Isolation of Intermediate Filament Assemblies from Human Hair Follicles
October 1985
in “
The Journal of Cell Biology
”
intermediate filament assemblies human hair follicles alpha-keratin para-like filament ortho-like filament hexagonally packed spiral filament whorl filament axial banding patterns lattice structure interfilamentous bridges low-sulfur proteins hard mammalian keratins filament-matrix framework hard keratin appendages hair follicles keratin filament protein
TLDR Researchers isolated and identified structural components of human hair follicles, providing a model for studying hair formation.
Researchers isolated hard alpha-keratin structural components from developing human hair follicle cells. Electron microscopy revealed individual alpha-keratin filaments and tactoid-like filament assemblies organized along subfibrillar arms of macrofibrils. These assemblies, averaging 47 nm in width, were composed of closely packed alpha-keratin filaments and exhibited two types: para-like (hexagonally packed) and ortho-like (spiral or whorl type). Axial banding patterns, with periods of 20-22 nm, suggested a lattice structure with interfilamentous bridges. Preliminary biochemical studies indicated that these filaments consist of low-sulfur proteins common in hard mammalian keratins. This isolation provided a new structural entity for studying the assembly mechanisms of the filament-matrix framework in hard mammalian keratin appendages.
