The presumption of proteolytic enzymes related to the formation of intermediates during the terminal differentiation.
The [14C]Gly-labelled keratin polypeptides extracted with 1% SDS and 10 mM DTT were made to undergo changes with an enzyme fraction (ammonium sulfate, 50-75% saturated fraction) prepared from a human epidermis in the presence of 1% Triton X-100. In particular, 69-67 kDa peptides were considerably decreased with the above enzyme fraction in the time course experiments, and the components strongly bound to the cell membrane had little effect on the above reaction. In addition, in the case of the [14C]Gly-labelled keratin filament assembly, 69 and 62 kDa peptides were decreased and 55, 52 and 50 kDa peptides were increased with the same enzyme fraction in the time course experiments. From these results, we estimated that the proteolytic enzyme(s) may exist in the human epidermis, and may be processed to keratin intermediates from prekeratin during the initial stage of terminal differentiation in the human epidermis.
D002454:Cell Differentiation; D004229:Dithiothreitol; D004591:Electrophoresis, Polyacrylamide Gel; D000078404:Epidermal Cells; D004817:Epidermis / Q000201:enzymology; D005590:Fractional Precipitation; D006801:Humans; D007381:Intermediate Filament Proteins; D007633:Keratins / Q000378:metabolism*; D007700:Kinetics; D010447:Peptide Hydrolases / Q000378:metabolism*; D011498:Protein Precursors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational
D007381:Intermediate Filament Proteins; D011498:Protein Precursors; C004818:prekeratin; D007633:Keratins; D010447:Peptide Hydrolases; D004229:Dithiothreitol