Fraser R D Bruce, Parry David A D
Institute of Fundamental Sciences, Massey University, Private Bag 11-222, Palmerston North, 4442, New Zealand.
, 28 Satinay Drive, Noosa Parklands, Tewantin, Qld, 4565, Australia.
Subcell Biochem. 2017;82:131-149. doi: 10.1007/978-3-319-49674-0_5.
The intermediate filaments (IF) in trichocyte (hard α-) keratin are unique amongst the various classes of IF in having not one but two topologically-distinct structures. The first is formed at an early stage of hair development in a reducing environment within the cells in the lower part of the follicle. The second structure occurs at a later stage of hair development in the upper part of the follicle, where there is a transition to an oxidizing environment. Crosslinking studies reveal that molecular slippage occurs within the IF upon oxidation and that this results in many cysteine residues lying in near axial alignment, thereby facilitating disulphide bond formation. The disulphide bonds so formed stabilize the assembly of IF molecules and convert the keratin fibre into a tough, resilient and insoluble structure suitable for its function in vivo as a thermo-regulator and a protector of the animal against its external environment.
毛母细胞(硬α-)角蛋白中的中间丝(IF)在各类中间丝中独具特色,它并非只有一种,而是具有两种拓扑结构不同的形态。第一种形态在毛囊下部细胞内的还原环境中,于毛发发育的早期形成。第二种结构出现在毛囊上部毛发发育的后期,此时环境转变为氧化环境。交联研究表明,氧化过程中中间丝内部会发生分子滑移,这使得许多半胱氨酸残基近乎轴向排列,从而促进二硫键的形成。如此形成的二硫键稳定了中间丝分子的组装,并将角蛋白纤维转化为一种坚韧、有弹性且不溶性的结构,使其适合在体内发挥热调节作用以及保护动物免受外部环境影响的功能。