Structural Changes in Trichocyte Keratin Intermediate Filaments During Keratinization

The study investigated the structural changes in trichocyte keratin intermediate filaments (IF) during keratinization, focusing on the transition from a reduced to an oxidized state. It found that during oxidation, cysteine residues in the IF and associated proteins formed disulfide bridges, leading to significant changes in molecular packing. The research supported a model of keratin IF containing 32 chains in cross-section, arranged in eight protofilaments, and discussed the lattice transformation upon oxidation. The study concluded that the original (8 + 0) structure did not persist through the oxidation process, highlighting the dynamic nature of keratin IF during keratinization, but it was not possible to definitively choose between the (8 + 0) and (7 + 1) models based on the available evidence. Further research was needed to resolve this uncertainty.