“…In 1949 Smith and Parkhurst (42) presented histochemical evidence that keratohyalin was a ribonucleoprotein, and this was later confirmed by Leuchtenberger and Lund (21) . On the basis of ultrastructural studies, it has been suggested that the small particles surrounding the keratohyalin granules were ribosomes (10,37), and that keratohyalin was formed by enzymatic degradation of these ribosomes (14,15,28) . However, failure to demonstrate rapid labeling by amino acids at the 4 20 THE JOURNAL OF CELL BIOLOGY • VOLUME 49, 1971 margins of keratohyalin granules (13) suggests that the small particles are not engaged in protein synthesis.…”
Histochemical and ultrastructural studies demonstrate that keratohyalin can be mobilized from fresh specimens of cattle hoof epidermis by 1 .0 M potassium phosphate buffer (pH 7.0) .Macroaggregates with histochemical characteristics identical to those of in situ keratohyalin granules (staining by Harris' hematoxylin, Congo red, diazotized sulfanilic acid, sodium alizarin sulfonate, toluidine blue, methyl green-pyronin, and acridine orange) and with similar morphological characteristics at the ultrastructural level are formed upon dialyzing the extracted keratohyalin against distilled water . Staining by basic dyes (toluidine blue, methyl green-pyronin, and acridine orange) is abolished by treating either in situ keratohyalin granules or isolated macroaggregates with ribonuclease . Electrophoresis of isolated macroaggregates on polyacrylamide gels in the presence of sodium decylsulfate results in the fractionation of a 13 member oligomeric series of ribonucleoproteins and two nonhomologous species of ribonucleoproteins . The oligomeric series can be purified by isolating "stacked" oligomers on low concentration (3 %) polyacrylamide gels . Fractionated oligomers on polyacrylamide gels and aggregates formed from purified ribonucleoproteins demonstrate histochemical characteristics identical to those of in situ keratohyalin granules.Aggregates formed from denatured ribonucleoproteins are highly disordered and are markedly different from in situ keratohyalin granules or nondenatured isolated macroaggregates at the ultrastructural level, possibly due to irreversible denaturation of the oligomers by sodium decylsulfate .
“…In 1949 Smith and Parkhurst (42) presented histochemical evidence that keratohyalin was a ribonucleoprotein, and this was later confirmed by Leuchtenberger and Lund (21) . On the basis of ultrastructural studies, it has been suggested that the small particles surrounding the keratohyalin granules were ribosomes (10,37), and that keratohyalin was formed by enzymatic degradation of these ribosomes (14,15,28) . However, failure to demonstrate rapid labeling by amino acids at the 4 20 THE JOURNAL OF CELL BIOLOGY • VOLUME 49, 1971 margins of keratohyalin granules (13) suggests that the small particles are not engaged in protein synthesis.…”
Histochemical and ultrastructural studies demonstrate that keratohyalin can be mobilized from fresh specimens of cattle hoof epidermis by 1 .0 M potassium phosphate buffer (pH 7.0) .Macroaggregates with histochemical characteristics identical to those of in situ keratohyalin granules (staining by Harris' hematoxylin, Congo red, diazotized sulfanilic acid, sodium alizarin sulfonate, toluidine blue, methyl green-pyronin, and acridine orange) and with similar morphological characteristics at the ultrastructural level are formed upon dialyzing the extracted keratohyalin against distilled water . Staining by basic dyes (toluidine blue, methyl green-pyronin, and acridine orange) is abolished by treating either in situ keratohyalin granules or isolated macroaggregates with ribonuclease . Electrophoresis of isolated macroaggregates on polyacrylamide gels in the presence of sodium decylsulfate results in the fractionation of a 13 member oligomeric series of ribonucleoproteins and two nonhomologous species of ribonucleoproteins . The oligomeric series can be purified by isolating "stacked" oligomers on low concentration (3 %) polyacrylamide gels . Fractionated oligomers on polyacrylamide gels and aggregates formed from purified ribonucleoproteins demonstrate histochemical characteristics identical to those of in situ keratohyalin granules.Aggregates formed from denatured ribonucleoproteins are highly disordered and are markedly different from in situ keratohyalin granules or nondenatured isolated macroaggregates at the ultrastructural level, possibly due to irreversible denaturation of the oligomers by sodium decylsulfate .
“…Iti this regard it is appropriate to point out that detise homogeneous deposits resembling portions of cytoplasmic keratohyaliti granules have been shown to exist in the nucleus (Fukuyama et al 1972). In fact, several investigators have suggested a nuclear and/or a cytoplasmic origin of keratohyalin granules (Sognnaes & Albright 1958, Oehmke & Petri 1964, lessen 1970, Squier & Meyer 1971.…”
The keratohyalin granules from 25 human oral leukoplakias, showing benign hyperorthokeratosis histologically, were examined employing a series of histochemical techniques. The tissues were fixed in 10% neutral buffered formalin, 80% methanol, or Carnoy's fluid. The keratohyalin granules stained intensely with Pauly's reagent, Congo red and Harris hematoxylin, indicating the presence of proteins. This was confirmed by abolishing the staining reaction by pretreatment with proteolytic enzymes. The keratohyalin granules also reacted with methyl green‐pyronin by staining pink at their peripheries; this staining was abolished by pretreatment with ribonuclease, indicating the presence of ribo‐nucleotides. The keratohyalin granules partially stained with toluidine blue and colloidal iron, indicating the presence of acidic polysaccharides. The keratohyalin granules did not react with the Feulgen reagent, suggesting the absence of DNA. Our studies indicate that the keratohyalin granules in human oral leukoplakia are primarily protein(s) complexed with polyribonucleotides. The presence of a carbohydrate moiety suggests the possibility of a protein‐polysaccharide component in the granules.
“…Although the DNA content is gradually decreased (Pelc, 1959;Alavaikko, 1971;Suzuki et al, 1977), synthesis of RNA continues as long as nucleoli are visible and protein synthesis unique to differentiating epidermal cells takes place in the nuclei (Fukuyama and Epstein, 1972) and cytoplasm (Fukuyama et al, 1965). Ultrastructural observations (Sognnaes and Albright, 1956;Oemke and Petry, 1964) and radiolabeling of synthesized proteins in the nuclei Epstein, 1972,1975) suggested that some proteins remain in the nucleus while others transfer into the cytoplasm. However, biochemical properties and the fate of these nuclear proteins in terminally differentiated cornified cells devoid of nucleic acids are not yet known.…”
Both DNA and RNA disappear from the nucleus during differentiation of granular cells into cornified cells but the fate of nuclear proteins remains unknown. We investigated localization of nuclear proteins in rat epidermis by light and electron microscopic immunoperoxidase techniques. As a probe, three sera that reacted, respectively, with the nucleoplasm, nucleolus, and nuclear envelope of basal cells of rat epidermis were used. In granular cells both the antinucleoplasm serum and antinucleolus serum increased intensity of the nuclear staining, but they reacted also with ribosomes, filaments, and periphery of keratohyalin granules in the cytoplasm. The staining appeared diffusely in cornified cells and identification of nuclear components became impossible. In contrast, the antinuclear envelope serum stained only the nuclear outline in granular cells and continued to stain the nuclear contour in cornified cells of the fourth and fifth proximal cell layers. The antigenic components surrounded amorphous but not filamentous materials in cornified cells. These findings suggest that some nuclear proteins become immunologically indistinguishable from cytoplasmic protein. However, the nuclear envelope protein maintains its localization even after nucleic acids are lost and the nuclear space is detectable in cornified cells by use of autoantibody directed to this protein(s).
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