Identification of a Rapidly Labelled 350K Histidine-Rich Protein in Neonatal Mouse Epidermis

Ramsden, Martin; Loehren, Diethard; Balmain, Allan

doi:10.1111/j.1432-0436.1982.tb01289.x

Cited by 25 publications

(14 citation statements)

References 22 publications

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“…Within this context, the initial aspects of the study were aimed to characterize further TR-PPT. The electrophoretic profile of TR-PPT on SDS gels was similar to the oligomeric series observed for the filaggrins (7,25,44). Recent studies have shown that the filaggrin oligomers are the proteolytic breakdown products of a high molecular weight precursor (25,35).…”

Section: Discussionsupporting

confidence: 64%

Trichohyalin, an intermediate filament-associated protein of the hair follicle.

Rothnagel¹,

Rogers²

1986

The Journal of Cell Biology

116

106

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Abstract.A precursor protein associated with the formation of the citrulline-containing intermediate filaments of the hair follicle has been isolated and characterized. The protein, with a molecular weight of 190,000, was isolated from sheep wool follicles and purified until it yielded a single band on a SDS polyacrylamide gel. The Mr 190,000 protein has a high content of lysine and glutamic acid/glutamine residues and is rich in arginine residues, some of which, it is postulated, undergo a side chain conversion in situ into citrulline residues. Polyclonal antibodies were raised to the purified protein, and these cross-react with similar proteins from extracts of guinea pig and human follicles and rat vibrissae inner root sheaths. Tissue immunochemical methods have localized the Mr 190,000 protein to the trichohyalin granules of the developing inner root sheath of the wool follicle. We propose that the old term trichohyalin be retained to describe this Mr 190,000 protein.Immunoelectron microscopy has located the Mr 190,000 protein to the trichohyalin granules but not to the newly synthesized filaments. This technique has revealed that trichohyalin becomes associated with the filaments at later stages of development. These results indicate a possible matrix role for trichohyalin.

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Section: Discussionsupporting

confidence: 64%

Trichohyalin, an intermediate filament-associated protein of the hair follicle.

Rothnagel¹,

Rogers²

1986

The Journal of Cell Biology

116

106

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“…EDMTFH is not homologous to mammalian filaggrin, which has also been referred to as histidine-rich protein [46]. Filaggrin is an S100 fused-type protein encoded by a gene in the mammalian EDC [47, 12].…”

Section: Discussionmentioning

confidence: 99%

Immunolocalization of a Histidine-Rich Epidermal Differentiation Protein in the Chicken Supports the Hypothesis of an Evolutionary Developmental Link between the Embryonic Subperiderm and Feather Barbs and Barbules

et al. 2016

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The morphogenesis of feathers is a complex process that depends on a tight spatiotemporal regulation of gene expression and assembly of the protein components of mature feathers. Recent comparative genomics and gene transcription studies have indicated that genes within the epidermal differentiation complex (EDC) encode numerous structural proteins of cornifying skin cells in amniotes including birds. Here, we determined the localization of one of these proteins, termed EDMTFH (Epidermal Differentiation Protein starting with a MTF motif and rich in Histidine), which belongs to a group of EDC-encoded proteins rich in aromatic amino acid residues. We raised an antibody against an EDMTFH-specific epitope and performed immunohistochemical investigations by light microscopy and immunogold labeling by electron microscopy of chicken embryos at days 14–18 of development. EDMTFH was specifically present in the subperiderm, a transient layer of the embryonic epidermis, and in barbs and barbules of feathers. In the latter, it partially localized to bundles of so-called feather beta-keratins (corneous beta-proteins, CBPs). Cells of the embryonic periderm, the epidermis proper, and the feather sheath were immunonegative for EDMTFH. The results of this study indicate that EDMTFH may contribute to the unique mechanical properties of feathers and define EDMTFH as a common marker of the subperiderm and the feather barbules. This expression pattern of EDMTFH resembles that of epidermal differentiation cysteine-rich protein (EDCRP) and feather CBPs and is in accordance with the hypothesis that a major part of the cyclically regenerating feather follicle is topologically, developmentally and evolutionarily related to the embryonic subperiderm.

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“…These granules are not membrane-bound, and they are morphologically and biochemically complex [3,8,10,12,14,191. Subsequent studies indicate that a major component of KHG is profilaggrin [5,27,28,30,32, 391, a high molecular weight and highly phosphorylated protein consisting of repeated subunits of a histidine-rich protein. Subsequent studies indicate that a major component of KHG is profilaggrin [5,27,28,30,32, 391, a high molecular weight and highly phosphorylated protein consisting of repeated subunits of a histidine-rich protein.…”

Section: Introductionmentioning

confidence: 99%

“…Brody [4] originally proposed that keratohyalin served as a source of the inter-filamentous ma-* To whom offprint requests should be sent trix protein which, together with the keratin filaments, formed the so-called "keratin pattern" in lower cornified cells. Subsequent studies indicate that a major component of KHG is profilaggrin [5,27,28,30,32, 391, a high molecular weight and highly phosphorylated protein consisting of repeated subunits of a histidine-rich protein. During later stages of epidermal differentiation, the profilaggrin is converted to filaggrin monomers via dephosphorylation and proteolytic processing.…”

Section: Introductionmentioning

confidence: 99%