Variation and frequency of cytokeratin polypeptide patterns in human squamous non-keratinizing epithelium

Abstract

The squamous non-keratinizing epithelium of the human upper digestive tract was analyzed for keratin-like cytoskeletal proteins (cytokeratins) by both high resolution one- and two-dimensional gel electrophoresis. The Triton/high salt-insoluble portion of pure epithelial homogenates contains a number of SDS- and urea-extractable polypeptides, whose two-dimensional gel pattern (NEpHG/SDS) typically represents a defined subset of human cytokeratins. The cytoskeletal preparations of epithelial tissue samples obtained from different individuals were found to be uniform with respect to their content of cytokeratin polypeptides 55.0 kD/basic, 52.0 kD/acidic, and 49.0 kD/acidic. However, we have observed that four basic members of apparent molecular weight 60.0, 59.0, 56.5, and 56.0 kD occur at an inconstant rate. Consequently, the cytokeratin polypeptide patterns appeared highly variable as a result of the presence of constant plus compositionally different subsets of inconstant members. From the analysis of cytoskeletal portions of more than 300 individual tissue samples we demonstrate eight different keratin-like polypeptide patterns including their frequencies and propose the existence of no more than nine. These, most probably, encompass all the possible inter-individual variations to which the cytokeratins of this type of epithelium will combine for forming intermediate-sized filaments in vivo. We furthermore hypothesize that the observed variation of cytokeratin patterns may reflect a polymorphism of genes coding for the variable keratin-like polypeptide members.