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  • 1
    Keywords: PROTEINS ; EXPRESSION ; CELL ; Germany ; BIOLOGY ; keratin ; INTERMEDIATE-FILAMENTS ; cytoskeleton ; RE ; review ; GENE DOMAIN ; FOLLICLE ; HUMAN TYPE-I ; intermediate filament ; HAIR FOLLICLE ; keratins ; ALPHA-KERATIN ; COMPANION LAYER ; EPITHELIAL KERATIN ; hair ; hair keratins ; INNERMOST CELL LAYER ; OUTER ROOT SHEATH ; RESOLUTION 2-DIMENSIONAL ELECTROPHORESIS
    Abstract: Intermediate filaments are a large family of proteins that are the cytoskeletal elements involved in a number of skin, liver, neuromuscular, cardiac, eye and hair diseases. Intermediate filament genes are regulated in a tissue-and cell type-specific manner and their polymerized protein products protects the cells and tissue they are part of against a variety of mechanical and nonmechanical stresses. This book provides a comprehensive resource of methodology essentials, describing a variety of essential tools and assays for studying intermediate filaments. The book provides user-friendly advice and protocols covering all aspects of intermediate filaments including protein isolation and structure, protein and gene regulation, relationship to disease and apoptosis, and associated proteins. Both mammalian and non-mammalian systems and animal models are covered, making this book a must-have for any investigator wishing to study IF genes or their protein products. This book covers intermediate filaments from crystallography, protein chemistry, cell and molecular biology, microrheology, gene regulation, to animal models and human disease. It is practical and user-friendly with detailed 'how-to-protocols and tricks of the trade'. It includes detailed tables of useful reagents, vendors and web links. Synopsis Intermediate filaments are a large family of proteins that are the cytoskeletal elements involved in a number of skin, liver, neuromuscular, cardiac, eye and hair diseases. Intermediate filament genes are regulated in a tissue- and cell type-specific manner and their polymerized protein products protects the cells and tissue they are part of against a variety of mechanical and nonmechanical stresses. This book provides a comprehensive resource of methodology essentials, describing a variety of essential tools and assays for studying intermediate filaments. The book provides user-friendly advice and protocols covering all aspects of intermediate filaments including protein isolation and structure, protein and gene regulation, relationship to disease and apoptosis, and associated proteins. Both mammalian and non-mammalian systems and animal models are covered, making this book a must-have for any investigator wishing to study IF genes or their protein products. This book covers intermediate filaments from crystallography, protein chemistry, cell and molecular biology, microrheology, gene regulation, to animal models and human disease. It is practical and user-friendly with detailed 'how-to-protocols' and 'tricks of the trade'. It includes detailed tables of useful reagents, vendors and web links.
    Type of Publication: Book chapter
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  • 2
    Keywords: CELLS ; EXPRESSION ; tumor ; CELL ; Germany ; human ; PATHWAY ; GENE ; GENE-EXPRESSION ; GENES ; DIFFERENTIATION ; TUMORS ; COMPLEX ; COMPLEXES ; INDUCTION ; CONTRAST ; SKIN ; LOCALIZATION ; BENIGN ; keratin ; skin tumors ; epidermis ; FOLLICLE ; HAIR-FOLLICLES ; HUMAN TYPE-I ; MATRIX ; BETA-CATENIN EXPRESSION ; CORTEX ; HAIR FOLLICLE ; hair follicles,human,transcription factors,tumors ; HOXC13 ; INVOLUCRIN
    Abstract: Human hair follicles exhibit a complex pattern of sequential hair keratin expression in the hair matrix, cuticle, and cortex. In pilomatricomas, that is, benign skin tumors thought to arise from germinative matrix cells of the hair follicle and retaining morphological signs of cortical differentiation, this differential hair keratin pattern has been shown to be faithfully preserved in the lower and upper transitional cell compartments of the tumors. Here we show that also the co-expression of hair keratin hHa5 with its regulatory nuclear homeoprotein HOXC13 in matrix cells of the hair follicle is maintained in lower transitional cells of pilomatricomas. In contrast, the nuclear co-expression of LEF1 and beta-catenin, which in the hair follicle has been postulated to initiate cortex cell differentiation through the induction of hair keratin hHa1 expression (Merill et al, Genes Dev 15:1688-1705, 2001), is not preserved in upper transitional cells of pilomatricomas. Although these cells correctly express hHa1, they are completely devoid of LEF1 and nuclear LEF1/beta-catenin co-expression is shifted to a subpopulation of hair keratin-free basaloid cells of the tumors. These data imply that unlike the normal hair follicle, cortical differentiation in pilomatricomas is not under the control of the canonical Wnt signaling pathway
    Type of Publication: Journal article published
    PubMed ID: 15140206
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  • 3
    Keywords: COMBINATION ; human ; PROTEIN ; PROTEINS ; COMPLEX ; COMPLEXES ; FAMILY ; SEQUENCE ; POLYMORPHISMS ; NUMBER ; NMR ; DATABASE ; intermediate filaments ; keratin ; SEQUENCE-ANALYSIS ; CLUSTERS ; GENE DOMAIN ; FOLLICLE ; RESIDUES ; ALPHA-KERATIN ; hair ; CONFORMATION ; modelling ; PROLINE ; keratin-associated protein
    Abstract: In this paper, we undertake a sequence analysis of the human keratin-associated proteins (KAP). This analysis has revealed two fundamental pentapeptide quasi-repeats (A and B) of the form C-C-X-P-X and C-C-X-S/T-S/T, respectively. The A repeats are also commonly found in two subforms A(1) and A(2), -C-C-Q-P-X and C-C-R-P-X, respectively-similar to those found in sheep wool 30-40 years previously. Some high-sulphur and ultra-high sulphur proteins contain predominantly A repeats or B repeats but not regular combinations of them, whereas others are characterised by a contiguous pair of pentapeptide repeats that largely (though imperfectly) alternate to generate decapeptide motifs of the form AB, A(1)B or A(2)B. The A and B repeats sometimes occur in complex runs and can generate both 19- and 20-residue repeats of the form BABB' or BA(1)AA, respectively, where the prime indicates a motif truncated by one residue. Likewise, a 42-residue repeat with BA(1)BXAAAB (40 residues) separated by a di-serine (two residues) has been observed in an ultra-high sulphur protein from cuticle. To understand the possible conformations adopted by the A and B motifs, a search was initiated of the PDB structural database for a number of overlapping pentapeptide repeats. The total number of matches was 658 and these were found in 451 different proteins. From representative and unique structures the means and standard deviations were calculated for the Phi(i) and psi(i) angles for the C-C-X P-X and the C-C-X-S/T-S/T motifs. Molecular modelling has been employed to represent the "average" structure found from crystallographic and nmr data determined for each motif in other proteins. The conformation of consecutive A repeats with proline residues in the cis state is akin to a string of disulphide bond-stabilised pentapeptide knots between which there is relative freedom of rotation about the single bonds that link them. For B pentapeptides, however, the likelihood that a similar disulphide bond is formed appears much lower. This may give additional conformational flexibility to the chain and hence allow the A pentapeptides greater opportunity to interact appropriately with the IF via disulphide bonds, ionic interactions and/or hydrogen bonding. (c) 2006 Elsevier Inc. All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 16713301
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  • 4
    Keywords: CELL, DIFFERENTIATION, FAMILY, FOLLICLE, GENE DOMAIN, Germany, human, Jun, keratin, MEMBERS, NEW-YOR
    Type of Publication: Journal article published
    PubMed ID: 17301834
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  • 5
    Keywords: CELLS ; EXPRESSION ; Germany ; FOLLICLE ; HUMAN TYPE-I ; INNER-ROOT-SHEATH ; COMPANION LAYER ; EPITHELIAL KERATIN ; GENE FAMILY ; INTERMEDIATE-FILAMENT STRUCTURE ; MOUSE TAIL EPIDERMIS ; SCALP HAIR
    Abstract: We have investigated the expression of 52 of the 54 keratins in beard hair medulla. We found that not only 12 hair keratins but, unexpectedly, also 12 epithelial keratins are potentially expressed in medulla cells. The latter comprise keratins also present in outer- and inner-root sheaths and in the companion layer. Keratins K5, K14, K17, K25, K27, K28, and K75 define a "pre-medulla,'' composed of cells apposed to the upper dermal papilla. Besides K6, K16, K7, K19, and K80, all pre-medullary epithelial keratins continue to be expressed in the medulla proper, along with the 12 hair keratins. Besides this unique feature of cellular keratin co-expression, the keratin pattern itself is highly variable in individual medulla cells. Remarkably, both epithelial and hair keratins behave highly promiscuously with regard to heterodimer- and IF formation, which also includes keratin chain interactions in IF bundles. We also identified cortex cells within the medullary column. These exhibit all the properties of genuine cortex cells, including a particular type of keratin heterogeneity of their compact IF bundles. In both keratin expression profile and keratin number, medulla cells are distinct from all other cells of the hair follicle or from any other epithelium
    Type of Publication: Journal article published
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  • 6
    Abstract: OBJECTIVES: To report the clinical features of the loose anagen hair syndrome and to test the hypothesis that the typical gap between the hair and the inner root sheath may result from hereditary defects in the inner root sheath or the apposed companion layer. DESIGN: Case series. SETTING: A pediatric dermatology unit (referral center). PATIENTS: A consecutive sample of 17 children (13 girls). For 9 of them and their first-degree relatives, molecular analyses were performed in the K6HF gene with 50 appropriate controls. INTERVENTION: Minoxidil therapy (5% lotion) in 11 patients for 1 to 12 months. MAIN OUTCOME MEASURES: Clinical and follow-up features and determination of mutations in the K6HF gene. RESULTS: Most patients had easily pluckable hair with no sign of scalp inflammation or scarring. Ten patients seldom cut their hair, and 4 had unmanageable hair. One patient had hypodontia. Two patients had an additional clinical phenotype of diffuse partial woolly hair. The family history was positive for loose anagen hair syndrome in 5 patients. Marked improvement was noted after treatment with 5% minoxidil lotion in 7 of the 11 patients treated. Polymerase chain reaction analysis of the gene segments encoding the alpha-helical 1A and 2B subdomains of K6hf, the type II cytokeratin exclusively expressed in the companion layer, was performed in 9 families. In 3 of these 9 families, a heterozygous glutamic acid and lysine mutation, E337K, was identified in the L2 linker region of K6HF. CONCLUSIONS: Diffuse partial woolly hair can be associated with loose anagen hair syndrome. A keratin mutation, E337K in K6HF, was possibly causative in 3 of the 9 families studied. Another keratin, and possibly the type I partner of K6hf, could be responsible for loose anagen hair syndrome in other patients, or the gene involved may be a minor gene.
    Type of Publication: Journal article published
    PubMed ID: 11939812
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  • 7
    Keywords: IN-VITRO ; GENE-EXPRESSION ; INTERMEDIATE-FILAMENTS ; REVEALS ; CORNIFIED CELL-ENVELOPE ; human hair follicle ; HUMAN EPIDERMIS ; GLAND DEVELOPMENT ; EPITHELIAL KERATINS ; SWEAT GLANDS
    Abstract: The differential expression of keratins is central to the formation of various epithelia and their appendages. Structurally, the type II keratin K77 is closely related to K1, the prototypical type II keratin of the suprabasal epidermis. Here, we perform a developmental study on K77 expression in human and murine skin. In both species, K77 is expressed in the suprabasal fetal epidermis. While K77 appears after K1 in the human epidermis, the opposite is true for the murine tissue. This species-specific pattern of expression is also found in conventional and organotypic cultures of human and murine keratinocytes. Ultrastructure investigation shows that, in contrast to K77 intermediate filaments of mice, those of the human ortholog are not attached to desmosomes. After birth, K77 disappears without deleterious consequences from human epidermis while it is maintained in the adult mouse epidermis, where its presence has so far gone unnoticed. After targeted Krt1 gene deletion in mice, K77 is normally expressed but fails to functionally replace K1. Besides the epidermis, both human and mouse K77 are present in luminal duct cells of eccrine sweat glands. The demonstration of a K77 ortholog in platypus but not in non-mammalian vertebrates identifies K77 as an evolutionarily ancient component of the mammalian integument that has evolved different patterns of intracellular distribution and adult tissue expression in primates.
    Type of Publication: Journal article published
    PubMed ID: 24057875
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  • 8
    Keywords: APOPTOSIS ; PROTEIN ; INDUCTION ; ASSOCIATION ; CERVICAL-CANCER ; p53 ; POSITIVE CANCER-CELLS ; NUCLEAR-LOCALIZATION ; E6-MEDIATED DEGRADATION ; AGGRESOMES
    Abstract: Oncogenic types of human papillomaviruses (HPVs) cause cervical cancer and other malignancies in humans. The HPV E6 oncoprotein is considered to be an attractive therapeutic target since its inhibition can lead to the apoptotic cell death of HPV-positive cancer cells. The HPV type 16 (HPV16) E6-binding peptide pep11, and variants thereof, induce cell death specifically in HPV16-positive cancer cells. Although they do not encompass the LxxLL binding motif found in cellular HPV16 E6 interaction partners, such as E6AP, the pep11 variants strongly bind to HPV16 E6 by contacting the recently identified E6AP binding pocket. Thus, these peptides can serve as prototype E6-inhibitory molecules which target the E6AP pocket. We here analyzed their intracellular interaction with HPV16 E6. By comprehensive intracellular binding studies and GST pull-down assays, we show that E6-binding competent pep11 variants induce the formation of a trimeric complex, consisting of pep11, HPV16 E6 and p53. These findings indicate that peptides, which do not contain the LxxLL motif, can reshape E6 to enable its interaction with p53. The formation of the trimeric HPV16 E6 / peptide / p53 complex was associated with an increase of endogenous HPV16 E6 protein amounts. Yet, total cellular p53 amounts were also increased, indicating that the E6 / E6AP-mediated degradation of p53 is blocked. These findings suggest that inhibition of oncogenic activities by targeting the E6AP pocket on HPV16 E6 could be a strategy for therapeutic intervention.
    Type of Publication: Journal article published
    PubMed ID: 26151636
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  • 9
    Keywords: CELLS ; EXPRESSION ; Germany ; human ; CLONING ; GENE ; GENES ; HYBRIDIZATION ; DIFFERENTIATION ; DOMAIN ; IN-SITU ; PATTERNS ; gene expression ; cytoskeleton ; intermediate filaments ; keratin ; LAYER ; CELLS FLUGELZELLEN ; CUTICLE CELLS ; CYTOKERATINS ; GENE DOMAIN ; human hair follicle ; HUXLEY ; MAMMALIAN-TISSUES
    Abstract: In this study we report on the cloning of two novel human type II keratin cDNAs, K6irs3 and K6irs4, which were specifically expressed in the inner root sheath of the hair follicle. Together with the genes of two previously described type II inner root sheath keratins, K6irs1 and K6irs2, the K6irs3 and K6irs4 genes were subclustered in the type II keratin/hair keratin gene domain on chromosome 12q13. Evolutionary tree analysis using all known type II epithelial and hair keratins revealed that the K6irs1-4 formed a branch separate from the other epithelial and hair keratins. RNA in situ hybridization and indirect immunofluorescence studies of human hair follicles, which also included the K6irs2 keratin, demonstrated that both K6irs2 and K6irs3 were specifically expressed in the inner root sheath cuticle, but showed a different onset of expression in this compartment. Whereas the K6irs3 expression began in the lowermost bulb region, that of K6irs2 was delayed up to the height of the apex of the dermal papilla. In contrast, the K6irs4 keratin was specifically expressed in the Huxley layer. Moreover, K6irs4 was ideally suited to further investigate the occurrence of Flugelzellen, i.e., Huxley cells, characterized by horizontal cell extensions that pass through the Henle layer, abut upon the companion layer, and form desmosomal connections with the surrounding cells. Previously, we detected Flugelzellen only in the region along the differentiated Henle layer. Using the Huxley-cell-specific K6irs4 antiserum, we now demonstrate this cell type to be clearly apposed to the entire Henle layer. We provide evidence that Flugelzellen penetrate the Henle layer actively and may play a role in conferring plasticity and resilience to the otherwise rigid upper Henle layer
    Type of Publication: Journal article published
    PubMed ID: 12648212
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  • 10
    Keywords: CELLS ; EXPRESSION ; GROWTH ; IN-VITRO ; human ; IN-VIVO ; DISEASE ; GENE ; GENES ; FAMILY ; DOMAIN ; CYCLE ; MEMBER ; MEMBERS ; ALPHA ; culture ; LOCALIZATION ; human hair follicle ; CATALOG ; hard keratin ; HUMAN TYPE-I ; in vitro growth ; organ culture
    Abstract: The keratin family includes epithelial (soft) keratins and hair (hard) keratins, and can be divided into acidic type I and basic to neutral type II subfamilies. Recently, nine type I and six type II hair keratin genes have been characterized through the screening of a human PAC library. The expression of these genes in the hair follicle was determined in vivo and a combined catalog of acidic and basic hair keratins was established. In this study, we investigated the expression and localization of most of the human hair keratin members of both types in human hair grown in vitro. We show that in vitro growth of hair follicles for 10 days in complete William's E culture medium did not alter the expression pattern of hair keratins. Similarly to the in vivo situation, each hair keratin was localized in precise and discrete compartments of the follicle, ranging from the matrix to the upper cortex and/or the hair cuticle. This study shows that the increase in length of in vitro grown follicles was accompanied by the proper hair shaft keratinization process. It also shows that hair follicle integrity was maintained in vitro, both in terms of gross morphology and molecular organization despite the complexity of the keratin expression pattern
    Type of Publication: Journal article published
    PubMed ID: 12702144
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