Cytokeratins
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Cytokeratins
Cytokeratins are keratin proteins found in the intracytoplasmic cytoskeleton of epithelial tissue. They are an important component of intermediate filaments, which help cells resist mechanical stress. Expression of these cytokeratins within epithelial cells is largely specific to particular organs or tissues. Thus they are used clinically to identify the cell of origin of various human tumors. Naming The term ''cytokeratin'' began to be used in the late 1970s, when the protein subunits of keratin intermediate filaments inside cells were first being identified and characterized. In 2006 a new systematic nomenclature for mammalian keratins was created, and the proteins previously called ''cytokeratins'' are simply called ''keratins'' (human epithelial category). For example, cytokeratin-4 (CK-4) has been renamed keratin-4 (K4). However, they are still commonly referred to as cytokeratins in clinical practice. Types There are two categories of cytokeratins: the acidic type I cyt ...
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Type II Cytokeratin
Type II keratins (or Type II cytokeratins) constitutes the Type II intermediate filaments (IFs) of the intracytoplasmatic cytoskeleton, which is present in all mammalian epithelial cells. The type 2 cytokeratins consist of basic or neutral, high molecular weight proteins which in vivo are arranged in pairs of heterotypic Type I and Type II keratin chains, coexpressed during differentiation of simple and stratified epithelial tissues. Type II cytokeratins are encoded on chromosome 12q and encompasses: CK1, CK2, CK3, CK4, CK5, CK6, CK7 and CK8. Their molecular weight ranges from 52 kDa (CK8) to 67 kDa (CK18). See also *Type I keratin Type I keratins (or Type I cytokeratins) are cytokeratins that constitute the Type I intermediate filaments (IFs) of the intracytoplasmatic cytoskeleton, which is present in all mammalian epithelial cells. Most of the type I keratins consist of aci ... External links * Proteopedia page on keratins {{Fibrous proteins Keratins ...
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Keratin 8
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. Utility as an immunohistochemical stain Antibodies to CK8 (e.g. CAM 5.2) can be used to differentiate lobular carcinoma of the breast from ductal carcinoma of the breast. CAM 5.2, an antibody that reacts with an epitope found on both CK8 and CK18, is used in immunohistochemistry to demonstrate certain forms of cancer. In normal tissue, it reacts mainly with secretory epithelia, but not with squamous epithelium, such as that found in the skin, cervix, and esophagus. However, it also reacts with a range of malignant cells, including those derived from secretory epithelia, but also some squamous carcinomata, such as spindle cell carcinoma. It is considered useful in identifying microscopic metastases of breast carcinoma in lymph nodes, and in distinguishing Paget's disease from malignant melanom ...
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Keratin 7
Keratin, type II cytoskeletal 7 also known as cytokeratin-7 (CK-7) or keratin-7 (K7) or sarcolectin (SCL) is a protein that in humans is encoded by the ''KRT7'' gene. Keratin 7 is a type II keratin. It is specifically expressed in the simple epithelia lining the cavities of the internal organs and in the gland ducts and blood vessels. Function Keratin-7 is a member of the keratin gene family. The type II cytokeratins consist of basic or neutral proteins which are arranged in pairs of heterotypic keratin chains coexpressed during differentiation of simple and stratified epithelial tissues. This type II cytokeratin is specifically expressed in the simple epithelia lining the cavities of the internal organs and in the gland ducts and blood vessels. The genes encoding the type II cytokeratins are clustered in a region of chromosome 12q12-q13. Alternative splicing may result in several transcript variants; however, not all variants have been fully described. Keratin-7 is found in ...
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Keratin 17
Keratin, type I cytoskeletal 17 is a protein that in humans is encoded by the ''KRT17'' gene. Keratin 17 is a type I cytokeratin. It is found in nail beds, hair follicles, sebaceous glands, and other epidermal appendages. Mutations in the gene encoding this protein lead to PC-K17 (previously known as Jackson-Lawler) type pachyonychia congenita and steatocystoma multiplex. Interactions Keratin 17 has been shown to interact with CCDC85B Coiled-coil domain-containing protein 85B is a protein that in humans is encoded by the ''CCDC85B'' gene. Function Hepatitis delta virus (HDV) is a pathogenic human virus whose RNA genome and replication cycle resemble those of plant viroids. .... References Further reading * * * * * * * * * * * * * * * * * External links GeneReviews/NCBI/NIH/UW entry on Pachyonychia Congenita Keratins {{gene-17-stub ...
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Keratin 15
Keratin 15 is a protein that in humans is encoded by the ''KRT15'' gene. It has also been referred to as cytokeratin 15, K1CO and KRTB. Keratin 15 is a type I cytokeratin Type I keratins (or Type I cytokeratins) are cytokeratins that constitute the Type I intermediate filaments (IFs) of the intracytoplasmatic cytoskeleton, which is present in all mammalian epithelial cells. Most of the type I keratins consist of aci .... It is well-expressed in the basal layer of complex epithelia. However, acral keratinocytes express little to no keratin 15. References Further reading * * * * * * * * * * * * * * * Keratins {{Gene-17-stub ...
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Keratin 4
Keratin, type I cytoskeletal 4 also known as cytokeratin-4 (CK-4) or keratin-4 (K4) is a protein that in humans is encoded by the ''KRT4'' gene. Keratin 4 is a type II cytokeratin. It is specifically found in differentiated layers of the mucosal and esophageal epithelia together with keratin 13. Mutations in the genes encoding this protein have been associated with White Sponge Nevus, characterized by oral, esophageal, and anal leukoplakia Oral leukoplakia is a ''potentially malignant disorder'' affecting the oral mucosa. It is defined as "essentially an oral mucosal white lesion that cannot be considered as any other definable lesion." Oral leukoplakia is a white patch or plaque th .... References Further reading * * * * * * * * * * * * * * * * * Keratins {{Gene-12-stub ...
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Keratin 16
Keratin 16 is a protein that in humans is encoded by the ''KRT16'' gene. Keratin 16 is a type I cytokeratin. It is paired with keratin 6 in a number of epithelial tissues, including nail bed, esophagus, tongue, and hair follicles. Mutations in the gene encoding this protein are associated with the genetic skin disorders including pachyonychia congenita, non-epidermolytic palmoplantar keratoderma and unilateral palmoplantar verrucous nevus A Unilateral palmoplantar verrucous nevus is a cutaneous condition that has features of pachyonychia congenita. See also * Unilateral nevoid telangiectasia * List of cutaneous conditions Many skin conditions affect the human integumenta .... References External links GeneReviews/NCBI/NIH/UW entry on Pachyonychia Congenita Further reading * * * * * * * * * * * * * * * * * * Keratins {{Gene-17-stub ...
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Keratin 13
Keratin 13 (or cytokeratin 13) is a protein that in humans is encoded by the ''KRT13'' gene. Keratin 13 is a type I cytokeratin, it is paired with keratin 4 and found in the suprabasal layers of non-cornified stratified epithelia. Mutations in the gene encoding this protein and keratin 4 have been associated with the autosomal dominant disorder White Sponge Nevus White sponge nevus (WSN) is an autosomal dominant condition of the oral mucosa (the mucous membrane lining of the mouth). It is caused by a mutations in certain genes coding for keratin, which causes a defect in the normal process of keratinizati .... References Further reading * * * * * * * * * * * * * * * * * * Keratins {{Gene-17-stub ...
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Keratin 6
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. Keratins Keratins are the intermediate filament proteins that form a dense meshwork of filaments throughout the cytoplasm of epithelial cells. Keratins form heteropolymers consisting of a type I and a type II keratin. Keratins are generally expressed in particular pairs of type I and type II keratin proteins in a tissue-specific and cellular differentiation-specific manner. The keratin proteins of epithelial tissues are commonly known as "keratins" or are sometimes referred to as "epithelial keratins" or "cytokeratins". The specialized keratins of hair and nail are known as "hard keratins" or " trichocyte keratins". Tric ...
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Keratin 5
Keratin 5, also known as KRT5, K5, or CK5, is a protein that is encoded in humans by the ''KRT5'' gene. It dimerizes with keratin 14 and forms the intermediate filaments (IF) that make up the cytoskeleton of basal epithelial cells. This protein is involved in several diseases including epidermolysis bullosa simplex and breast and lung cancers. Structure Keratin 5, like other members of the keratin family, is an intermediate filament protein. These polypeptides are characterized by a 310 residue central rod domain that consists of four alpha helix segments (helix 1A, 1B, 2A, and 2B) connected by three short linker regions (L1, L1-2, and L2). The ends of the central rod domain, which are called the helix initiation motif (HIM) and the helix termination motif (HTM), are highly conserved. They are especially important for helix stabilization, heterodimer formation, and filament formation.Shinkuma, Satoru, et al. "A Novel Keratin 5 Mutation in an African Family with Epidermolysis ...
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Keratin
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 amon ...
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Keratin 1
Keratin 1 is a Type II intermediate filament (IFs) of the intracytoplasmatic cytoskeleton. Is co-expressed with and binds to Keratin 10, a Type I keratin, to form a coiled coil heterotypic keratin chain. Keratin 1 and Keratin 10 are specifically expressed in the spinous and granular layers of the epidermis. In contrast, basal layer keratinocytes express little to no Keratin 1. Mutations in ''KRT1'', the gene encoding Keratin 1, have been associated with variants of the disease bullous congenital ichthyosiform erythroderma in which the palms and soles of the feet are affected. Mutations in ''KRT10'' have also been associated with bullous congenital ichthyosiform erythroderma; however, in patients with KRT10 mutations the palms and soles are spared. This difference is likely due to Keratin 9, rather than Keratin 10, being the major binding partner of Keratin 1 in acral (palm and sole) keratinocytes. Type II cytokeratins are clustered in a region of chromosome 12q12-q13. Interactions ...
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