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Microscopy of keratin filaments inside cells. Keratin (/ ˈ k ɛr ə t ɪ n / [1] [2]) is one of a family of structural fibrous proteins also known as scleroproteins.It is the key structural material making up scales, hair, nails, feathers, horns, claws, hooves, and the outer layer of skin in vertebrates.
Keratinization is part of the physical barrier formation (cornification), in which the keratinocytes produce more and more keratin and undergo terminal differentiation. The fully cornified keratinocytes that form the outermost layer are constantly shed off and replaced by new cells.
Keratinization begins in the stratum spinosum, [5] although the actual keratinocytes begin in the stratum basale. [4] They have large pale-staining nuclei as they are active in synthesizing fibrillar proteins, known as cytokeratin, which build up within the cells aggregating together forming tonofibrils. The tonofibrils go on to form the ...
Keratohyalin is a protein structure found in cytoplasmic granules of the keratinocytes in the stratum granulosum of the epidermis.Keratohyalin granules (KHG) mainly consist of keratin, profilaggrin, [1] loricrin [2] and trichohyalin proteins which contribute to cornification or keratinization, the process of the formation of epidermal cornified cell envelope.
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The end-domain sequences of type I and II cytokeratin chains contain in both sides of the rod domain the subdomains V1 and V2, which have variable size and sequence. The type II also presents the conserved subdomains H1 and H2, encompassing 36 and 20 residues respectively.
16678 Ensembl ENSG00000167768 ENSMUSG00000046834 UniProt P04264 P04104 RefSeq (mRNA) NM_006121 NM_008473 RefSeq (protein) NP_006112 NP_032499 Location (UCSC) Chr 12: 52.67 – 52.68 Mb Chr 15: 101.75 – 101.76 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Keratin 1 is a Type II intermediate filament (IFs) of the intracytoplasmatic cytoskeleton. Is co-expressed with and binds to ...
Similar to other intermediate filament subunit proteins, a prevalent secondary structure exists: a well-preserved, central alpha-helical domain made up of four coiled-coil segments along with non-helical end-terminal domains that vary in sequences and lengths [14]. Recent findings suggest that the interaction between acidic and basic soft ...