Egelrud T, Lundström A.
DOI: 10.2340/0001555569105110

Precursor-product relationships among keratin polypeptides (cytokeratins) were studied in living and cornified layers of palmar-plantar epidermis. Serial 10 microns horizontal freeze-cut sections of punch biopsies were analysed by means of light microscopy and one-dimensional electrophoresis in a system that permitted identification of all major keratin polypeptides with apparent molecular weights over 60 kDa. Peptides that appeared to be related were compared by means of peptide mapping after partial proteolysis. The results suggest that both the basic-neutral (type II) cytokeratin no. 1 and the acidic (type I) cytokeratin no. 9 undergo two distinct modification steps with subsequent decreases in apparent molecular weight during keratinization. For both polypeptides the first modification appeared to take place and run to completion in close relation to the transition between the uppermost living epidermal layers and the lowest cornified layers. The second conversions of cytokeratins nos. 1 and 9 both appeared to take place within the stratum corneum but differed in two respects: 1) they appeared to start at different tissue sites; 2) whereas the second modification step appeared to comprise all cytokeratin 1 molecules, only a fraction of the cytokeratin 9 molecules passed through this step. These variations suggest that the different modification steps may be produced by different mechanisms that are regulated separately. It is concluded that the processing of cytokeratins during keratinization may be more complex than has previously been realized.