Structural changes in trichocyte keratin intermediate filaments during keratinization

被引:20
|
作者
Fraser, RDB
Steinert, PM
Parry, DAD
机构
[1] Massey Univ, Inst FUndamental Sci, Palmerston North, New Zealand
[2] NIAMSD, Skin Biol Lab, NIH, Bethesda, MD 20892 USA
关键词
hair; surface lattice; compaction; packing; protofilaments; protofibrils; ring-core structure; keratin;
D O I
10.1016/S1047-8477(02)00636-6
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 2003 Elsevier Science (USA). All rights reserved.
引用
收藏
页码:266 / 271
页数:6
相关论文
共 50 条