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Oral Cytokeratins in Health and Disease 1Roopa S Rao, 2Shankargouda Patil, 3BS Ganavi

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Oral Cytokeratins in Health and Disease 1Roopa S Rao, 2Shankargouda Patil, 3BS Ganavi JCDP Oral10.5005/jp-journals-10024-1502 Cytokeratins in Health and Disease REVIEW ARTICLE Oral Cytokeratins in Health and Disease 1Roopa S Rao, 2Shankargouda Patil, 3BS Ganavi ABSTRACT The word keratin comes from the Greek word ‘kera’ 4 The dynamics of oral mucosa is known by its inherent defensive meaning horn. Keratins are defined as intermediate fila­ nature. Certain areas demand tough shield when subjected to ment forming proteins, (10 nm in diameter) with specific mechanical insults. This is met by structural scaffolding material physicochemical properties, produced in any vertebrate referred as cytoskeleton comprised of intracellular protein epithelia.5 They form the cytoskeletal structural proteins of filaments called cytokeratins in the surface squames of oral 6 epithelia. They also equally contribute towards the architecture stratified keratinizing epithelia. of odontogenic apparatus and salivary gland. Differentiation of epithelial cells within stratified epithelia regulates the expression HISTORY of specific keratin gene. Any mutation in, or autoantibodies to keratins, desmosomal and cornified envelope proteins is A century ago in 1850, the word ‘keratin’ first appeared translated into genetic and acquired human disorders. Sound in literature to denote a material that constituted the hard knowledge of structural proteins, their expression, distribution tissues like animal horns and hooves.4 William T Astbury and function plays a vital role in acquainting with these disorders and their application as differentiation markers. Thus, they form and Francis Crick contributed to the structure of keratin, an integral aid in diagnostic pathology and may be instrumental following which Sun and Green popularized the monoclonal in the future interventions by gene therapy. This review focuses keratin antibodies. The identification of types I and II on basics to current updates on oral cytokeratins with an emphasis on the genetic and acquired disorders of cytokeratins subunits in keratin and requirement of both these types to with oral implications. constitute a stable keratin assembly was noted by Fuchs and co-workers. All these developments were followed by Keywords: Cytokeratins, Cytokeratin markers, Keratin genes, Keratin disorders. extensive research in biology and pathology using mono- How to cite this article: Rao RS, Patil S, Ganavi BS. Oral clonal antibodies with the discovery of Epidermolysis 7 Cytokeratins in Health and Disease. J Contemp Dent Pract bullosa simplex (EBS) as the first disease of IF. 2014;15(1):127-136. Source of support: Nil KERATINIZATION IN ORAL EPITHELIA Conflict of interest: None declared Oral epithelia demonstrate one of the 2 patterns of epithelial maturation (Fig. 1).2 INTRODUCTION 1. Keratinization—mucosa matures by formation of surface Oral epithelium has regional diversity corresponding to layer of keratin. functional needs as it is subjected to different forms and intensity a. Orthokeratinization—refers to the absence of nuclei of stress which demand tougher epithelial cells. Thus, this in the surface layer of squames on maturation. need is met by the formation of intracytoplasmic filamentous b. Parakeratinization—refers to the retention of arrays called keratins. ‘The keratins’ are most diverse and an pyknotic nuclei in the surface layer of squames on outstanding group of proteins belonging to the intermediate maturation.2 filament (IF) family which constitute about 80% of the total 2. Nonkeratinization—refers to maturation with absence of 1-3 protein content in differentiated cells of stratified epithelia. keratin layer. Hence the surface cells retain their nuclei with sparse keratin filaments in the cytoplasm.8 Meeting the functional demands, gingiva demonstrates 1Professor and Head, 2Associate Professor, 3Postgraduate both types of epithelia­keratinized (e.g. Attached and free Student gingiva) and nonkeratinized (e.g. Sulcular and junctional 1-3 Department of Oral Pathology and Microbiology, Faculty of epithelia).2 Dental Sciences, MS Ramaiah University of Applied Sciences MSRIT Post, MSR Nagar, Bangalore, Karnataka, India The following terms denote pathologic states: • Keratosis: When keratinization occurs in a normally Corresponding Author: Shankargouda Patil, Associate Professor, Department of Oral Pathology and Microbiology nonkeratinized tissue, it is referred to as keratosis. Faculty of Dental Sciences, MS Ramaiah University of Applied • Parakeratosis: When normally keratinizing tissue, such Sciences, MSRIT Post, MSR Nagar, Bengaluru-560054 as epidermis, becomes parakeratinized, it is referred to as Karnataka, India, e-mail: [email protected] parakeratosis.9 The Journal of Contemporary Dental Practice, January-February 2014;15(1):127-136 127 Roopa S Rao et al KERATIN STRUCTURE Keratins are obligate heterodimer proteins, expressed in pairs of types I and II proteins.13 The molecular weight of human keratins ranges from 44 to 66 kDa.1 Filament assembly begins by parallel association of a type I chain with its type II counterpart to form a paired dimer. Two such paired dimers associate in an antiparallel fashion to form a staggered tetramer. Two tetramers pack together laterally to form the protofilament. Eight such protofilaments are twisted into a rope which forms the keratin Fig. 1: Keratinization in oral mucosa filament. Each individual keratin filament therefore has a cross section of 32 individual α helical coils. Strong lateral hydrophobic interactions stabilize the polypeptide chains. Keratin filaments are subsequently bundled and assembled into macromolecular networks that radiate throughout the cytoplasm (Fig. 2).14,15 BASIC MOLECULAR STRUCTURE OF KERATIN POLYPEPTIDE CHAINS All keratin molecules contain a central rod domain of 310 aminoacids with α­helical conformation. This central core is made up of four subdomains (1A, 1B, 2A, 2B) separated by three nonhelical linker sequences (L1, L2 and L3) (Fig. 3A). Diversity among keratin filaments resides in nonhelical extensions at the amino and carboxy terminals (H, V and E end domains)15­18Further, there are two highly conserved helix boundary sequence motives on each rod, called helix initiation peptide (HIP) in the 1A domain and Fig. 2: Assembly of keratin filament the helix termination peptide (HTP) at the end of helix 2B. Any mutations in these regions, lead to more severe disease 19 FACTORS INFLUENCING phenotypes than the other regions (Fig. 3B). EPITHELIAL DIFFERENTIATION Glycine is the most abundant residue in cytokeratins. The heads and/or tails of epidermal keratins are glycine and Debbie Tudor et al in 2004 reviewed all the experimental phenylalanine rich but alanine poor and those of simple-type evidence on the ‘Intrinsic Patterns of Behavior of Epithelial epithelial keratins are enriched in acidic and/or basic residues.20 Stem Cells’ and concluded that the intrinsic property of epithelial stem cells and mesenchymal modulation of stem cells determine the epithelial phenotype. In addition, mesenchymal modulation of the basic stem and amplification pattern is essential to produce and maintain most epithelial structures.10 Retinoids and calcium also influence the normal termi­ nal differentiation of epithelium. Vitamin A and its analogs, retinoids affect the gene expression by a group of nuclear 11 receptor proteins. Deficiency of vitamin A leads to squa- A mous metaplasia and epithelial keratinization whereas, 12 excess vitamin A inhibits keratinization. Also, high calcium B concentrations are necessary for stratification and desmo- Figs 3A and B: (A) Molecular structure of type I and II keratin, some assembly.11 (B) Regions of ‘hot spot’ mutations in keratin ( ) 128 JCDP Oral Cytokeratins in Health and Disease Table 1: KFAPs expressed in oral epithelia Class of KFAP Example Description Significance Class I Filaggrin • Low molecular weight, cationic protein that binds Marker to distinguish the keratin in tight arrays. nonkeratinized epithelia • Synthesized in the granular layer and stored in from keratinized keratohyalin granules. epithelia. • Converted to filaggrin upon transition of granular cells tocornified cells. • Functions: Aggregates and aids keratin filaments in dense packing within the cornified layer. Class II Trichohyalin • High molecular weight and binds keratin in loose network arrays. • Expressed in keratinizing papillae of the tongue, nail matrix, new born fore skin epidermis. • Functions: Intercellular cementing, cross bridging the proteins, regulation of calcium dependent enzymes Class III Loricrin • Expressed in the superficial layers of keratinized Markers to determine and nonkeratinized oral epithelia the extent of cell • Function: Binds to the ends of keratin and differentiation. contributes towards cornification Desmosomal • They include integral proteins (desmoglein and Antibodies to proteins desmocollin), cytoplasmic adapter proteins desmosomal proteins (desmoplakin and plakoglobin) and plaque are demonstrable in associated proteins (plakophilin, envoplakin and autoimmune diseases periplakin). like pemphigus. • Function: Bind epithelial cells and help in attachment of keratin intermediate filament to cell surface. KERATIN FILAMENT ASSOCIATED (20 epithelial keratins and 6 hair keratins). The keratin PROTEINS (KFAPS) genes are located at two different chromosomal sites: chromosome 17q21.2 (type I keratins, except K18) and KFAPs are nonfilamentous, structural proteins that interact chromosome 12q13.13 (type II keratins including K18) with keratin filaments. They are produced in the kerati­
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