Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.3.1 (Mg2+-ATPase)
 1,484 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The outer and inner bilayers of the apical membrane complex of Schistosoma mansoni were sequentially stripped from adult worms by two incubations in 0.1% digitonin solutions. Membrane removal was evaluated by electron microscopy of worms and bilayer material, using Con A-ferritin as a marker for the outer bilayer. Amounts of Con A removed by the digests were measured with a tritiated Con A marker. To measure the purity of the fractions membrane markers were characterised and quantitated for both bilayers. In the absence of the usual enzymatic markers for plasma membrane diazotised [125I]-iodosulfanilic acid was used as a marker for the outer bilayer. Alkaline phosphatase and a Na+, Mg2+-ATPase were localised to the inner bilayer. From these results we can deduce that the inner bilayer is analogous to the typical, apical plasma membrane of other animal epithelia. The outer bilayer does not share these enzymatic similarities. The integrity of the syncytium after removal of the outer bilayer and the increased levels of lactate dehydrogenase in the supernatant after removal of the inner bilayer suggests that the outer bilayer is secondary in maintaining the permeability barrier of the apical membrane complex, with respect to soluble proteins. The possible significance of these results in terms of the destructive action of complement on the parasite are discussed.
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PMID:Sequential removal of outer bilayer and apical plasma membrane from the surface epithelial syncytium of Schistosoma mansoni. 685 11

Cholesterol and phospholipids serve as structural and functional components of cellular membranes in all eukaryotes. Heterogeneity in cholesterol and phospholipid content both within and between different organelles is an important characteristic of eukaryotic membranes. How this heterogeneity is achieved and orchestrated to maintain proper cellular physiology remains poorly understood. We previously found that overexpression of the Drosophila oxysterol-binding protein (OSBP) leads to sterol accumulation in the Golgi apparatus. Here, we show that Osbp overexpression in a set of neuroendocrine neurons compromises the function of the Golgi apparatus. It impairs trafficking of the neuropeptide bursicon and results in post-eclosion behavior defects characterized by unexpanded wings. We performed a genetic screen to identify modifiers that suppress the unexpanded wing phenotype. A putative phospholipid flippase-encoding gene, CG33298, was validated, suggesting that a membrane-asymmetry-directed mechanism balances cholesterol chaos within the Golgi membranes. Since the functional connection between cholesterol metabolism and the activity of phospholipid flippase has been implicated in studies in yeast and worms, our findings here support an evolutionarily conserved causal link between cholesterol homeostasis and phospholipid asymmetry that maintains normal cellular physiology.
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PMID:Membrane phospholipid asymmetry counters the adverse effects of sterol overloading in the Golgi membrane of Drosophila. 2223 59