filaggrin

Scientists hope to develop treatments for eczema through their newfound knowledge of filaggrin.

Filaggrin is essential for the regulation of epidermal homeostasis.

The protein filaggrin is believed to have an important role in holding them together as tonofibrils.

The penetrance of filaggrin mutations may be increased by household exposure to cats.

Filaggrin is a filament-associated protein that binds to keratin fibers in epithelial cells.

The gene produces the protein filaggrin, the lack of which causes dry skin and impaired skin barrier function.

Filaggrin was obtained from human epidermis and purified using reversed phase high-performance liquid chromatography.

The barrier defect seen in filaggrin null carriers also appears to lead to increased asthma susceptibility and exacerbations.

It has been shown that almost 50% of all severe cases of eczema may have at least one mutated filaggrin gene.

The citrulline rich (pro)filaggrin molecule makes an ideal substrate for detecting this reactivity.

Filaggrin monomers are tandemly clustered into a large, 350kDa protein precursor known as profilaggrin.

Within the stratum corneum, filaggrin monomers can become incorporated into the lipid envelope, which is responsible for the skin barrier function.

It is usually an autosomal dominant inherited disease (often associated with filaggrin), although a rare non-heritable version called acquired ichthyosis exists.

Filaggrin undergoes further processing in the upper stratum corneum to release free amino acids that assist in water retention.

Autoantibodies in rheumatoid arthritis recognizing an epitope of citrullinated peptides are cross-reactive with filaggrin.

Moreover, the SA antigen, which, unlike (pro)filaggrin, is detectable in rheumatoid synovium, has recently been shown to also be citrullinated.

Individuals with truncation mutations in the gene coding for filaggrin are strongly predisposed to a severe form of dry skin, ichthyosis vulgaris, and/or eczema.

Filaggrin deficiency is one of the top genome-wide genetic determinants of asthma, along with the variants found that regulate ORMDL3 expression.

Filaggrin mutations are associated with atopic eczema, and may contribute to the excessive dryness of the skin and the loss of the barrier function of normal skin.

The main epitope for these antibodies is filaggrin, and there is cross-reactivity between ACPA and anti-keratin and anti-perinuclear factor.

The type III enzyme modulates hair structural proteins, such as filaggrin in the hair follicle and trichohyalin in the inner root sheath, during hair follicle formation.

It may be possible that the filaggrin mutations and the loss of the normal skin barrier expose crevices that make it possible for Staphylococcus aureus to colonize the skin.

The disorder is believed to be caused by mutations to the gene encoding profilaggrin (a protein which is converted to filaggrin which plays a vital role in the structure of the skin).

AFA, AKA, and antiperinuclear factor (APF) have all been proposed to identify a common antigen present in the skin protein (pro)filaggrin.

Profilaggrin undergoes proteolytic processing to yield individual filaggrin monomers at the transition between the stratum granulosum and the stratum corneum, which may be facilitated by calcium-dependant enzymes.