title: Distribution of alkaline phosphatase in vegetative dictyostelium cells in relation to the contractile vacuole complex.
abstract: The structure of the contractile vacuole complex of Dictyostelium discoideum has long been a subject of controversy. A model that originated from the work of John Heuser and colleagues described this osmoregulatory organelle as an interconnected array of tubules and cisternae the membranes of which are densely populated with vacuolar proton pumps. A conflicting model described this same organelle as bipartite, consisting of a pump-rich spongiome and a pump-free bladder, the latter membranes being identified by their alkaline phosphatase activity. In the present study we have employed an antiserum specific for Dictyostelium alkaline phosphatase to examine the distribution of this enzyme in vegetative cells. The antiserum labels puncta, probably vesicles, that lie at or near the plasma membrane and are sometimes, but only rarely, enriched near contractile vacuole membranes. We conclude that alkaline phosphatase is not a suitable marker for contractile vacuole membranes. We discuss these results in relation to the two models of contractile vacuole structure and suggest that all data are consistent with the first model.
authors.affiliation: Program in Molecular, Cell, and Developmental Biology, Oklahoma Medical Research Foundation, 825 N. E. 13th Street, Oklahoma City, OK 73104, USA. clarkem@omrf.ouhsc.edu
authors.forename: Margaret
authors.initials: M
authors.lastname: Clarke
authors.forename: Lucinda
authors.initials: L
authors.lastname: Maddera
mesh_terms: D000469:Alkaline Phosphatase / Q000378:metabolism*; D000818:Animals; D004023:Dictyostelium / Q000166:cytology / Q000201:enzymology*; D007150:Immunohistochemistry; D017494:Proton Pumps / Q000378:metabolism; D025262:Vacuolar Proton-Translocating ATPases / Q000378:metabolism*; D014617:Vacuoles / Q000201:enzymology*
chemical_list: D017494:Proton Pumps; D000469:Alkaline Phosphatase; D025262:Vacuolar Proton-Translocating ATPases