Fraser R D Bruce, Steinert Peter M, Parry David A D
Institute of Fundamental Sciences, Massey University, Private Bag 11-222, Palmerston North, New Zealand.
J Struct Biol. 2003 May;142(2):266-71. doi: 10.1016/s1047-8477(02)00636-6.
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.
所谓的硬α-角蛋白,如羽毛和毛发,具有一种复合结构,其中中间丝(IF)嵌入富含硫的基质中。最近对这些毛细胞角蛋白中间丝的研究表明,当半胱氨酸残基氧化作为终末分化/角质化过程的一部分发生时,分子结构会发生显著变化。最近的冷冻电子显微镜研究表明,中间丝在角质化之前具有管状结构,但完全角质化纤维薄片的透射电子显微照片显示出“环芯”结构。在本论文中,我们基于交联研究开发了一种还原状态下中间丝的通用模型,并讨论了这种结构在角质化过程中可能被修饰的两种方式。