Nephrology. 33 (3): 511–529. doi:10.1681/ASN.2021040491. PMC 8975067 . PMID 35228297.
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