Type I keratin involved in the formation and maintenance of various skin appendages, specifically in determining shape and orientation of hair (By similarity). Regulates protein synthesis and epithelial cell growth through binding to the adapter protein SFN and by stimulating Akt/mTOR pathway (By similarity).
Keratin (cytokeratin) is an intermediate filament protein, which is mainly expressed in epithelial cells such as gastric epithelium and intestinal epithelium. Keratin heterodimers composed of acidic keratin (or type I keratin, keratin 9 to 23) and basic keratin (or type II keratin, keratin 1 to 8) assemble to form filaments. Keratin isoforms exhibit tissue- and differentiation-specific characteristics, making them useful as research biomarkers. Studies have shown that mutations in the keratin gene are related to skin diseases, liver and pancreatic diseases, and inflammatory bowel disease. Therefore, cytokeratin can be used as a tumor immunohistochemical marker.Keratin 20 (CK-20) is an essential intermediate filament component and the main cytoskeleton keratin of the intestinal epithelium. Studies have shown that keratin 20 is an important marker for colon cancer, liver cancer, and stomach cancer.
The protein encoded by this gene is a member of the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins consist of acidic proteins which are arranged in pairs of heterotypic keratin chains. This cytokeratin is a major cellular protein of mature enterocytes and goblet cells and is specifically expressed in the gastric and intestinal mucosa. The type I cytokeratin genes are clustered in a region of chromosome 17q12-q21.
There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
Keratin is a type I and type II intermediate filament protein that forms a cytoskeletal network in all epithelial cells. They are expressed in pairs in a tissue- and differentiation-specific manner. In recent years, a rare autosomal dominant genetic disease-white sponge nevus (WSN) in the oral mucosa is related to mutations in the keratin 4 (KRT4) and keratin 13 (KRT13) genes.
Keratins (cytokeratins) are intermediate filament proteins that are mainly expressed in epithelial cells. Keratin heterodimers composed of an acidic keratin (or type I keratin, keratins 9 to 23) and a basic keratin (or type II keratin, keratins 1 to 8) assemble to form filaments. Keratin isoforms demonstrate tissue- and differentiation-specific profiles that make them useful as research biomarkers.
The term 'keratin' covers all intermediate filament-forming proteins with specific physicochemical properties and produced in any vertebrate epithelia. Similarly, the nomenclature of epithelia as cornified, keratinized or non-keratinized is based historically on the notion that only the epidermis of skin modifications such as horns, claws and hooves is cornified.
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