Journal of Cell Science · 1980 · 50 citations · 26 references
Life SciencesBiochemistryCell BiologyEnzymologyExocytosisMembrane BiophysicsCellular UltrastructureEndomembrane SystemExocytic Site OrganizationRegulated ExocytosisVesicle FormationVesicle TraffickingCalcium AtpaseRegulated Exocytosis SitesSecretory Pathway Calcium AtpasesSecretory Vesicle PrimingSecretory VesiclesStructure-function CorrelationVesicle Docking Sites
In different Paramecium tetraurelia strains the occurrence of a Ca2+-ATPase (or p-nitro-phenylphosphatase) activity at the preformed attachment and exocytosis sites of the secretory vesicles (trichocysts) was analysed by electron-microscopic cytochemistry and X-ray microanalysis. In conjunction with freeze-fracture studies it was found that only those strains, which contain rosette particles, display this Ca2+-ATPase activity (7S, K 40I, nd 9 (18 degrees C), while other strains (nd 6, nd 9 (27 degrees C), tam 38) are devoid of both these characteristics. The presence (absence) of rosette particles and of Ca2+-ATPase activity at the preformed exocytosis sites is correlated with the capability (incapability) of performing exocytosis in these strains. We discuss several possible interpretations of this structure-function correlation.
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Robert J. DeLorenzo, Steven D. Freedman, Wendy B. Yohe et al. · Proceedings of the National Academy of Sciences · 1979 · 346 citations · Full text