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At least 19 recordsLinked to original sources
PubMed2006

Epidermal differentiation complex yields a secret: mutations in the cornification protein filaggrin underlie ichthyosis vulgaris.

Ichthyosis vulgaris (IV), characterized by mild scaling on limbs and lower abdomen, has an incidence of 1 in 250. Smith, McLean, and colleagues demonstrate that common mutations in filaggrin underlie IV. Filaggrin aggregates keratin intermediate filaments and is cross-linked into the cornified envelope to form the epidermal barrier. These findings reinforce the importance of the epidermal barrier in pathogenesis of skin diseases.

Cell Differentiation↗
PubMed1983

Histidine-rich proteins (filaggrins): structural and functional heterogeneity during epidermal differentiation.

The urea-soluble protein profiles of guinea pig, rat, mouse and human epidermis have been compared by non-equilibrium pH gradient/sodium dodecyl sulphate two-dimensional gel electrophoresis. The histidine-rich proteins (filaggrins) were identified firstly by their characteristic specificity and kinetics of labelling with [3H]histidine and [32P]phosphate, and secondly by their ability in vitro to aggregate keratin filaments specifically into bundles. In all species the phosphorylated filaggrin precursor, profilaggrin, is resolved as a single or doublet band with an apparent molecular weight greater than 300,000 and a neutral or slightly acidic iso-electric point. In striking contrast, the strongly basic filaggrins produced from similar profilaggrins form molecular weight families that are clearly species specific. In rat and man there is a single, principal molecular weight form of filaggrin (Mr 45,000 and 38,000, respectively), while mouse and guinea pig have heterogeneous families, including high molecular weight variants (Mr greater than 200,000). Even filaggrins of a particular molecular weight are not homogeneous proteins, but consist of a number of iso-electric variants, some of which are considerably less basic than the bulk of the filaggrins. Incorporation studies using [3H]arginine and [32P]phosphate indicate that the iso-electric variance is not due to residual phosphate, following profilaggrin breakdown, but rather to a conversion of basic arginine residues into neutral citrulline residues. Filaggrins of all the molecular weights from all the species studied share the ability to aggregate keratin filaments into large, insoluble macrofibrils. However, the more acidic iso-electric variants have lower affinities for keratin, particularly in man and guinea pig where the most acidic filaggrins have completely lost the ability to aggregate keratins. We discuss the possibility that a loss of keratin binding ability, resulting in a loosening of the keratin fibre/filaggrin matrix is necessary before the normal complete proteolysis of the filaggrins can occur.

Amino Acids↗
PubMed1984

Alteration in the distribution of the epidermal protein filaggrin during two-stage chemical carcinogenesis in the SENCAR mouse skin.

The histidine-rich epidermal protein filaggrin was purified from urea extracts of newborn SENCAR mouse epidermis. The protein had a molecular weight of 28,000 and an amino acid composition distinctive for this class of proteins. The purified protein was a phosphate acceptor in an in vitro protein kinase assay. Rabbit antibodies raised against filaggrin were used in an indirect immunofluorescent survey of the distribution of filaggrin in the epidermis after single and multiple 12-O-tetradecanoylphorbol-13-acetate treatments as well as in papillomas and carcinomas. The immunofluorescent pattern of acetone-treated adult SENCAR mouse epidermis showed primarily granular layer fluorescence. A single topical 12-O-tetradecanoylphorbol-13-acetate treatment increased immunofluorescence in basal and suprabasal cells. Large papillomas produced by a dimethylbenz[a]anthracene initiation-12-O-tetradecanoylphorbol-13-acetate promotion protocol showed increased fluorescence in all layers. Exuberant papillomas showed a pleomorphic distribution of filaggrin with alternating positive and negative areas of immunofluorescence. Filaggrin immunofluorescence in invasive carcinomas was negative or only slightly positive. The distribution of filaggrin as detected by indirect immunofluorescence is a good indicator of maturation and differentiation in experimental tumors, and its presence correlates with the absence of aggressive or invasive growth.

Amino Acids↗
PubMed1993

Independent regulation of two cytoplasmic processing stages of the intermediate filament-associated protein filaggrin and role of Ca2+ in the second stage.

One of the final events in cornification of epidermal cells is processing of profilaggrin to the keratin-associated protein filaggrin. Processing involves several proteolytic events and occurs in two discrete proteolytic stages (Resing, K. A., Walsh, K. A., and Dale, B. A. (1984) J. Cell Biol. 99, 1372-1378; Resing, K. A., Walsh, K. A., Haugen-Scofield, J., and Dale, B. A. (1989) J. Biol. Chem. 264, 1837-1846). In a keratinocyte cell line derived from newborn rat epidermis, these two stages are independently regulated. Profilaggrin was expressed when the cells reached confluence; processing to intermediates began 24-36 h later (stage one), with filaggrin appearing at 48 h (stage two). Stage two processing required calcium in the medium with maximum processing occurring at 5-10 mM. Furthermore, stage two processing was inhibited by nifedipine, a calcium channel blocker, suggesting that calcium influx activates this event. Second-stage processing was also inhibited by the protease inhibitor leupeptin, implicating calpain. Confluent cells had higher levels of calpain I than subconfluent cells; in confluent cells, two immunoreactive bands were detected, comigrating with inactive (80 kDa) and activated (78 kDa) calpain I. In cells processing profilaggrin, most of the calpain I was in the 78-kDa form, implying extensive activation, supporting a role for calpain in processing.

Animals↗
PubMed2006

Common loss-of-function variants of the epidermal barrier protein filaggrin are a major predisposing factor for atopic dermatitis.

Atopic disease, including atopic dermatitis (eczema), allergy and asthma, has increased in frequency in recent decades and now affects approximately 20% of the population in the developed world. Twin and family studies have shown that predisposition to atopic disease is highly heritable. Although most genetic studies have focused on immunological mechanisms, a primary epithelial barrier defect has been anticipated. Filaggrin is a key protein that facilitates terminal differentiation of the epidermis and formation of the skin barrier. Here we show that two independent loss-of-function genetic variants (R510X and 2282del4) in the gene encoding filaggrin (FLG) are very strong predisposing factors for atopic dermatitis. These variants are carried by approximately 9% of people of European origin. These variants also show highly significant association with asthma occurring in the context of atopic dermatitis. This work establishes a key role for impaired skin barrier function in the development of atopic disease.

Alleles↗
PubMed1993

The cytokeratin filament-aggregating protein filaggrin is the target of the so-called "antikeratin antibodies," autoantibodies specific for rheumatoid arthritis.

In rheumatoid arthritis (RA), the high diagnostic value of serum antibodies to the stratum corneum of rat esophagus epithelium has been widely reported. These so-called "antikeratin antibodies," detected by indirect immunofluorescence, were found to be autoantibodies since they also labeled human epidermis. Despite their name, the actual target of these autoantibodies was not known. In this study, a 40-kD protein (designated as 40K), extracted from human epidermis and specifically immunodetected by 75% of RA sera, was purified and identified as a neutral/acidic isoform of basic filaggrin, a cytokeratin filament-aggregating protein, by peptide mapping studies and by the following evidences: (a) mAbs specific for filaggrin reacted with the 40K protein; (b) the autoantibodies, affinity-purified from RA sera on the 40K protein, immunodetected purified filaggrin; (c) the reactivity of RA sera to the 40K protein was abolished after immunoadsorption with purified filaggrin; (d) the 40K protein and filaggrin had similar amino acid compositions. Furthermore, autoantibodies against the 40K protein and the so-called "antikeratin antibodies" were shown, by immunoadsorption experiments, to be largely the same. The identification of filaggrin as a RA-specific autoantigen could contribute to the understanding of the pathogenesis of this disease and, ultimately, to the development of methods for preventing the autoimmune response.

Amino Acids↗
PubMed1987

Exposure to 12-O-tetradecanoylphorbol-13-acetate (TPA) induces the synthesis of histidine-rich protein (filaggrin) in monolayer cultures of rat keratinocytes.

The effect of 12-O-tetradecanoylphorbol-13-acetate (TPA), a potent tumor promoter, on epidermal differentiation has been studied by investigating the appearance of the epidermal differentiative marker protein, histidine-rich protein (HRP), in monolayer cultures of rat keratinocytes grown in low-calcium (0.1 mM) medium. Monoclonal antibody, 3F6-6, raised against the 60K HRP (HRPII) derived from the epidermis of the newborn rat was utilized to detect HRP in cultured keratinocytes. As a major component of keratohyalin in the cells of the granular layer in epidermis, HRP is not normally found in a monolayer culture of rat keratinocytes containing a high population of proliferating cells. However, when these cultures were exposed to 10 ng/ml of TPA, DNA and protein synthesis were decreased by up to 95% and 60%, respectively, and the cells in the monolayer culture became HRP-positive within 18-24 h. TPA has been shown to cause a withdrawal of the basal cells from the cell cycle and a commitment of these cells to an accelerated rate of terminal differentiation. Exposure to TPA at the same time that the calcium level of the monolayer cultures was raised to 2.0 mM in order to allow stratification resulted in positive immunostaining for HRP much earlier and much more intensively than in the absence of TPA. TPA also enhanced stratification of these cultures; however, the positive expression of HRP preceded the stratification. These observations support the view that the induction of terminal differentiation occurs independently of stratification and that the process of terminal differentiation (maturation) of basal cells precedes and triggers the movement of these cells to a suprabasal position (stratification).

Animals↗
PubMed1982

Characterization of a phosphorylated form of the intermediate filament-aggregating protein filaggrin.

Filaggrin and a phosphorylated form of filaggrin, which has been shown by pulse-chase studies to be a precursor form of the protein [Dale, B. A., & Ling, S. Y. (1979) Biochemistry 18, 3539-3546], were compared for functional, biochemical, and physical properties. Filaggrin reacts with keratin filaments to form visible macrofibrils, unlike the precursor which does not. Biochemical and peptide-mapping studies suggest that the two proteins have similar, perhaps identical, amino acid sequences. The major differences between the two proteins are in molecular weight (precursor, 44 200 g/mol; filaggrin, 38 400 g/mol), the existence of oligomeric forms of the precursor, and the presence of phosphate in the precursor (15-20 mol/mol of protein). Phosphoserine was identified in the precursor, but neither phosphothreonine nor phosphotyrosine was observed. The results of proteolytic digests of [32P]phosphate-radiolabeled precursor show that the phosphate is unevenly distributed throughout the molecule and may be localized in approximately 30% of the precursor. A discrete localization of the phosphate in the precursor may block a specific keratin filament combining site and so prevent premature aggregation of these filaments during epidermal differentiation. It is suggested that a specific phosphatase is involved in the dephosphorylation, because several phosphatases of general specificity, including rat epidermal lysosomal acid phosphatase, did not catalyze this conversion.

Amino Acids↗
PubMed1982

Abnormal epidermal keratinization in the repeated epilation mutant mouse.

Repeated epilation (Er) is a radiation-induced, autosomal, incomplete dominant mutation in mice which is expressed in heterozygotes but is lethal in the homozygous condition. Many effects of the mutation occur in skin: the epidermis in Er/Er mice is adhesive (oral and nasal orifices fuse, limbs adhere to the body wall), hyperplastic, and fails to undergo terminal differentiation. Skin from fetal +/+, Er/+ and Er/Er mice at ages pre- and postkeratinization examined by light, scanning, and transmission electron microscopy showed marked abnormalities in tissue architecture, differentiation, and cell structure; light and dark basal epidermal cells were separated by wide intercellular spaces, joined by few desmosomes, and contained phagolysomes. The numbers of spinous, granular, and superficial layers were highly variable within any given region and among various regions of the body. In some areas, 2-8 layers of granular cells, containing large or diminutive keratohyalin granules, extended to the epidermal surface; in others, the granular layers were covered by several layers of partially keratinized or nonkeratinized cells. In rare instances, a single or small group of cornified cells was present among the granular layers but was not associated with the epidermal surface. Both the granular and nonkeratinized/partially keratinized upper epidermal layers Er/Er skin gave positive immunofluorescence with antiserum to the histidine-rich, basic protein, filaggrin. Proteins in epidermal extracts from +/+, Er/+ and Er/Er mice were separated and identified by radio- and immunolabeling techniques. The Er/Er extract was missing a 26.5- kdalton protein and had an altered ratio of bands in the keratin region. The 26.5-kdalton band was histidine-rich and cross-reacted with the antiserum to rat filaggrin. Several high molecular weight bands present in both Er/Er and +/+ extracts also reacted with the antiserum. These are presumed to be the precursors of filaggrin and to account for the immunofluorescence om Er/Er epidermis even though the product protein is absent. The morphologic and biochemical data indicated that the genetic defect has a general and profound influence on epidermal differentiation, including alteration of two proteins (filaggrin and keratin) important in normal terminal differentiation, tissue architecture, and cytology. Identification of epidermal abnormalities at early stages of development (prekeratinization) and defective structure of other tissues and gross anatomy suggest that the mutation is responsible for a defect in same regulatory step important in many processes of differentiation and development.

Animals↗
PubMed1983

The characterization of human epidermal filaggrin. A histidine-rich, keratin filament-aggregating protein.

Filaggrin is a histidine-rich, cationic protein that aggregates with keratin filaments in vitro and may function as the keratin matrix protein in the terminally differentiated cells of the epidermis. This protein has been previously isolated from rodent epidermis. In this investigation, a similar protein from human skin was identified, isolated and characterized by biochemical and immunologic techniques. Indirect immunofluorescence of human skin using antiserum to rat filaggrin gave positive immunofluorescence of keratohyalin granules and the stratum corneum. This indicated the presence of a human filaggrin in the epidermis in a localization similar to that of the rodent. The protein was isolated from human epidermis and purified by ion-exchange chromatography and preparative gel electrophoresis. The purified protein crossreacts with antibody to rat filaggrin and migrates as a doublet of molecular weight (Mr) approximately 35 000 on SDS-polyacrylamide gels. It is relatively rich in polar amino acids such as histidine, arginine, serine and glycine, but is poor in nonpolar amino acids. Unlike rodent filaggrin, the human protein contains ornithine. This protein aggregates with human keratin filaments, forming compact macrofibrils in a manner analogous to that of rodent filaggrin. Thus, a human epidermal protein has been isolated which has many of the characteristics of rodent filaggrin and may function as the human keratin matrix protein.

Amino Acids↗
PubMed1995

The proteins elafin, filaggrin, keratin intermediate filaments, loricrin, and small proline-rich proteins 1 and 2 are isodipeptide cross-linked components of the human epidermal cornified cell envelope.

The cornified cell envelope (CE) is a 15-nm thick layer of insoluble protein deposited on the intracellular side of the cell membrane of terminally differentiated stratified squamous epithelia. The CE is thought to consist of a complex amalgam of proteins cross-linked by isodipeptide bonds formed by the action of transglutaminases, but little is known about how or in which order the several putative proteins are cross-linked together. In this paper, CEs purified from human foreskin epidermis were digested in two steps by proteinase K, which released as soluble peptides about 30% and then another 35% of CE protein mass, corresponding to approximately the outer third (cytoplasmic surface) and middle third, respectively. Following fractionation, 145 unique peptides containing two or more sequences cross-linked by isodipeptide bond(s) were sequenced. Based on these data, most (94% molar mass) of the outer third of CE structure consists of intra- and interchain cross-linked loricrin, admixed with SPR1 and SPR2 proteins as bridging cross-links between loricrin. Likewise, the middle third of CE structure consists largely of cross-linked loricrin and SPR proteins, but is mixed with the novel protein elafin which also forms cross-bridges between loricrin. In addition, cross-links involving loricrin and keratins 1, 2e, and 10 or filaggrin were recovered in both levels. The data establish for the first time that these several proteins are indeed cross-linked protein components of the CE structure. In addition, the data support a model for the intermediate to final stages of CE assembly: the proteins elafin, SPR1 and SPR2, and loricrin begin to be deposited on a preformed scaffold; later, elafin deposition decreases as loricrin and SPR accumulation continues to effect final assembly. The recovery of cross-links involving keratins further suggests that the subjacent cytoplasmic keratin intermediate filament-filaggrin network is anchored to the developing CE during these events.

Amino Acid Sequence↗
PubMed1984

Abnormal keratinization in the pupoid fetus (pf/pf) mutant mouse epidermis.

During its development the epidermis of the pf/pf mutant mouse is invaded by cells from the underlying dermis. These invading cells establish a network of cells including fibroblasts, endothelial cells, and nerve fibers, throughout the epidermis. Subsequent to these events the keratohyalin protein, filaggrin, is drastically reduced and keratinization fails to occur. Heterotypic tissue recombinations indicate that the pf gene is not expressed in the skin. After simply grafting whole mutant dorsal skin, filaggrin synthesis is initiated and an orderly process of epidermal differentiation is achieved. These results suggest that the pf gene acts systemically and that the failure of epidermal differentiation in the mutant occurs secondary to abnormal epidermal organization.

Animals↗
PubMed1998

Abnormal cornified cell envelope formation in mutilating palmoplantar keratoderma unrelated to epidermal differentiation complex.

Mutilating palmoplantar keratoderma represents a heterogeneous group of disorders, unified by characteristic mutilation of the fingers or toes, associated with palmoplantar keratoderma. Although loricrin gene mutations were recently reported in Vohwinkel's syndrome and erythrokeratoderma, the genetic basis of mutilating palmoplantar keratoderma is largely unexplored. We studied a family of non-Vohwinkel's syndrome, nonerythrokeratoderma mutilating palmoplantar keratoderma. The proband and his sister were similarly affected. Recessive inheritance was expected from the consanguineous family history. The patients had hyperkeratosis restricted to the palms and the soles. No other body sites were affected. Digital constriction was seen on all the fingers and the mutilation was severe on the distal interphalangeal region of several fingers. Histopathologically, hyperkeratosis without parakeratosis was seen in the lesional skin. Ultrastructural, immunohistochemical, and immunoelectron microscopic analyses revealed malformed cornified cell envelopes, the abnormal intracytoplasmic loricrin retention, and reduced deposition of loricrin to cornified cell envelopes. Involucrin and small proline-rich proteins 1 and 2 were normally distributed. Sequencing of the entire exons and exon-intron borders of loricrin gene of the patients excluded a mutation in loricrin DNA sequence. Linkage analysis excluded the possibility of causative mutation in the epidermal differentiation complex region of 1q21, including loricrin, involucrin, small proline-rich proteins, filaggrin, and trichohyalin. These data confirm the presence of non-Vohwinkel's syndrome mutilating palmoplantar keratoderma phenotype with abnormal loricrin cross-linking at the final stage of cornified cell envelope formation, which is caused by mutations outside the epidermal differentiation complex region.

Adult↗
PubMed1992

[Ozena and allergic rhinitis in ichthyosis vulgaris].

The clinical course of an ozaena in a patient with an autosomal dominant ichthyosis vulgaris was complicated by the skin disease related atopic disposition with allergic rhinitis. Electron microscopic studies of the pathologically keratinized mucosa of the nasopharynx revealed a similar defect of the mucosal keratohyalin caused by the absence of the protein filaggrin.

Chromosome Aberrations↗
PubMed1995

Characterization of profilaggrin endoproteinase 1. A regulated cytoplasmic endoproteinase of epidermis.

Profilaggrin, an insoluble precursor of the intermediate filament-associated protein filaggrin, contains multiple internal repeats (PIRs). At terminal differentiation of epidermis, proteolytic processing within a "linker" region of each PIR releases soluble filaggrin in a two-stage process. The first stage endoproteinase (PEP1, profilaggrin endoproteinase 1) cleaves mouse profilaggrin at a subset of the linkers, yielding processing intermediates consisting of several filaggrin repeats. An epidermal endoproteinase that cleaves the requisite linker subset has been purified 4,966-fold from mouse epidermal extracts. SDS-polyacrylamide gel electrophoresis demonstrated a band of molecular mass of 29.5 kDa that correlated with the activity. Labeling with [3H]diisopropylfluorophosphate identified PEP1 as a serine protease; inhibitor studies suggest that it is similar to chymotrypsin, as expected from previous in vivo studies. The purified PEP1 cleaved a peptide derived from profilaggrin (P1) at three residues within and adjacent to a multiple tyrosine sequence, consistent with the in vivo processing sites. No exopeptidase activity was detected. PEP1 is only active toward insoluble profilaggrin, resulting in partial solubilization, consistent with a role in dispersal of profilaggrin during terminal differentiation. In contrast to the specific cleavage of mouse profilaggrin, PEP1 cleaved all linker regions of rat profilaggrin. Studies with phosphorylated P1 suggest that PEP1 specificity may be partly regulated by profilaggrin phosphorylation.

Amino Acid Sequence↗
PubMed2002

In utero exposure to 2,3,7,8-tetrachlorodibenzo-p-dioxin causes accelerated terminal differentiation in fetal mouse skin.

2,3,7,8 Tetrachlorodibenzo-p-dioxin (TCDD), a ubiquitous environmental toxin, has been shown to cause a human skin pathology called chloracne. The majority of laboratory mouse strains, with the exception of mice bearing a mutation in thehairless gene, fail to display overt signs of chloracne upon exposure to TCDD. As a result, only minimal data exist on the effects of TCDD in adult haired mice and no data exist on the effects of TCDD in developing mouse skin. Here we report that TCDD affects the temporal expression of protein markers of keratinocyte terminal differentiation during murine skin morphogenesis. Immunohistochemical analysis of E16 mice reveals accelerated expression of the intermediate filament-associated protein filaggrin in response to TCDD. At a later developmental time and after birth, expression of filaggrin and loricrin is indistinguishable between treatment and control groups. At E16 expression of keratins 5, 6, and 10 are unaltered in TCDD-exposed individuals and TUNEL analysis shows no apoptotic cells in the basal and spinous layers of either treatment or control groups. At E16, immunohistochemical analysis of AhR-null mouse skin reveals accelerated filaggrin expression in both vehicle and TCDD exposed animals. We therefore hypothesize that AhR acts as a modulator of late stage keratinocyte terminal differentiation.

Animals↗
PubMed1987

Arrested epidermal morphogenesis in three newborn infants with a fatal genetic disorder (restrictive dermopathy).

Two sibs and one unrelated infant were born prematurely with taut, shiny, restrictive skin that was abnormal in structure, organization, biochemistry, and state of differentiation. Prominent abnormalities in all regions of the skin were recognized by light and electron microscopy, immunohistochemistry, and biochemistry. The epidermis was hyperplastic, hyperkeratotic, and parakeratotic. Keratohyaline granules were abnormal in structure, but the keratohyalin-derived protein filaggrin was apparently normal in quantity and biochemistry. The epidermal cells contained less than the expected quantity of high-molecular-weight, differentiation-specific keratins and the tissue stained with antikeratin antibodies in an aberrant pattern. Additional 48 and 56 kD keratin polypeptides, indicative of a hyperproliferative state, were expressed. The dermal-epidermal junction was remarkably flat and the dermis was thinner than normal. The connective tissue appeared stretched and was oriented like tendon rather than dermis. Collagen fiber bundles and fibrils were smaller in diameter than normal. The nails were normal but other epidermal appendages such as the pilosebaceous structures and the eccrine sweat glands were underdeveloped, suggesting that morphogenesis of these structures was arrested at an early stage in utero. The subcutaneous fat was at least twice the thickness of the dermis. The skin abnormalities appeared to be the cause of the flexion contractions, characteristic facies, and inability to survive because of restricted respiratory movements. The structural and biochemical abnormalities in the skin of affected infants may serve as markers for prenatal and postnatal diagnosis of the disorder, and may provide insight into the basic mechanism of the disease.

Filaggrin Proteins↗
PubMed1997

Cytokeratin expression in normal human bulbar conjunctiva obtained by impression cytology.

PURPOSE: To document the cytokeratin expression patterns in the normal human conjunctival epithelium obtained directly from patients using impression cytology. METHODS: Impression cytology specimens were obtained from normal volunteers using pure nitrocellulose membranes rather than cellulose acetate. The 31 volunteers of both sexes ranged in age from 18 to 79 years. Impression cytology specimens were analyzed for individual cytokeratins by either immunocytochemistry or electrophoresis with immunoblotting using a defined panel of monoclonal antibodies. RESULTS: Using the corroborative methods of immunocytochemistry and electrophoresis with immunoblotting, cytokeratins characteristic of nonkeratinized, stratified (K4 and K13), simple (K8 and K19), and glandular epithelia (K7) were present in the superficial layer (s) of normal human conjunctiva. Cytokeratins typical of keratinized epithelia (K1, K2, and K10) and the keratinization-related proteins filaggrin and involucrin were not expressed in normal conjunctival epithelium. CONCLUSIONS: The normal human conjunctiva demonstrates a unique cytokeratin expression pattern containing cytokeratins characteristic of nonkeratinized, stratified epithelia, as well as others more typical of a simple differentiation pattern, a glandular differentiation pattern, or both. These findings provide a foundation for examining changes in the cytokeratin expression pattern in diseased human conjunctival epithelium using impression cytology.

Adolescent↗