Keratin Intermediate Filaments (keratin + intermediate_filament)

Distribution by Scientific Domains


Selected Abstracts


Impact of topical oils on the skin barrier: possible implications for neonatal health in developing countries

ACTA PAEDIATRICA, Issue 5 2002
GL Darmstadt
Topical therapy to enhance skin barrier function may be a simple, low-cost, effective strategy to improve outcome of preterm infants with a developmentally compromised epidermal barrier, as lipid constituents of topical products may act as a mechanical barrier and augment synthesis of barrier lipids. Natural oils are applied topically as part of a traditional oil massage to neonates in many developing countries. We sought to identify inexpensive, safe, vegetable oils available in developing countries that improved epidermal barrier function. The impact of oils on mouse epidermal barrier function (rate of transepidermal water loss over time following acute barrier disruption by tape-stripping) and ultrastructure was determined. A single application of sunflower seed oil significantly accelerated skin barrier recovery within 1 h; the effect was sustained 5 h after application. In contrast, the other vegetable oils tested (mustard, olive and soybean oils) all significantly delayed recovery of barrier function compared with control- or Aquaphor-treated skin. Twice-daily applications of mustard oil for 7 d resulted in sustained delay of barrier recovery. Moreover, adverse ultrastructural changes were seen under transmission electron microscopy in keratin intermediate filament, mitochondrial, nuclear, and nuclear envelope structure following a single application of mustard oil. Conclusion: Our data suggest that topical application of linoleate-enriched oil such as sunflower seed oil might enhance skin barrier function and improve outcome in neonates with compromised barrier function. Mustard oil, used routinely in newborn care throughout South Asia, has toxic effects on the epidermal barrier that warrant further investigation. [source]


Ultrastructural characteristics of the process of cornification in developing claws of the brushtail possum (Trichosurus vulpecula)

ACTA ZOOLOGICA, Issue 3 2009
Lorenzo Alibardi
Abstract Cornification of developing claws in the brush possum has been analysed by electron microscopy and compared with the process in other tetrapods. Newborns from 3 to 60 days postparturition were studied. After formation of symmetric and round outgrowth in digits the epidermis becomes thicker in the dorsal with respect to the ventral digit tip. The claw elongates forming the unguis and a shorter subunguis. Spinosus keratinocytes in both unguis and subunguis accumulate tonofilaments that fill their cytoplasm. Keratohyaline-like granules are formed in early stages of differentiation in both unguis and subunguis but they later disappear in highly cornified corneocytes. Tonofilaments become electron-dense in keratinocytes of the precorneous layer in the large corneocytes of the unguis and in narrow corneocytes of the subunguis. Keratin bundles transform into an amorphous corneous material that embeds or masks the original keratin intermediate filaments. Nucleated corneocytes are accumulated in the unguis while thinner corneocytes are present in the subunguis. The latter contain a dense material, possibly containing high sulphur keratin associated proteins, as occurs during cornifcation of the cortex and cuticle hair cells and in the nail. The process of cornification of mammalian claws is compared with that of reptilian and avian claws. [source]


Keratin 9 gene mutations in five Korean families with epidermolytic palmoplantar keratoderma

EXPERIMENTAL DERMATOLOGY, Issue 6 2003
Joo-Heung Lee
Abstract:, Epidermolytic palmoplantar keratoderma (EPPK) is an autosomal dominant disease characterized clinically by localized palmoplantar thickening and histopathologically by granular degeneration of the epidermis. Recent molecular biological studies have revealed that EPPK is caused by mutations of the keratin 9 gene in sequences mainly encoding the highly conserved 1 A rod domain. Here we demonstrate a novel mutation of N160H (position 8 of the 1 A domain) and two other previously reported mutations, R162W and N160S, in five unrelated Korean families with EPPK. The three-dimensional structure of the 1 A domain of the related vimentin intermediate filament protein chain is now known. Based on its likely similarity to the keratin 9 chain, we predict that inappropriate amino acid substitutions in position 10 of 1 A will likely interfere with coiled-coil dimer stability, and those in position 8 will interfere with tetramer stability. Accordingly, these mutations compromise the structural integrity of the keratin intermediate filaments leading to the pathology of EPPK. [source]


Stratum corneum keratin structure, function and formation , a comprehensive review

INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Issue 6 2006
L. Norlén
Synopsis A comprehensive review on stratum corneum keratin organization, largely based on the recently published cubic rod-packing and membrane templating model [J. Invest. Dermatol., 123, 2004, 715], is presented. Keratin is the major non-aqueous component (wt/wt) of stratum corneum. As 90,100% of the stratum corneum water is thought to be located intracellularly one may presume that keratin also is a major factor (together with filaggrin-derived free amino acids) determining stratum corneum hydration level and water holding capacity. This water holding capacity depends in turn on the structural organization of the corneocyte keratin intermediate filament network. The cubic rod-packing model for the structure and function of the stratum corneum cell matrix postulates that corneocyte keratin filaments are arranged according to a cubic-like rod-packing symmetry. It is in accordance with the cryo-electron density pattern of the native corneocyte keratin matrix and could account for the swelling behaviour and the mechanical properties of mammalian stratum corneum. The membrane templating model for keratin dynamics and for the formation of the stratum corneum cell matrix postulates the presence in viable epidermal cellular space of a highly dynamic small lattice parameter (<30 nm) membrane structure with cubic-like symmetry, to which keratin is associated. It further proposes that membrane templating, rather than spontaneous self-assembly, is responsible for keratin intermediate filament formation and dynamics. It is in accordance with the cryo-electron density patterns of the native keratinocyte cytoplasmic space and could account for the characteristic features of the keratin network formation process, the dynamic properties of keratin intermediate filaments, the close lipid association of keratin, the insolubility in non-denaturating buffers and pronounced polymorphism of keratin assembled in vitro, and the measured reduction in cell-volume and hydration level between stratum granulosum and stratum corneum. Résumé, La kératine est le composant majeur anhydre de la couche cornée. Etant donné que l'on considère que 90 à 100% de l'eau de la couche cornée est localisée à l'intérieur des cellules, on peut penser que la kératine joue également un rôle important (en association avec les acides aminés libres dérivés de la filagrine) dans le niveau d'hydratation de la couche cornée et sa capacité de rétention de l'eau. Cette capacité de rétention de l'eau dépend elle-même de l'organization structurelle du réseau de filaments intermédiaires de la kératine des cornéocytes. Le modèle de cylindre en réseau cubique appliquéà la structure et aux fonctions de la matrice des cellules de la couche cornée stipule que les filaments de la kératine des cornéocytes sont disposés symétriquement, les paquets de fibrilles formant une structure cubique. Ceci est conforme au modèle de densité cryo-électronique de la matrice kératinique des cornéocytes natifs et pourrait expliquer le comportement de gonflement et les propriétés mécaniques de la couche cornée des mammifères. Le modèle d'assemblage membranaire appliquéà la dynamique de la kératine et à la formation de la matrice cellulaire du stratum cornéum postule la présence dans l'espace cellulaire viable de l'épiderme d'une structure membranaire hautement dynamique présentant un petit paramètre de maille (<30 nm) et une organization en forme de cube, à laquelle la kératine est associée. D'autre part, ce modèle suggère qu'un assemblage membranaire plutôt qu'un auto-assemblage spontané puisse être à l'origine de la formation des filaments intermédiaires de kératine et de leur dynamique. Ceci concorde avec les modèles de densité cryo-électronique du cytoplasme des kératinocytes natifs et pourrait expliquer les caractéristiques du processus de formation du réseau kératinique, les propriétés dynamiques des filaments intermédiaires de kératine, l'association de la kératine avec les lipides, l'insolubilité dans les tampons non dénaturants, le polymorphisme caractéristique de la kératine assemblée in vitro, ainsi que la diminution mesurée du volume cellulaire et du niveau d'hydratation entre le stratum granulosum et le stratum corneum. [source]


"Free-Floating" Desmosomes in Lipoid Proteinosis: An Inherent Defect in Keratinocyte Adhesion?

PEDIATRIC DERMATOLOGY, Issue 1 2006
Jon A. Dyer M.D.
However, the characteristic manifestation in children , erosive, crusted lesions that lead to scarring , is rarely discussed and poorly understood. Lipoid proteinosis results from mutations in extracellular matrix protein 1, but the function of this protein is largely unknown. We performed ultrastructural studies on lesional epidermis, cultured monolayer keratinocytes, and raft keratinocyte cultures from blistering lesions of a child with lipoid proteinosis. All sections showed the dissociation of relatively intact desmosomes from keratinocytes, with desmosomes that were "free-floating" in the intercellular spaces or attached by thin strands to the cell membrane. These changes were present in serial sections of both tissue and cultured keratinocytes, suggesting this observation to be an inherent feature of keratinocytes devoid of extracellular matrix protein 1, rather than an artifact. Although additional patients should be studied, the diminished appearance of the inner dense plaque , the region of attachment of keratin intermediate filaments to desmosomal proteins , provides preliminary evidence that extracellular matrix protein 1 may participate in attaching keratin intermediate filaments to desmosomal region protein(s). [source]


Characterization and expression analysis of the hair keratin associated protein KAP26.1

BRITISH JOURNAL OF DERMATOLOGY, Issue 3 2008
M.A. Rogers
Summary Background, Human hair follicle keratin-associated proteins (KAPs) comprise a large multigene family of proteins thought to be responsible for the bundling of keratin intermediate filaments. Recently, four new KAP family members KAP24.1, KAP25.1, KAP26.1 and KAP27.1 were identified from the genome, but the expression of only one, KAP24.1, was investigated and shown in hair follicles. Objectives, In the current study, the expression of the remaining members of the family were analysed. Methods, Reverse transcriptase-polymerase chain reaction analysis of samples from numerous human organs was used. Results, Only KAP26.1 showed expression, which was limited to the hair follicle. By in situ hybridization and immunohistochemistry using a specific antiserum, KAP26.1 was localized to the differentiated portion of the hair cuticle. Conclusions, As well as KAP24.1 in hair follicles, expression of KAP26.1 was shown and is found in the differentiated part of the hair cuticle. [source]