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• White noise semi truck
• Hair Restore Ultra Scalp Solution
• Cadherin 23 and protocadherin 15 interact to form tip-link filaments in sensory hair cells
• Keratoderma with woolly hair
• Clinical spectrum of woolly hair: indications for cerebral involvement
• Cardiocutaneous Syndrome: The Tale between Heart and Skin
• 6v6 tube equivalent
• Human hair growth

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White noise semi truck

Owens, N. Wilson, A. Hill, E. Rugg, R. Porter, A. Hutcheson, R. Quinlan, D. Parkes, D. Jewell, S. Campbell, S. Ghosh, J. Satsangi, E. Lane; Human keratin 8 mutations that disturb filament assembly observed in inflammatory bowel disease patients. J Cell Sci 15 April ; 10 : — We have identified miss-sense mutations in keratin 8 in a subset of patients with inflammatory bowel disease Crohn disease and ulcerative colitis. Inflammatory bowel diseases are a group of disorders that are polygenic in origin and involve intestinal epithelial breakdown.

We investigated the possibility that these keratin mutations might contribute to the course of the disease by adversely affecting the keratin filament network that provides mechanical support to cells in epithelia.

The G62C mutation also gives rise to homodimer formation on oxidative stress to cultured intestinal epithelial cells, and homodimers are known to be polymerization incompetent. Impaired keratin assembly resulting from the K8 mutations found in some inflammatory bowel disease patients would be predicted to affect the maintenance and re-establishment of mechanical resilience in vivo, as required during keratin cytoskeleton remodeling in cell division and differentiation, which may lead to epithelial fragility in the gut.

Simple epithelial keratins may thus be considered as candidates for genes contributing to a risk of inflammatory bowel disease. The keratins are a family of structural proteins that form the intermediate filaments of the cytoskeleton in epithelial cells. At least 49 keratin genes are present in humans Hesse et al. Each keratin pair has a specific and characteristic tissue distribution pattern.

Human hereditary skin disorders caused by mutations in keratin genes have shown that keratin intermediate filaments in stratified squamous epithelia provide vital mechanical resilience to the keratinocytes, without which the epithelium breaks down under physical stress reviewed by Corden and McLean, Mutations in keratins K5 type II or K14 type I , synthesized in the basal cell layer of the epidermis, cause epidermolysis bullosa simplex EBS , a condition characterized by basal cell cytolysis and epidermal blistering in response to mild physical trauma.

Similar mutations in other differentiation-specific keratins result in a range of very different clinical phenotypes, depending on which subpopulation of cells in the tissue uses the mutated keratin for its structural resilience reviewed by Irvine and McLean, Compared with the epidermal keratins, there is less evidence to date for human pathogenic mutations in K8 or K18, the major keratins of simple epithelia.

The absence of functional K8 or K18 predisposes mice to hepatotoxic damage Magin et al. Mutations in human K8 and K18 genes may contribute to disorders of internal systems without this being readily apparent, because early lesions caused by cell fragility in internal simple epithelia would not be visible.

We reasoned that even if cell fragility was involved in gut disorders, the lack of access and visibility of the gut epithelium would mean that primary pathology might go undetected. An internal epithelial fragility disorder might not present clinically until secondary effects had become established such as a dysregulated immune response to entry of gut lumen antigens into the intestinal wall , and the tissue damage had become so extensive as to obscure the primary cause.

A candidate group of gut disorders for simple epithelial keratin involvement is that of the inflammatory bowel diseases IBD. IBD is a heterogeneous group of disorders of poorly understood aetiology affecting individuals per , in the United Kingdom Rubin et al. It is characterized by an ill-defined increase in intestinal permeability and an abnormal inflammatory response, with a polygenic determination of the disease type and severity.

The two main forms are Crohn disease Crohn's disease, OMIM and ulcerative colitis, and the quest to identify the genes responsible for these disorders has been ongoing for some time. Genetic linkage with IBD has been reported for loci on chromosomes 3, 5, 6, 7, 12, 14, 16 and 19 Hugot et al.

This gene encodes a receptor for a common peptidoglycan motif on all bacteria, the muramyl dipeptide Girardin et al. The linkage of inflammatory bowel disorders to multiple genetic loci indicates that there are likely to be many susceptibility genes involved, either contributing to molecularly distinct subsets of IBD that cannot be separately identified clinically, or perhaps contributing in different combinations to cause the same disease. Any single genetic change is therefore unlikely to be present at a very high frequency in patients with inflammatory bowel disorder and may also be detected in healthy controls.

These considerations make the problem of identification and analysis of causative mutations especially difficult. We found sequence variations in the K8 gene in both ulcerative colitis and Crohn disease patients, and we present experimental evidence that these mutations have significant effects on keratin filament assembly.

The data suggest that these mutations have the potential to compromise cytoskeleton function in the intestinal epithelium in vivo. By analogy with the effects of mutations in skin keratins, the K8 mutations may render intestinal epithelia fragile, providing a mechanism whereby keratins may be one of the genetic factors which, in some patients, predispose them towards inflammatory bowel disorders.

Bishr Omary Stanford University. Keratins were expressed and purified as described previously Porter et al. Efficiency of assembly was assessed by sedimentation assay Nicholl and Quinlan, The assembly mixture was layered onto 0.

SW cells human colorectal adenocarcinoma stably expressing FLAG-tagged K8 G62C were derived from single cell clones after selection of transfected cells with 0. Bound antibody was detected by enhanced chemiluminescence. The complete coding regions of the keratin 8 K8 and keratin 18 K18 genes, KRT8 and KRT18 , respectively, were sequenced from genomic DNA samples collected from 50 sporadic and 47 familial inflammatory bowel disorder patients.

A total of 57 patients were diagnosed as having Crohn disease, 32 as having ulcerative colitis and 8 as having indeterminate colitis. Heterozygous miss-sense mutations in keratin K8 were found in five unrelated inflammatory bowel disease patients 5.

In one familial incidence, the K8 G62C proband's UC-affected sister also expressed the mutation, as did the brother who had symptoms of colitis but had not been formally diagnosed. This mutation lies in the non-helical head domain of the keratin protein, in subdomain H1, and is homologous to the K8 Gly61 to Cys mutation reported in liver disease patients Ku et al. A third mutation leading to an amino acid substitution at K8 Lys to Asn in the tail domain was found in an ulcerative colitis patient with a family history of IBD Fig.

One heterozygous KRT18 sequence variant of potential interest was identified in four patients Fig. The positions of the sequence variants in the protein are shown in Fig. None of them are in the major hotspot cluster sites associated with severe disease in epidermal keratins.

Instead, they lie within the non-helical domains, which in the skin keratins are usually associated with milder forms of disease Letai et al. Detection of K8 and K18 sequence variations in inflammatory bowel disease patients. E Positions of the amino acid substitutions in the K8 and K18 proteins. The helical domains are represented by boxes shaded regions are hotspots for mutations causing severe disease in epidermal keratins and the non-helical domains are represented by the solid line.

Solid red triangles represent familial ulcerative colitis, solid green triangles represent familial Crohn disease and open green triangles represent sporadic Crohn disease. With the known polygenic etiology of IBD, a population incidence of 1 in and a typical pattern of onset in young adulthood, one would predict that predisposing but asymptomatic genetic changes should be found in some unaffected individuals, particularly in young ones.

When unaffected control samples were screened by direct sequencing for the presence of keratin mutations, the K8 KN mutation was not found in control alleles, but the K8 G62C and K8 I63V sequences were each detected once, the latter in a young individual.

These individuals may be presymptomatic for IBD, or for cirrhosis of the liver Ku et al. The K18 ST variant was detected altogether in 4 out of alleles and may therefore be a polymorphism rather than a mutation. With this degree of complexity in the system, statistical analysis on this sample size is not informative.

Tissue samples could not be obtained from these patients, and in any case they may not have shown much morphological change in the cytoplasmic keratin filaments.

These mutations occurred outside the helix boundary motifs, and from studies of mutations in skin keratins, it is only the rod end hotspot mutations that have been associated with any obvious keratin dysmorphism in situ.

We therefore focused our analysis of the potential pathogenicity of these mutations on their impact on the keratin cytoskeleton in vitro.

We initially assessed the assembly potential of IBD mutant versus wild-type recombinant K8 with wild-type recombinant K18 using sedimentation assays and electron microscopy of negatively stained filament preparations as previously used to show deficiencies in keratins with EBS mutations Coulombe et al.

Recombinant proteins produced in bacteria were purified Fig. However, none of the K8 mutants assembled as efficiently with wild-type K18 as did wild-type K8; much of the protein remained in the supernatant and a smaller proportion was recovered in the pellet. In vitro filament assembly properties of variant keratins. A SDS polyacrylamide gel electrophoresis plus Coomassie Blue staining to show left to right molecular weight markers Mr in kDa as indicated , recombinant K8 wt and K18 wt , respectively.

K8 wt and K18 wt readily assemble into pelletable polymers, whereas the mutant K8 forms smaller amounts of pelleted material in the sedimentation assay. D Electron micrograph showing long, uniform filaments formed by in vitro polymerization of K8 wt with K18 wt.

Bars, nm. By contrast, polymerization with mutant K8 produced shorter filaments of less uniform diameter; these filaments were less straight, made sharper bends and showed fewer lateral associations than the wild-type filaments Fig. More aggregates and short fragments were invariably present, indicating that the polymerization efficiency of these proteins is impaired. In combination with wild-type K8, the K18 ST variant produced filaments more similar to wild-type Kbased filaments Fig.

Because the in vitro analyses described above do not discriminate between the different stages of keratin filament assembly, we sought to determine the effects of the sequence variants on the first stage of assembly, i. Surface plasmon resonance analysis was undertaken with recombinant wild-type K8 or K18 covalently bound to the sensor chip and exposed to recombinant K18 or K8 solutions, respectively, flowing across the chip under reducing conditions.

The optical detection system read-out depends on the mass of protein bound to the chip Fig. No dissociation of any of the keratin-keratin interactions was observed within the 5 minute wash period, reflecting the high affinity of type I-type II keratin interactions.

Once formed, all K8-K18 interactions were stable as shown by the persistent plateau through the wash period. The other two sequence variants revealed differences between defects seen in dimerization rates this assay and in their ultimate efficiency of filament formation see above. Binding of K8 I63V to K18 was not significantly different from wild-type K8 under these conditions, although in vitro assembly over a longer timecourse had shown abnormalities by electron microscopy.

The different behaviour of individual sequence variants in the different assays probably reflects the different stage in hierarchical protein folding and filament assembly at which the conformational effect of the mutation has most impact. These experiments indicate that mutant keratins K8 G62C , K8 KN , and to a lesser extent K18 ST , are inherently abnormal in the process of assembling heterodimers in this assay system.

Yet although the mutations affect the rate at which heterodimers initially form, they do not weaken the affinity between subunits once they are assembled into heterodimers as there is no dissociation of any of them during the wash period.

We carried out transient transfection studies to determine whether the keratin sequence variants also perturbed filament assembly and organization in the cellular environment. Intermediate filament proteins with substantial deletions and disruptive mutations can still become incorporated into a pre-existing cytoplasmic filament network for example, see Lu et al. SW13 adrenal cortex adenocarcinoma cells are reported to contain no cytoplasmic intermediate filaments Hedberg and Chen, and so were used for these experiments.

SW13 cells were cotransfected with constructs expressing wild-type or variant K8, together with wild-type or variant K18, then fixed at intervals after transfection and the keratin visualized by immunofluorescence Fig. The other keratin variants were less obviously different from wild type not shown. By late timepoints hours the wild-type keratins were unchanged, while the keratin involving K8 G62C was nearly all in the form of filamentous fragments with infrequent aggregates Fig.

This experiment supports the interpretation that K8 G62C is clearly a disruptive variant, but that filament assembly is still only impaired by this mutation rather than prevented.

Hair Restore Ultra Scalp Solution

Review Series Free access Fax: ; E-mail: mbishr umich. Find articles by Omary, M. Published July 1, - More info.

Cadherin 23 and protocadherin 15 interact to form tip-link filaments in sensory hair cells

A, A typical trichogram showing almost only dystrophic anagen hairs. B, Detail showing ruffled cuticles and distorted bulbs. Pedigrees of families 2, 3, and 7 who are affected by loose anagen hair syndrome. DNA samples were obtained from all individuals. Black symbols indicate clinically affected members of the families; gray symbols, individuals who are clinically not affected but carry the K6HF EK mutation; and open symbols, individuals who are not clinically affected and who do not carry the mutation. A patient with partial diffuse woolly hair. A, Clinical features showing a mixture of curly and straight hairs. B, Polarizing microscopy: torsion of a hair shaft in a woolly hair.

Keratoderma with woolly hair

Proteins of the intermediate filament IF supergene family are ubiquitous structural components that comprise, in a cell type—specific manner, the cytoskeleton proper in animal tissues. IF proteins are highly charged, thus representing versatile polyampholytes with multiple functions. Taking vimentin, keratins, and the nuclear lamins as our prime examples, we present an overview of their molecular and structural parameters. These, in turn, document the ability of IF proteins to form distinct, highly diverse supramolecular assemblies and biomaterials found, for example, at the inner nuclear membrane, throughout the cytoplasm, and in highly complex extracellular appendages, such as hair and nails, of vertebrate organisms.

Clinical spectrum of woolly hair: indications for cerebral involvement

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Cardiocutaneous Syndrome: The Tale between Heart and Skin

Wilson-Kubalek [1]; Ronald A. Hair cells of the inner ear are mechanosensors that transduce mechanical forces arising from sound waves and head movement into electrochemical signals to provide our sense of hearing and balance. Each hair cell contains at the apical surface a bundle of stereocilia. Mechanoelectrical transduction takes place close to the tips of stereocilia in proximity to extracellular tip-link filaments that connect the stereocilia and are thought to gate the mechanoelectrical transduction channel [1, 2, 3]. Recent reports on the composition [4, 5, 6, 7, 8], properties and function [9, 10, 11] of tip links are conflicting [29]. Here we demonstrate that two cadherins that are linked to inherited forms of deafness in humans [12, 13, 14, 15] interact to form tip links.

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Plectin is a large, kDa, intermediate filament IF -associated protein. It acts as a cytoskeletal crosslinker and signaling scaffold, affecting mechanical as well as dynamic properties of the cytoskeleton. As a member of the plakin family of cytolinker proteins, plectin has a multidomain structure that is responsible for its vast binding portfolio. It not only binds to all types of IFs, actin filaments and microtubules, but also to transmembrane receptors, proteins of the subplasma membrane protein skeleton, components of the nuclear envelope, and several kinases with known roles in migration, proliferation, and energy metabolism of cells.

Human hair growth

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Italian Journal of Pediatrics volume 43 , Article number: 99 Cite this article. Metrics details. Woolly Hair is an uncommon congenital anomaly of the scalp hair presenting with strongly coiled hair involving a localized area of the scalp or covering the entire side and occurring in non-black people. On the contrary, the generalized type may be related to disorders and syndromes affecting heart, cutis, liver and gastrointestinal organs. To our knowledge, no cases of wooly hair syndromes has been associated to neurologic involvement.

Reply to this Discussion! Login or Sign Up. I recently just bought a fluorescent lowell rifa kit and am looking to expand my kit with a hair light and backlight. Since my key and fill lights are fluorescent I would need my hair and backlight to be fluorescent as well right? If so, do you have any recommendations? I am mostly shooting 1 person talking head interviews and just need to bring my subject out from the background.

Keratoderma with woolly hair is a group of related conditions that affect the skin and hair and in many cases increase the risk of potentially life-threatening heart problems. People with these conditions have hair that is unusually coarse, dry, fine, and tightly curled. In some cases, the hair is also sparse. The woolly hair texture typically affects only scalp hair and is present from birth.