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- W2014130010 abstract "Ultrathin sections of epidermis embedded in Epon were subjected to enzymatic digestion according to the method of Monneron and Bernhard (37). Tonofilaments were digested by pronase, trypsin, and pepsin. Perinuclear tonofilaments were more easily digested than filaments associated with desmosomes, and so were tonofilaments of the upper epidermal layers as compared to filaments of basal cells. The proteases, particularly pronase, almost selectively removed the attachment plaques of desmosomes, and this facilitated the recognition of the interrelationship of the individual desmosomal components. Keratohyalin granules were digested by the proteases, by ribonuclease and phospholipase C. Pronase and trypsin digested the interior of horny cells while pepsin only reduced the stainability of the matrix. All proteases digested the shell of condensed cytoplasm subjacent to the cell membrane, which was shown to possess a unit membrane structure. These findings support the contention that the “thickening” of the cell membranes in the stratum corneum is not the result of the addition of material from the outside, but is due rather to the deposition of protein material on the cytoplasmic side of the membranes. Lipid droplets and proteinaceous inclusions were identified by their sensitivity to phospholipase and the proteases, respectively. Ribosomes were digested by RNase after having been exposed to pronase. The method employed in this study permits the recognition of the general chemical nature of keratinocyte constituents and of the chemical differences between morphologically distinct cell components. The differential digestion effects unmask substructures which are not revealed by conventional electron microscopy." @default.
- W2014130010 created "2016-06-24" @default.
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- W2014130010 date "1971-08-01" @default.
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- W2014130010 title "Differential enzymatic digestion of cytoplasmic components of keratinocytes: Electron microscopic observations" @default.
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- W2014130010 doi "https://doi.org/10.1016/s0022-5320(71)80116-8" @default.
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