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TRPV2 has a pivotal role in macrophage particle binding and phagocytosis.

Nature immunology | Mar 16, 2010

Macrophage phagocytosis is critical for defense against pathogens. Whereas many steps of phagocytosis involve ionic flux, the underlying ion channels remain ill defined. Here we show that zymosan-, immunoglobulin G (IgG)- and complement-mediated particle binding and phagocytosis were impaired in macrophages lacking the cation channel TRPV2. TRPV2 was recruited to the nascent phagosome and depolarized the plasma membrane. Depolarization increased the synthesis of phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P(2)), which triggered the partial actin depolymerization necessary for occupancy-elicited phagocytic receptor clustering. TRPV2-deficient macrophages were also defective in chemoattractant-elicited motility. Consequently, TRPV2-deficient mice showed accelerated mortality and greater organ bacterial load when challenged with Listeria monocytogenes. Our data demonstrate the participation of TRPV2 in early phagocytosis and its fundamental importance in innate immunity.

Pubmed ID: 20118928 RIS Download

Mesh terms: Actins | Animals | Calcium | Calcium Channels | Cell Membrane | Listeria monocytogenes | Listeriosis | Macrophages | Mice | Mice, Knockout | Phagocytosis | RNA, Small Interfering | Receptors, IgG | Ruthenium Red | Survival Analysis | TRPV Cation Channels

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Associated grants

  • Agency: NIAID NIH HHS, Id: AI059298
  • Agency: NIAID NIH HHS, Id: AI071117
  • Agency: NIGMS NIH HHS, Id: GM059251
  • Agency: NIAID NIH HHS, Id: R01AI42287-05
  • Agency: NINDS NIH HHS, Id: R01NS051551
  • Agency: NIAID NIH HHS, Id: R56 AI059298-01A1
  • Agency: NIAID NIH HHS, Id: R56 AI071117-01A1

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