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Title:
Guanosine 5ā²-[γ-thio]triphosphate-Mediated Activation of Cytosol Phospholipase C Caused Lysosomal Destabilization | The Journal of Membrane Biology
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Lysosomal disintegration is critical for the organelle functions and cellular viability. In this study, we established that guanosine 5ā²-[γ-thio]triphosphate (GTP-γ-S)-activated cytosol of rat hepatocytes could increase lysosomal permeability to both potassium ions and protons and osmotically destabilize the lysosomes via K+/H+ exchange. These results were obtained through measurements of lysosomal β-hexosaminidase-free activity, membrane potential and intralysosomal pH. Assays of phospholipase C (PLC) activity show that cytosolic PLC was activated upon addition of GTP-γ-S to the cytosol. The effects of cytosol on the lysosomes could be abolished by D609, an inhibitor of PLC, but not by the inhibitors of phospholipase A2. The cytosol-treated lysosomes disintegrated markedly in hypotonic sucrose medium, reflecting that the lysosomal osmotic sensitivity increased. Microscopic observations showed that the lysosomes became more swollen in hypotonic sucrose medium. This indicates that the cytosol treatment induced osmotic shock to the lysosomes and an influx of water into the organelle.
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Keywords {š}
google, scholar, cas, pubmed, article, lysosomal, lysosomes, phospholipase, wang, cell, biol, membrane, biophys, zhang, biochim, acta, activation, cytosol, permeability, privacy, cookies, content, journal, rat, access, chem, sci, information, publish, search, destabilization, xiang, lili, osmotic, biochem, apoptosis, lysosome, data, log, research, biology, guanosine, guojiang, hepatocytes, ions, activity, plc, cytosolic, gtpγs, effects,
Topics {āļø}
tumor-necrosis-factor-α-induced production guanosine 5ā²-[γ-thio]triphosphate-mediated activation ask1/jnk-dependent signaling pathway guanosine 5ā²-[γ-thio]triphosphate lysosomal β-hexosaminidase-free activity month download article/chapter guo-jiang zhang photodamage-induced lysosomal destabilization phospholipase c-type reaction fluorescein isothiocyanate-dextran fluorescence tnf activates nf-Īŗb photo-oxidative disruption tpa-induced signals important virulence factor full article pdf lysosomal osmotic sensitivity privacy choices/manage cookies phosphatidylcholine-specific phospholipase membrane biology aims caused lysosomal destabilization article wang related subjects cultured human fibroblasts hydrolytic enzyme activity organelle-specific initiation european economic area hypotonic sucrose medium microscopic observations showed pinocytic vesicles compared brush border microvilli phosphatidylcholine breakdown folin phenol reagent antitumoral xanthate compound murine cerebral listeriosis pathways involving reduction membrane fluidity modifiers photoinduced membrane rigidification cell death pathways conditions privacy policy increase lysosomal permeability lysosomal cystine transport rat kidney ii proton-translocating atpase molecular dynamics simulations acid-active lipases lysosomal proton pump calcium-independent pla2 calcium-apoptosis link author information authors lipid membrane studied
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headline:Guanosine 5ā²-[γ-thio]triphosphate-Mediated Activation of Cytosol Phospholipase C Caused Lysosomal Destabilization
description:Lysosomal disintegration is critical for the organelle functions and cellular viability. In this study, we established that guanosine 5ā²-[γ-thio]triphosphate (GTP-γ-S)-activated cytosol of rat hepatocytes could increase lysosomal permeability to both potassium ions and protons and osmotically destabilize the lysosomes via K+/H+ exchange. These results were obtained through measurements of lysosomal β-hexosaminidase-free activity, membrane potential and intralysosomal pH. Assays of phospholipase C (PLC) activity show that cytosolic PLC was activated upon addition of GTP-γ-S to the cytosol. The effects of cytosol on the lysosomes could be abolished by D609, an inhibitor of PLC, but not by the inhibitors of phospholipase A2. The cytosol-treated lysosomes disintegrated markedly in hypotonic sucrose medium, reflecting that the lysosomal osmotic sensitivity increased. Microscopic observations showed that the lysosomes became more swollen in hypotonic sucrose medium. This indicates that the cytosol treatment induced osmotic shock to the lysosomes and an influx of water into the organelle.
datePublished:2006-09-18T00:00:00Z
dateModified:2006-09-18T00:00:00Z
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Lysosome
GTP-γ-S
Phospholipase C
Ion permeability
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Biochemistry
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headline:Guanosine 5ā²-[γ-thio]triphosphate-Mediated Activation of Cytosol Phospholipase C Caused Lysosomal Destabilization
description:Lysosomal disintegration is critical for the organelle functions and cellular viability. In this study, we established that guanosine 5ā²-[γ-thio]triphosphate (GTP-γ-S)-activated cytosol of rat hepatocytes could increase lysosomal permeability to both potassium ions and protons and osmotically destabilize the lysosomes via K+/H+ exchange. These results were obtained through measurements of lysosomal β-hexosaminidase-free activity, membrane potential and intralysosomal pH. Assays of phospholipase C (PLC) activity show that cytosolic PLC was activated upon addition of GTP-γ-S to the cytosol. The effects of cytosol on the lysosomes could be abolished by D609, an inhibitor of PLC, but not by the inhibitors of phospholipase A2. The cytosol-treated lysosomes disintegrated markedly in hypotonic sucrose medium, reflecting that the lysosomal osmotic sensitivity increased. Microscopic observations showed that the lysosomes became more swollen in hypotonic sucrose medium. This indicates that the cytosol treatment induced osmotic shock to the lysosomes and an influx of water into the organelle.
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