The structure of the basal labyrinth in kidney cells of freshwater sticklebacks was studied in ultrathin sections (after fixation with permanganate, osmium tetroxide, and combinations of glutaraldehyde with osmium tetroxide) and in freeze-etch replicas (after pretreatment with glutaraldehyde and/or glycerol, or without pretreatment). The structure of the basal labyrinth in sticklebacks, and probably in other teleost species, differs essentially from the type of labyrinth found in kidney cells of mammals like the rat. In the latter animals, the space enclosed by the membranes of the labyrinth is intercellular. In the stickleback the labyrinth consists of an intracellular system of branched membranes lining narrow saccular spaces. These spaces communicate with the exterior of the cells by means of small pores, located in the lateral and basal parts of the outer cell membranes.
All chemical fixation procedures used introduced specific structural artifacts. It is concluded that the structure of the basal labyrinth is relatively well preserved after fixation with potassium permanganate, with a mixture of glutaraldehyde and osmium tetroxide, or with osmium tetroxide when applied for 10 min only. The unit-membrane structure was, however, absent after all procedures involving osmium tetroxide.
In freeze-etch replicas determinations were made of the numbers of small particles covering the surfaces and fracture faces of the membranes of the basal labyrinth and of the outer cell membranes. The numbers per unit area of surface proved to be markedly constant and specific for each of the four faces of both types of membranes. Specific differences were found between the particle densities of the outer cell membranes and the membranes of the basal labyrinth. This finding points to functional differences between these types of membranes.
Particle densities were not influenced by pre-incubation with glycerol. After fixation with glutaraldehyde, the particles adhering to the outer and inner surfaces had decreased in number.
It is concluded from this study that membrane structure, as revealed in thin sections as well as in freeze-etch replicas, is consistent with Singer's ‘fluid lipid-crystal protein’ model.