Structural changes in trichocyte keratin intermediate filaments during keratinization.
The so-called hard alpha-keratins, such as quill and hair, have a composite structure in which intermediate filaments (IF) are embedded in a sulfur-rich matrix. Recent studies of these trichocyte keratin IF have revealed that substantial changes in the molecular architecture take place when oxidation of the cysteine residues occurs as part of the terminal differentiation/keratinization process. Recent cryoelectron microscope studies suggest that the IF has a tubular structure prior to keratinization, but transmission electron micrographs of thin sections of fully keratinized fibers exhibit a "ring-core" structure. In the present contribution we develop a generic model for the IF in the reduced state based on cross-linking studies and discuss two possibilities for the way in which this structure may be modified during the keratinization process.
Fraser
R D Bruce
RD
Institute of Fundamental Sciences, Massey University, Private Bag 11-222, Palmerston North, New Zealand.
Steinert
Peter M
PM
Parry
David A D
DA
D000818:Animals; D020285:Cryoelectron Microscopy; D003545:Cysteine / Q000378:metabolism; D004220:Disulfides; D007381:Intermediate Filament Proteins / Q000737:chemistry*; D007382:Intermediate Filaments / Q000737:chemistry / Q000648:ultrastructure*; D007633:Keratins / Q000737:chemistry* / Q000378:metabolism; D008854:Microscopy, Electron; D008954:Models, Biological; D010084:Oxidation-Reduction; D014935:Wool
D004220:Disulfides; D007381:Intermediate Filament Proteins; D007633:Keratins; D003545:Cysteine