title: Fine structural localization of Ca2+-ATPase activity at the frog neuromuscular junction.
abstract: Ca2+-ATPase activity has been shown to be associated with the nerve terminal plasma membrane at the frog neuromuscular junction. Using a modification of the Wachstein-Meisel procedure for localization of phosphatases, a dense reaction product forms at the neuronal plasma membrane/Schwann cell interface. It has been determined that this reaction product is associated with the plasma membrane of the nerve terminal and not the plasma membrane of the Schwann cell. No ATPase activity is demonstrated at the presynaptic portion of the plasma membrane facing the synaptic gap. When a preparation is denervated, a Schwann cell process moves into the space previously occupied by the nerve. There is no ATPase activity associated with the Schwann cell plasma membrane. Conversely, when the Schwann cell is selectively injured, dense reaction product continues to be associated with the nerve terminal plasma membrane. There is some indication that this ATPase activity is dependent on the presence of Ca2+ and Mg2+. Incubation in the calmodulin inhibitor, R24571, shows little inhibition of labelling.
authors.affiliation: University of Illinois, Department of Anatomy and Cell Biology, Chicago 60680.
authors.forename: G D
authors.initials: GD
authors.lastname: Pappas
authors.forename: V
authors.initials: V
authors.lastname: Kriho
mesh_terms: D000818:Animals; D000252:Calcium-Transporting ATPases / Q000032:analysis*; D002462:Cell Membrane / Q000201:enzymology / Q000648:ultrastructure; D006651:Histocytochemistry; D008854:Microscopy, Electron; D009469:Neuromuscular Junction / Q000201:enzymology* / Q000648:ultrastructure; D011894:Rana pipiens
chemical_list: D000252:Calcium-Transporting ATPases