Interaction of filaggrin with keratin filaments during advanced stages of normal human epidermal differentiation and in Ichthyosis vulgaris

Manabe, Motomu; Sanchez, Miguel; Sun, Tung‐Tien; Dale, Beverly A.

doi:10.1111/j.1432-0436.1991.tb00241.x

Cited by 114 publications

(99 citation statements)

References 42 publications

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“…Double-labeling experiments revealed that caspase-14 and involucrin are present at the same sites in these cells. Because previous reports have shown that loricrin and other minor proteins destined to form the cornified envelope co-localize with involucrin (Warhol et al 1985;Steven et al 1990;Manabe et al 1991;Ishida-Yamamoto et al 1996Presland et al 1997; Ishida-Yamamoto and Iizuka 1998), our findings suggest that all these components of keratohyalin are potential substrates for caspase-14. By contrast, the weak labeling intensity of F-granules suggests that filaggrin and its binding partners are less likely candidates.…”

Section: Discussionmentioning

confidence: 78%

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Ultrastructural Localization of Caspase-14 in Human Epidermis

Alibardi

Dockal

Reinisch

et al. 2004

J Histochem Cytochem.

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Caspase-14 has been implicated in the formation of stratum corneum because of its specific expression and activation in terminally differentiating keratinocytes. However, its precise physiological role and its protein substrate are elusive. We studied the ultrastructural localization of caspase-14 in human epidermis to compare its distribution pattern with that of well-characterized differentiation markers. Immunogold cytochemistry confirmed that caspase-14 is nearly absent in basal and spinous layers. In the granular, layer nuclei and keratohyalin granules were labeled with increasing intensity towards the transitional layer. Particularly strong caspase-14 labeling was associated with areas known to be occupied by involucrin and loricrin, whereas F-granules, occupied by profilaggrin/filaggrin, were much less labeled. A high density of gold particles was also present at the forming cornified cell envelope, including desmosomes. In corneocytes, intense labeling was both cytoplasmic and associated with nuclear remnants and corneodesmosomes. These observations will allow focusing efforts of biochemical substrate screening on a subset of proteins localizing to distinct compartments of terminally differentiated keratinocytes.

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Section: Discussionmentioning

confidence: 78%

“…Profilaggrin, a histidin-rich protein that aggregates keratins, is present in F-granules of composite keratohyalin (Fukuyama and Epstein 1986;Holbrook 1989;Steven et al 1990;Manabe et al 1991). F-granules have been described for both rodents and human keratohyalin (Yoneda et al 1992;Ishida-Yamamoto et al 1993).…”

mentioning

confidence: 99%

Ultrastructural Localization of Caspase-14 in Human Epidermis

Alibardi

Dockal

Reinisch

et al. 2004

J Histochem Cytochem.

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“…(3) Profilaggrin/Filaggrin Filaggrin is an abundant protein expressed in differentiating keratinocytes that functions to aggregate keratin IFs into tightly aligned bundles or macrofibrils in the stratum corneum of the epidermis and other stratified keratinizing epithelia, including the gingiva and tongue (Dale et al, 1978;Manabe et al, 1991;reviewed in Dale et al, 1990breviewed in Dale et al, , 1993. It is synthesized in suprabasal granular cells, as a large, highly phosphorylated precursor, profilaggrin, that consists of multiple filaggrin repeats flanked by N-and C-terminal domains that differ from filaggrin.…”

Section: (B) Skin Disorders Associated With Keratin Mutationsmentioning

confidence: 99%

“…In mouse epidermis, loricrin is initially expressed in granular cells and forms keratohyalin granules termed Lgranules that are morphologically distinct from profilaggrin-containing F-keratohyalin (Steven et al, 1990;Manabe et al, 1991;Dale et al, 1994). In human epithelia, loricrin does not localize to L-granules except in newborn foreskin epidermis and acrosyringium (the epidermis surrounding sweat ducts) (Ishida-Yamamoto et al, 1993.…”

Section: (4) Trichohyalinmentioning

confidence: 99%

Epithelial Structural Proteins of the Skin and Oral Cavity: Function in Health and Disease

Presland

Dale

2000

Critical Reviews in Oral Biology & Medicine

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350

328

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Epithelial tissues function to protect the organism from physical, chemical, and microbial damage and are essential for survival. To perform this role, epithelial keratinocytes undergo a well-defined differentiation program that results in the expression of structural proteins which maintain the integrity of epithelial tissues and function as a protective barrier. This review focuses on structural proteins of the epidermis and oral mucosa. Keratin proteins comprise the predominant cytoskeletal component of these epithelia. Keratin filaments are attached to the plasma membrane via desmosomes, and together these structural components form a threedimensional array within the cytoplasm of epithelial cells and tissues. Desmosomes contain two types of transmembrane proteins, the desmogleins and desmocollins, that are members of the cadherin family. The desmosomal cadherins are linked to the keratin cytoskeleton via several cytoplasmic plaque proteins, including desmoplakin and plakoglobin (-y-catenin). Epidermal and oral keratinocytes express additional differentiation markers, including filaggrin and trichohyalin, that associate with the keratin cytoskeleton during terminal differentiation, and proteins such as loricrin, small proline-rich proteins, and involucrin, that are cross-linked into the cornified envelope by transglutaminase enzymes. The importance of these cellular structures is highlighted by the large numbers of genetic and acquired (autoimmune) human disorders that involve mutations in, or autoantibodies to, keratins and desmosomal and cornified envelope proteins. While much progress has been made in the identification of the structural proteins and enzymes involved in epithelial differentiation, regulation of this process is less clear. Both calcium and retinoids influence epithelial differentiation by altering the transcription of target genes and by regulating activity of enzymes critical in epithelial differentiation, such as transglutaminases proteinases, and protein kinases. These studies have furthered our understanding of how epithelial tissue and cell integrity is maintained and provide a basis for the future treatment of skin and oral disorders by gene therapy and other novel therapeutics.

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“…Ichthyosis vulgaris (IV) is a heterogeneous autosomal skin disease characterized by dry and scaly skin, mild hyperkeratosis, and a decreased or absent granular layer that either lacks, or contains morphologically abnormal, keratohyalin granules (Manabe, et al, 1991). Several lines of evidences point to a genetic defect in a gene encoding FLG in IV.…”

Section: Flaky Tail Mouse and Ichtyosis Vulgarismentioning

confidence: 99%