2010
DOI: 10.1007/s11010-010-0650-z
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The β-subunit of ATP synthase is involved in cellular uptake and resecretion of apoA-I but does not control apoA-I-induced lipid efflux in adipocytes

Abstract: Cellular uptake and resecretion of apoA-I (apoA-I recycling) could be an important factor in determining the circulating plasma levels of apoA-I and/or HDL. Using a novel method to study protein recycling, we have recently demonstrated recycling of apoA-I by adipocytes and suggested that this is a receptor mediated process independent of ABCA1 function. In the present study, it is shown that apoA-I recycling by adipocytes can be blocked by a monoclonal antibody against the β-subunit of ATP synthase, a protein … Show more

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Cited by 15 publications
(17 citation statements)
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“…In contrast, at 37°C the cell association and the transport of both apoA-I and HDL were diminished by the stream receptor. 10 In line with observations and conclusions of Howard and colleagues made in experiments with adipocytes, 33 our findings suggest that in addition to mature HDL also lipid-free apoA-I can be internalized by this pathway. However, based on our previously reported findings that initially lipid-free apoA-I is lipidated by ABCA1 for subsequent ABCA1-independent internalization and transport, we assume that a nascent lipidated apoA-I particle rather than lipid-free apoA-I is the substrate for ␤-ATPase triggered endocytosis.…”
Section: Discussionsupporting
confidence: 90%
See 1 more Smart Citation
“…In contrast, at 37°C the cell association and the transport of both apoA-I and HDL were diminished by the stream receptor. 10 In line with observations and conclusions of Howard and colleagues made in experiments with adipocytes, 33 our findings suggest that in addition to mature HDL also lipid-free apoA-I can be internalized by this pathway. However, based on our previously reported findings that initially lipid-free apoA-I is lipidated by ABCA1 for subsequent ABCA1-independent internalization and transport, we assume that a nascent lipidated apoA-I particle rather than lipid-free apoA-I is the substrate for ␤-ATPase triggered endocytosis.…”
Section: Discussionsupporting
confidence: 90%
“…In this regard it is interesting to note that ␤-ATPase was previously shown to modulate the internalization and resecretion of apoA-I by adipocytes without affecting phospholipid and cholesterol efflux. 33 The interaction of ABCG1, SR-BI, and the ␤-ATPase-ADP-P2Y 12 -axis is even more elusive. Figure 6 summarizes our current model of transendothelial transport of apoA-I and HDL: By lipidating apoA-I, ABCA1 generates a particle that is then processed by ABCA1-independent mechanisms for transendothelial transport.…”
Section: Discussionmentioning
confidence: 99%
“…We analyzed the expression level of nuclear-encoded mitochondrial complex I subunit NDUFB8 (Davis et al, 2010), complex II subunit A (Gleason et al, 2011), complex III subunit core 2 (Suthammarak et al, 2010), and ATP synthase beta subunit (Howard et al, 2011), as well as MT-encoded complex IV subunit II (Pang et al, 2011) using specific antibodies (Fig. 6C).…”
Section: Resultsmentioning
confidence: 99%
“…All of the three P2Y receptors that are preferentially activated by ADP (P2Y 1 , P2Y 12 and P2Y 13 ) have been found to be coupled to ecto-F 1 -ATPase activity and display different functions depending on the cell type [32]. For instance, in hepatocytes the apoA-I/ecto-F 1 -ATPase/P2Y 13 axis activates an intracellular RhoA/ROCKI signaling pathway that stimulates HDL uptake and appears to have atheroprotective properties by promoting reverse cholesterol transport [21-24, 30, 44, 45], and in adipocytes HDL-apoA-I, ecto-F 1 -ATPase and P2Y signaling are all involved in lipid metabolism [46-50]. In endothelial cells, apoA-I/ecto-F 1 -ATPase has been previously shown to stimulate HDL transcytosis via activation of P2Y 12 ADP receptors [20].…”
Section: Discussionmentioning
confidence: 99%