Ultrastructural studies on the Malpighian tubule of the pill millipede, Glomeris marginata (villers).
Ultrastructural studies on the Malpighian tubules of Glomeris marginata (Villers) reveal considerable morphological differences between the upper, fluid secreting, segment, and the lower segment which is at present of unknown function. Previous reports have shown that the upper tubule has a high permeability to compounds of high molecular weight. This may be accounted for by the fact that the epithelium shows very extensive intercellular spaces which are linked directly to junctions apparently specialised to provide a low resistance extracellular pathway between the haemocoel and the tubule lumen. Histochemical studies on the localisation of phosphatase enzymes reveal intracellular vesicles with acid phosphatase activity. The basal labyrinth of the lower tubule exhibits considerable alkaline phosphatase activity which is apparently identical in location to the enzyme revealed by two different ATPase localisation techniques.
D000135:Acid Phosphatase / Q000032:analysis; D000251:Adenosine Triphosphatases; D000469:Alkaline Phosphatase / Q000032:analysis; D000818:Animals; D001181:Arthropods / Q000033:anatomy & histology*; D002988:Cloaca / Q000648:ultrastructure*; D005110:Extracellular Space; D008317:Malpighian Tubules / Q000201:enzymology / Q000648:ultrastructure*; D008970:Molecular Weight; D010539:Permeability
D000469:Alkaline Phosphatase; D000135:Acid Phosphatase; D000251:Adenosine Triphosphatases