Different polypeptides form the intermediate filaments in bovine hoof and esophageal epithelium and in aortic endothelium.
Polypeptides that form 10-nm filaments in vitro were isolated from three different bovine tissues: the viable portion of the hoof epithelium, the epithelium of the esophagus, and cultured endothelial cells derived from aorta. The seven polypeptides from hoof, the two from esophagus, and the one from endothelial cells were different with respect to mobility in SDS polyacrylamide gels and/or limited proteolytic digestion. Peptide maps of the different filament-forming polypeptides (FFP's) showed that none of the smaller FFP's was a fragment of any of the larger FFP's. Several isomobile fragments were found in the peptide maps of different FFP's, suggesting that they might contain regions of amino acid sequence homology. We present a hypothesis that suggests how the different 10-nm filament-forming proteins may be related.
D000595:Amino Acid Sequence; D000818:Animals; D001011:Aorta / Q000648:ultrastructure*; D002417:Cattle; D003599:Cytoskeleton / Q000032:analysis*; D004727:Endothelium / Q000648:ultrastructure; D004848:Epithelium / Q000648:ultrastructure; D004947:Esophagus / Q000648:ultrastructure*; D006724:Hoof and Claw / Q000648:ultrastructure*; D008970:Molecular Weight; D010455:Peptides / Q000032:analysis*
D010455:Peptides