Ultrastructural tracer studies on the permeability of the Malpighian tubule of the pill millipede, Glomeris marginate (Villers).
The electron-dense tracers ferritin, and iron-dextran, and the protein horseradish peroxidase, have been used to investigate the ultrastructural basis of permeability in the upper and lower segments of the Malpighian tubules of Glomeris marginata. All these materials were able to cross the basal lamina and enter the tubule lumen of the upper segment, and it was established that horseradish peroxidase was able to enter the channels which interrupt the apical junctions. In the upper segment, ferritin, iron-dextran, and horseradish peroxidase are taken up and accumulated within intracellular vesicles. In the lower segment ferritin and iron-dextran enter the cells but become generally distributed over the cytoplasm, as well as entering membrane-bounded vacoules. The behaviour of horseradish peroxidase could not be assessed by owing to the presence of endogenous peroxidase activity in the cells. After fixation by direct application of glutaraldehyde to the undissected tubules, the extracellular spaces contained large numbers of membrane-bounded vesicles. The significance of these observations is discussed in relation to the physiological activities of the tubules.
D000818:Animals; D001181:Arthropods / Q000166:cytology*; D002988:Cloaca / Q000648:ultrastructure*; D003911:Dextrans; D005293:Ferritins; D006735:Horseradish Peroxidase; D007501:Iron; D008317:Malpighian Tubules / Q000648:ultrastructure*; D008854:Microscopy, Electron; D010539:Permeability
D003911:Dextrans; D005293:Ferritins; D007501:Iron; D006735:Horseradish Peroxidase