Fine fibrillar structure of apical zone on inner ear receptor cells in guinea pig has been investigated using several fixation methods under transmission electron microscopy (TEM).
1) The structure of hair rootlets and cuticular plates has been observed as almost dense and homogenous material using the ordinary glutaraldehyde-osmium fixation method. The original structure was concealed and unobvious because of selectively destructive effect of the fixatives.
2) The finer structure was revealed by using tannic acid fixation, and modified glutaraldehyde-osmium fixation method which was developed to preserve actin filaments during preparation. These methods enabled to visualize those fibrillar structure in greater detail under TEM.
3) The structure of hair rootlet was proved to be composed of actin paracrystal or its near form. The width of actin filament in hair rootlet was 83 Å and a pitch of the double helix was 2×(332-388) Å. Cross-sectioned actin filaments in hair rootlet were arranged in extremely regular pattern (hexagon) and were chained to one another by smaller filaments (10 Å in diameter). About 80 Å-diametered filaments radiated from paracrystal structure into the lighter zone surrounding each rootlet. Hair rootlet was suspected to have a variable elasticity or flexibility induced by polymorphism of actin. This system may be initiated by mechanical stimuli and controled automatically.
4) Individual filaments (ca. 80Å in diameter) in sensory hair and cuticular plate were also composed of actin filaments. In the cuticular plate fibrillar structure was enhanced by using EDTA (Ca
+ chelating agent) as pre-treatment before tannic acid fixation procedure. There were filaments surrounding lighter zone and connecting rootlets each other, to the cuticular plate filaments and to the tight junction between the supporting cell. Paracrystal structure in hair rootlet was not affected.
5) Actin filaments in hair rootlet and cuticular plate may have a different regulatory protein each other.
6) The dense material was connecting each sensory hair in a characteristic form. The material was suspected to be composed of glycoprotein.
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