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Published on: January 22, 2019
Cell surface F1Fo ATP synthase: a new paradigm?
Sulene L Chi1, Salvatore V Pizzo
1Department of Pathology, Duke University Medical Center, Durham, NC 27710, USA.
Annals of Medicine
|September 30, 2006
Summary
The cell surface ATP synthase, previously known as mitochondrial enzyme, plays new roles in regulating cholesterol and cellular proliferation. Its unique caveolar location is key to these functions.
Area of Science:
- Biochemistry
- Cell Biology
- Enzymology
Background:
- Mitochondrial F1Fo adenosine triphosphate (ATP) synthase is extensively studied.
- Emerging evidence indicates cell surface localization of ATP synthase.
- This cell surface enzyme has functions distinct from its mitochondrial role.
Purpose of the Study:
- To review the expression, interactions, functions, and inhibition of cell surface ATP synthase.
- To highlight the shift in paradigm regarding the location and roles of ATP synthase.
- To explore the implications of cell surface ATP synthase in various physiological and pathological processes.
Main Methods:
- Literature review of recent studies on cell surface ATP synthase.
- Analysis of data concerning enzyme expression and localization.
- Synthesis of findings on functional roles and therapeutic strategies.
Main Results:
- Cell surface ATP synthase is often localized in caveolae.
- It mediates intracellular pH, cellular response to antiangiogenic agents, and cholesterol homeostasis.
- Recent studies show applications in regulating serum cholesterol, cellular proliferation, and antitumor strategies.
Conclusions:
- Cell surface ATP synthase represents a significant shift in understanding enzyme location and function.
- Its diverse roles, particularly in cholesterol regulation and cancer, warrant further investigation.
- Inhibition of cell surface ATP synthase presents potential therapeutic avenues.
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