The proton pump ATPase of lysosomes and related organelles of the vacuolar apparatus

Schneider, Donald L.

doi:10.1016/s0304-4173(87)80013-7

Cited by 42 publications

(23 citation statements)

References 104 publications

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“…Three major classes of H÷-ATPases exist in mammalian cells: (a) the mitochondrial F-class ATPases; (b) the plasma membrane H÷-ATPases of the P-class; and (c) the V-class of vacuolar H÷-ATPases (Schneider, 1987;Nelson & Taiz, 1989). Each class is distinguished by several parameters including their sensitivity to inhibitors (Nelson & Taiz, 1989).…”

Section: Discussionmentioning

confidence: 99%

“…Studies with members of the Togaviridae and Myxoviridae groups indicate that once the virus particles are bound to their receptors, they are internalized in coated vesicles that soon mature to endosomes (Hoekstra & Kok, 1989;Marsh & Helenius, 1989). Endosomes become acidified by the action of H+-ATPase pumps (MeUman et al, 1986;Schneider, 1987;Nelson & Taiz, 1989). This acidification, in turn, triggers conformational changes in the fusogenic viral glycoprotein(s) located in the virus envelope (White, 1990;Stegmann et al, 1989; 0001-2490 © 1994 SGM L. P~rez and L. Carrasco Lamb, 1993).…”

Section: Introductionmentioning

confidence: 99%

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Involvement of the vacuolar H+-ATPase in animal virus entry

Pérez

Carrasco²

1994

Journal of General Virology

118

110

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Semliki Forest virus (SFV) enters cells by receptormediated endocytosis, followed by acidification of endosomes by the action of the vacuolar H+-ATPase. Fusion of the viral and the endosomal membrane delivers the viral genome to the cytoplasm. Direct blockade of the vacuolar H+-ATPase by the selective inhibitor bafilomycin A1 (BFLA1) prevented the infection of cells by SFV, if the compound was present during the first minutes of infection. Attachment and penetration of virus particles were not the targets of the antibiotic. BFLA1 and the ionophore monensin potently blocked SFV infection even at low pH, indicating that acidic pH is not sufficient for SFV to deliver its genome to the cytoplasm, but the proper functioning of the H +-ATPase pump is necessary. Other enveloped RNAcontaining viruses, such as vesicular stomatitis virus or influenza virus were also blocked by BFLA 1, whereas no effect was observed with Sendai virus, which enters into cells by direct fusion with the plasma membrane. Enveloped DNA-containing viruses, such as herpesviruses and vaccinia virus, infected the cells even when the vacuolar H+-ATPase was inhibited by BFLA1; similar behaviour was observed with poliovirus and adenovirus. Animal virus particles promote the internalization of proteins and other macromolecules during entry. BFLA1 blocked co-entry of the toxin ~-sarcin when induced by SFV, but not when induced by Sendai virus. The inhibition of the enzyme responsible for acidification of endosomes by means of the potent inhibitor BFLA1 constitutes a selective and powerful tool to analyse the low-pH dependent mechanism(s) during virus entry and will aid in understanding the mechanisms and routes of entry of animal viruses into cells.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Involvement of the vacuolar H+-ATPase in animal virus entry

Pérez

Carrasco²

1994

Journal of General Virology

118

110

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“…Proton transport activity mediated by vacuolar H + ATPase, that is N-ethylmaleimide (NEM)-and N,N-dicyclohexylcarbodiimide(DCCD)-sensitive and vanadate-and oligomycin-insensitive H + ATPase, has been identified in numerous intracellular organelles such as endosomes, Golgi apparatus, lysosomes and plant tonoplasts (Schneider, 1987). The acidic interior created by the H + ATPase is considered of critical importance in carrying out an array of organellar functions including receptorligand dissociation, protein digestion, secretion and membrane and receptor recycling (A1- Awqati, 1986).…”

Section: Introductionmentioning

confidence: 99%

H+/Ca2+ exchange in rabbit renal cortical endosomes

Hilden

Madias

1989

J. Membrain Biol.

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We have examined the effect of second messengers on ATP-driven H+ transport in an H+ ATPase-bearing endosomal fraction isolated from rabbit renal cortex. cAMP (0.1 mM) had no effect on H+ transport. Acridine orange fluorescence in the presence of 0.5 mM Ca2+ (+1 mM EGTA) was 19 +/- 6% of control. Inhibition of ATP-driven H+ transport by Ca2+ was concentration dependent; 0.25 and 0.5 mM Ca2+ (+1 mM EGTA) inhibited acridine orange fluorescence by approximately 50 and approximately 80%, respectively. Ca2+ also produced a concentration-dependent increase in the rate of pH-gradient dissipation. Ca2+ did not affect ATP hydrolysis. ATP-dependent Br- uptake was virtually unchanged in the presence of 0.5 mM Ca2+ (+1 mM EGTA). These vesicles were also shown to transport Ca2+ in an ATP-dependent mode. Inositol 1,4,5-trisphosphate had no effect on ATP-dependent Ca2+ uptake. These results are consistent with the co-existence of an H+ ATPase and an H+/Ca2+ exchanger on these endosomes, the latter transport system using the H+ gradient to energize Ca2+ uptake. Attempts to demonstrate an H+/Ca2+ antiporter in the absence of ATP have been unsuccessful. Yet, when a pH gradient was established by preincubation with ATP and residual ATP was subsequently removed by hexokinase + glucose, stimulation of Ca2+ uptake could be demonstrated. A Ca2(+)-dependent increase in H+ permeability and an ATP-dependent Ca2+ uptake might have important implications for the regulation of vacuolar H+ ATPase activity as well as the homeostasis of cytosolic Ca2+ concentration.

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“…The mechanism of endosome-lysosome acidification is also well characterized. The low pH is maintained by a vacuolar proton pump ATPase (Mellman et al, 1986;Schneider, 1987). However, little is known about the mechanism by which lysosomes maintain a high density.…”

Section: Discussionmentioning

confidence: 99%

Effect of pH and ATP on the equilibrium density of lysosomes

Mayorga¹,

Veca²,

Colombo³

et al. 1993

Journal Cellular Physiology

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Lysosomes are membrane bound structures that accumulate and hydrolyze material internalized by the endocytic pathway. A very conspicuous property of this subcellular compartment is its relatively high equilibrium density. The actual mechanism that regulates lysosomal density is poorly understood. In an attempt to gain knowledge on the factors that regulate lysosomal density we have assessed the equilibrium density of lysosomal markers after in vitro incubation of a lysosome-enriched subcellular fraction. Incubation at pH 6 for 10 min at 37 degrees C causes a density shift of several lysosomal markers to light density regions of Percoll gradients. Addition of ATP was able to prevent the acid-induced density shift. Pretreatment of the vesicles with N-ethylmaleimide (NEM) or trypsin inhibited the effect of ATP. Working in intact cells, ATP depletion, a condition that causes cytoplasmic acidification, also decreases lysosomal density. The results indicate that at low pH lysosomal density is preserved by an active process that requires ATP and membrane associated proteins.

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The proton pump ATPase of lysosomes and related organelles of the vacuolar apparatus

Cited by 42 publications

References 104 publications

Involvement of the vacuolar H+-ATPase in animal virus entry

Involvement of the vacuolar H+-ATPase in animal virus entry

H+/Ca2+ exchange in rabbit renal cortical endosomes

Effect of pH and ATP on the equilibrium density of lysosomes

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