Specialized keratin expression pattern in human ridged skin as an adaptation to high physical stress

Swensson,; Langbein,; McMillan,; Stevens, '; Leigh,; McLean, W.H. Irwin; Lane, .; Eady,

doi:10.1046/j.1365-2133.1998.02499.x

Cited by 114 publications

(120 citation statements)

References 41 publications

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“…3F). Regarding K6, which is normally expressed in hair follicle keratinocytes and in some basal and suprabasal keratinocytes in ridged skin (Swensson et al, 1998), we found expression in the companion layer of epidermal hair follicles without any difference between K5-Cre KO and control animals (Fig. 3G,H).…”

Section: Highly Efficient Reduction Of Plectin Levels By K5-controllementioning

confidence: 74%

Conditional targeting of plectin in prenatal and adult mouse stratified epithelia causes keratinocyte fragility and lesional epidermal barrier defects

Ackerl

Walko

Fuchs

et al. 2007

Journal of Cell Science

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Plectin, a widespread intermediate filament-based cytolinker protein capable of interacting with a variety of cytoskeletal structures and plasma membrane-bound junctional complexes, serves essential functions in maintenance of cell and tissue cytoarchitecture. We have generated a mouse line bearing floxed plectin alleles and conditionally deleted plectin in stratified epithelia. This strategy enabled us to study the consequences of plectin deficiency in this particular type of tissues in the context of the whole organism without plectin loss affecting other tissues. Conditional knockout mice died early after birth, showing signs of starvation and growth retardation. Blistering was observed on their extremities and on the oral epithelium after initial nursing, impairing food uptake. Knockout epidermis was very fragile and showed focal epidermal barrier defects caused by the presence of small skin lesions. Stratification, proliferation and differentiation of knockout skin seemed unaffected by epidermis-restricted plectin deficiency. In an additionally generated mouse model, tamoxifen-induced Cre-ERT-mediated recombination led to mice with a mosaic plectin deletion pattern in adult epidermis, combined with microblister formation and epidermal barrier defects. Our study explains the early lethality of plectin-deficient mice and provides a model to ablate plectin in adult animals which could be used for developing gene or pharmacological therapies.

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Section: Highly Efficient Reduction Of Plectin Levels By K5-controllementioning

confidence: 74%

Conditional targeting of plectin in prenatal and adult mouse stratified epithelia causes keratinocyte fragility and lesional epidermal barrier defects

Ackerl

Walko

Fuchs

et al. 2007

Journal of Cell Science

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“…8b). Collectively, this scenario, which resembles that of the complex epithelial keratin K1, K10, K9, and K2e expression pattern in suprabasal human plantar epidermis (35,36), suggests competitive, complex, and unique type I and type II hair keratin-pairing patterns. The same dynamics hold true for the potential pairing possibilities of matrix keratins and in particular cortex keratins (Fig.…”

Section: Resultsmentioning

confidence: 99%

The Catalog of Human Hair Keratins

Langbein¹,

Rogers²,

Winter³

et al. 2001

Journal of Biological Chemistry

271

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The human type II hair keratin subfamily consists of six individual members and can be divided into two groups. The group A members hHb1, hHb3, and hHb6 are structurally related, whereas group C members hHb2, hHb4, and hHb5 are rather distinct. Specific antisera against the individual hair keratins were used to establish the two-dimensional catalog of human type II hair keratins. In this catalog, hHb5 showed up as a series of isoelectric variants, well separated from a lower, more acidic, and complex protein streak containing isoelectric variants of hair keratins hHb1, hHb2, hHb3, and hHb6. Both in situ hybridization and immunohistochemistry on anagen hair follicles showed that hHb5 and hHb2 defined early stages of hair differentiation in the matrix (hHb5) and cuticle (hHb5 and hHb2), respectively. Although cuticular differentiation proceeded without the expression of further type II hair keratins, cortex cells simultaneously expressed hHb1, hHb3, and hHb6 at an advanced stage of differentiation. In contrast, hHb4, which is undetectable in hair follicle extracts and sections, could be identified as the largest and most alkaline member of this subfamily in cytoskeletal extracts of dorsal tongue. This hair keratin was localized in the posterior compartment of the tongue filiform papillae. Comparative analysis of type II with the previously published type I hair keratin expression profiles suggested specific, but more likely, random keratin-pairing principles during trichocyte differentiation. Finally, by combining the previously published type I hair keratin catalog with the type II hair keratin catalog and integrating both into the existing catalog of human epithelial keratins, we present a two-dimensional compilation of the presently known human keratins.The large keratin multigene family comprises the epithelial keratins (also designated as "cytokeratins" or historically "soft keratins"), which are differentially expressed in the various types of epithelia, and the hair keratins (historically designated as "hard keratins"), which are involved in the formation of hard keratinized structures such as hairs, nails, claws, etc. These keratins can be divided into acidic type I and basicto-neutral type II members, which form the 10-nm intermediate filament network of the cytoskeleton of epithelial cells through the obligatory association of equimolar amounts of type I and type II keratins (for review see Refs. 1-3).Earlier gel electrophoretic studies on native hair keratins of several mammals including man revealed the presence of four type I (44 -48 kDa) and four type II (55-60 kDa) members (4, 5). According to a proposal by Heid et al. (4), hair keratins were collectively designated "H" for hair, "b" for the basic members (Hb), 1 and "a" for the acidic members (Ha), with the two-dimensionally resolved and Coomassie-stained protein spots of each subfamily being numbered from 1 to 4 in a counterclockwise manner. In addition to the "major" hair keratins hHa1-hHa4 and hHb1-hHb4, a weakly expressed additional pair was de...

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“…Several other keratins are expressed in different parts of the epidermis and its appendages, in areas of distinct differentiation. These include the keratin K2e, which is widespread in the upper layers of the human epidermis (Collin et al, 1992), and K9, K6, K16, and K17, which are expressed in palmoplantar epidermis (Swensson et al, 1998). K6, K16, and K17 are also normally expressed in the hair follicles but are induced in suprabasal cells elsewhere during wound healing, tumorigenesis, and some hyperproliferative diseases, usually with a concomitant reduction in expression of K1 and K10 (Weiss et al, 1984;Wilson et al, 1994).…”

mentioning

confidence: 99%

K15 Expression Implies Lateral Differentiation within Stratified Epithelial Basal Cells

et al. 2000

Laboratory Investigation

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SUMMARY:Keratins are intermediate filament proteins whose expression in epithelial tissues is closely linked to their differentiated state. The greatest complexity of this expression is seen in the epidermis and associated structures. The critical basal (proliferative) cell layer expresses the major keratin pair, K5 and K14, but it also expresses an additional type I keratin, K15, about which far less is known. We have compared the expression of K15 with K14 in normal, pathological, and tissue culture contexts; distinct differences in their expression patterns have been observed that imply different regulation and function for these two genes. K15 appears to be preferentially expressed in stable or slowly turning over basal cells. In steady-state epidermis, K15 is present in higher amounts in basal cells of thin skin but in lower amounts in the rapidly turning over thick plantar skin. Although remaining high in basal cell carcinomas (noninvasive) it is suppressed in squamous cell carcinomas (which frequently metastasize). Wounding-stimulated epidermis loses K15 expression, whereas K14 is unchanged. In cultured keratinocytes, K15 levels are suppressed until the culture stratifies, whereas K14 is constitutively expressed throughout. Therefore, unlike K14, which appears to be a fundamental component of all keratinocytes, K15 expression appears to be more tightly coupled to a mature basal keratinocyte phenotype. (Lab Invest 2000, 80:1701-1710.

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Specialized keratin expression pattern in human ridged skin as an adaptation to high physical stress

Cited by 114 publications

References 41 publications

Conditional targeting of plectin in prenatal and adult mouse stratified epithelia causes keratinocyte fragility and lesional epidermal barrier defects

Conditional targeting of plectin in prenatal and adult mouse stratified epithelia causes keratinocyte fragility and lesional epidermal barrier defects

The Catalog of Human Hair Keratins

K15 Expression Implies Lateral Differentiation within Stratified Epithelial Basal Cells

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