Extracellular ATP is generated by ATP synthase complex in adipocyte lipid rafts

Kim, Bong Woo; Choo, Hyo Jung; Lee, Joong Won; Kim, Ji Hyun; Ko, Young Gyu

doi:10.1038/emm.2004.60

Cited by 123 publications

(90 citation statements)

References 27 publications

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“…In addition, it was not only shown that ATP subunit a is present at the cell surface but also that the subunit a is a part of a competent multi-subunit F 1 F 0 -ATP synthase complex. [20][21][22]35 The transport of ATP synthase subunit a to the cell surface is sensitive to brefeldin A, a specific blocker of protein translocation from the endoplasmic reticulum to the Golgi apparatus. This observation indicates that cell surface-localized ATP synthase subunit a is transported via the secretory pathway to the cell surface, providing additional proof that the enzyme reaches the cell surface via a well-established processing pathway.…”

Section: Discussionmentioning

confidence: 99%

“…47 Our results showing IF 1 -sensitive extracellular generation of ATP by the glioma C6 cell line lead us to the conclusion that in this cell type there must also be a competent F 1 F 0 -ATP synthase complex at the cell surface, which could also be shown for other cell types. [20][21][22]35 Another known inhibitor of ATP synthase subunit a activity is angiostatin, a proteolytically derived 38 kDa fragment of plasminogen. 19,35 This interaction has been suggested to trigger the caspase-dependent apoptotic pathway in endothelial cells 48 and cytotoxicity in non-endothelial cells.…”

Section: Discussionmentioning

confidence: 99%

“…18 Although first described as a predominantly mitochondrial protein, the entire F 1 F 0 -ATP synthase complex has also been localized to the cell surface of endothelial cells, fibroblasts and hepatocytes, where the complex produces ATP extracellularly. [19][20][21][22] Our observations demonstrate a novel function for APP and Ab in regulating ATP synthase activity through interaction with the a subunit of ATP synthase. ATP is thus not only the main energy source of mammalian cells, but also an important extracellular signaling molecule with multiple functions.…”

Section: Introductionmentioning

confidence: 99%

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Amyloid precursor protein and amyloid β-peptide bind to ATP synthase and regulate its activity at the surface of neural cells

et al. 2007

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Amyloid precursor protein (APP) and amyloid b-peptide (Ab) have been implicated in a variety of physiological and pathological processes underlying nervous system functions. APP shares many features with adhesion molecules in that it is involved in neurite outgrowth, neuronal survival and synaptic plasticity. It is, thus, of interest to identify binding partners of APP that influence its functions. Using biochemical cross-linking techniques we have identified ATP synthase subunit a as a binding partner of the extracellular domain of APP and Ab. APP and ATP synthase colocalize at the cell surface of cultured hippocampal neurons and astrocytes. ATP synthase subunit a reaches the cell surface via the secretory pathway and is N-glycosylated during this process. Transfection of APP-deficient neuroblastoma cells with APP results in increased surface localization of ATP synthase subunit a. The extracellular domain of APP and Ab partially inhibit the extracellular generation of ATP by the ATP synthase complex. Interestingly, the binding sequence of APP and Ab is similar in structure to the ATP synthase-binding sequence of the inhibitor of F1 (IF 1 ), a naturally occurring inhibitor of the ATP synthase complex in mitochondria. In hippocampal slices, Ab and IF 1 similarly impair both short-and long-term potentiation via a mechanism that could be suppressed by blockade of GABAergic transmission. These observations indicate that APP and Ab regulate extracellular ATP levels in the brain, thus suggesting a novel mechanism in Ab-mediated Alzheimer's disease pathology.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Amyloid precursor protein and amyloid β-peptide bind to ATP synthase and regulate its activity at the surface of neural cells

et al. 2007

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“…The oxidation-reduction chain and ATP synthase in the plasma membrane lipid rafts might be necessary for the synthesis of extracellular ATP [44]. Extracellular ATP is generated rapidly immediately after the addition of ADP and Pi into the cell media.…”

Section: Discussionmentioning

confidence: 99%

Oxidation–reduction respiratory chains and ATP synthase complex are localized in detergent-resistant lipid rafts

Ki-Bum

Lee

et al. 2006

Proteomics

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In order to detect and identify ubiquitous lipid raft marker proteins, we isolated lipid rafts from different mouse organs, including the liver, lung, large brain, and kidney, and analyzed their proteins via 2-DE. Many protein spots were determined to be ubiquitous in all of the lipid rafts, and were annotated via LC and MS/MS. Twelve proteins were identified as ubiquitous raft proteins, and most of these were determined to be mitochondrial proteins, including mortalin, prohibitin, voltage-dependent anion channel, ATP synthase, NADH dehydrogenase, and ubiquinol-cytochrome c reductase. Via immunoblotting, these proteins were shown to exist in detergent-resistant lipid rafts prepared using different organ tissues. Since these oxidationreduction respiratory chains and ATP synthase complex were detected in detergent-resistant lipid raft fractions which had been isolated from the plasma membrane but not from the mitochondria, and found in the cell surface when determined by immunofluoresence and immunohistochemistry, we conclude that plasma membrane lipid rafts might contain oxidation-reduction respiratory chains and ATP synthase complex.

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“…Recent studies have suggested regulatory as well as structural functions for caveolin, which may directly regulate numerous signaling proteins in caveolae (Razani et al, 2002;Cohen et al, 2003b;Ha et al, 2003;Gratton et al, 2004;Kim et al, 2004;Kim and Pak, 2005). Different groups have demonstrated inhibition of G proteins, Src family kinases, nitric oxide synthase, epidermal growth factor receptor, MAP kinase, and protein kinase C by a caveolin scaffolding domain, leading to the suggestion that the biological function of caveolin in caveolae is to suppress cellular signaling (Uttenbogaard et al, 2000;Liu et al, 2002;Razani et al, 2002;Cohen et al, 2003b;Gratton et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Modulation of the caveolin-3 and Akt status in caveolae by insulin resistance in H9c2 cardiomyoblasts

Pak²

2005

Exp Mol Med

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Extracellular ATP is generated by ATP synthase complex in adipocyte lipid rafts

Cited by 123 publications

References 27 publications

Amyloid precursor protein and amyloid β-peptide bind to ATP synthase and regulate its activity at the surface of neural cells

Amyloid precursor protein and amyloid β-peptide bind to ATP synthase and regulate its activity at the surface of neural cells

Oxidation–reduction respiratory chains and ATP synthase complex are localized in detergent-resistant lipid rafts

Modulation of the caveolin-3 and Akt status in caveolae by insulin resistance in H9c2 cardiomyoblasts

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