Protein disulfide isomerase redox-dependent association with p47phox: evidence for an organizer role in leukocyte NADPH oxidase activation
Leukocyte NADPH oxidase activity is regulated by associated protein disulfide isomerase via redox mechanisms involving p47phox. Mechanisms of leukocyte NADPH oxidase regulation remain actively investigated. We showed previously that vascular and macrophage oxidase complexes are regulated by the asso...
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| Published in | Journal of leukocyte biology Vol. 90; no. 4; pp. 799 - 810 |
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| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
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Society for Leukocyte Biology
01.10.2011
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| Abstract | Leukocyte NADPH oxidase activity is regulated by associated protein disulfide isomerase via redox mechanisms involving p47phox.
Mechanisms of leukocyte NADPH oxidase regulation remain actively investigated. We showed previously that vascular and macrophage oxidase complexes are regulated by the associated redox chaperone PDI. Here, we investigated the occurrence and possible underlying mechanisms of PDI‐mediated regulation of neutrophil NADPH oxidase. In a semirecombinant cell‐free system, PDI inhibitors scrRNase (100 μg/mL) or bacitracin (1 mM) near totally suppressed superoxide generation. Exogenously incubated, oxidized PDI increased (by ∼40%), whereas PDIred diminished (by ∼60%) superoxide generation. No change occurred after incubation with PDI serine‐mutated in all four redox cysteines. Moreover, a mimetic CxxC PDI inhibited superoxide production by ∼70%. Thus, oxidized PDI supports, whereas reduced PDI down‐regulates, intrinsic membrane NADPH oxidase complex activity. In whole neutrophils, immunoprecipitation and colocalization experiments demonstrated PDI association with membrane complex subunits and prominent thiol‐mediated interaction with p47phox in the cytosol fraction. Upon PMA stimulation, PDI was mobilized from azurophilic granules to cytosol but did not further accumulate in membranes, contrarily to p47phox. PDI‐p47phox association in cytosol increased concomitantly to opposite redox switches of both proteins; there was marked reductive shift of cytosol PDI and maintainance of predominantly oxidized PDI in the membrane. Pulldown assays further indicated predominant association between PDIred and p47phox in cytosol. Incubation of purified PDI (>80% reduced) and p47phox in vitro promoted their arachidonate‐dependent association. Such PDI behavior is consistent with a novel cytosolic regulatory loop for oxidase complex (re)cycling. Altogether, PDI seems to exhibit a supportive effect on NADPH oxidase activity by acting as a redox‐dependent enzyme complex organizer. |
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| AbstractList | ABSTRACT
Mechanisms of leukocyte NADPH oxidase regulation remain actively investigated. We showed previously that vascular and macrophage oxidase complexes are regulated by the associated redox chaperone PDI. Here, we investigated the occurrence and possible underlying mechanisms of PDI-mediated regulation of neutrophil NADPH oxidase. In a semirecombinant cell-free system, PDI inhibitors scrRNase (100 μg/mL) or bacitracin (1 mM) near totally suppressed superoxide generation. Exogenously incubated, oxidized PDI increased (by ∼40%), whereas PDIred diminished (by ∼60%) superoxide generation. No change occurred after incubation with PDI serine-mutated in all four redox cysteines. Moreover, a mimetic CxxC PDI inhibited superoxide production by ∼70%. Thus, oxidized PDI supports, whereas reduced PDI down-regulates, intrinsic membrane NADPH oxidase complex activity. In whole neutrophils, immunoprecipitation and colocalization experiments demonstrated PDI association with membrane complex subunits and prominent thiol-mediated interaction with p47phox in the cytosol fraction. Upon PMA stimulation, PDI was mobilized from azurophilic granules to cytosol but did not further accumulate in membranes, contrarily to p47phox. PDI-p47phox association in cytosol increased concomitantly to opposite redox switches of both proteins; there was marked reductive shift of cytosol PDI and maintainance of predominantly oxidized PDI in the membrane. Pulldown assays further indicated predominant association between PDIred and p47phox in cytosol. Incubation of purified PDI (>80% reduced) and p47phox in vitro promoted their arachidonate-dependent association. Such PDI behavior is consistent with a novel cytosolic regulatory loop for oxidase complex (re)cycling. Altogether, PDI seems to exhibit a supportive effect on NADPH oxidase activity by acting as a redox-dependent enzyme complex organizer. Mechanisms of leukocyte NADPH oxidase regulation remain actively investigated. We showed previously that vascular and macrophage oxidase complexes are regulated by the associated redox chaperone PDI. Here, we investigated the occurrence and possible underlying mechanisms of PDI-mediated regulation of neutrophil NADPH oxidase. In a semirecombinant cell-free system, PDI inhibitors scrRNase (100 mu g/mL) or bacitracin (1 mM) near totally suppressed superoxide generation. Exogenously incubated, oxidized PDI increased (by similar to 40%), whereas PDIred diminished (by similar to 60%) superoxide generation. No change occurred after incubation with PDI serine-mutated in all four redox cysteines. Moreover, a mimetic CxxC PDI inhibited superoxide production by similar to 70%. Thus, oxidized PDI supports, whereas reduced PDI down-regulates, intrinsic membrane NADPH oxidase complex activity. In whole neutrophils, immunoprecipitation and colocalization experiments demonstrated PDI association with membrane complex subunits and prominent thiol-mediated interaction with p47phox in the cytosol fraction. Upon PMA stimulation, PDI was mobilized from azurophilic granules to cytosol but did not further accumulate in membranes, contrarily to p47phox. PDI-p47phox association in cytosol increased concomitantly to opposite redox switches of both proteins; there was marked reductive shift of cytosol PDI and maintainance of predominantly oxidized PDI in the membrane. Pulldown assays further indicated predominant association between PDIred and p47phox in cytosol. Incubation of purified PDI (>80% reduced) and p47phox in vitro promoted their arachidonate-dependent association. Such PDI behavior is consistent with a novel cytosolic regulatory loop for oxidase complex (re)cycling. Altogether, PDI seems to exhibit a supportive effect on NADPH oxidase activity by acting as a redox-dependent enzyme complex organizer. Leukocyte NADPH oxidase activity is regulated by associated protein disulfide isomerase via redox mechanisms involving p47phox. Mechanisms of leukocyte NADPH oxidase regulation remain actively investigated. We showed previously that vascular and macrophage oxidase complexes are regulated by the associated redox chaperone PDI. Here, we investigated the occurrence and possible underlying mechanisms of PDI‐mediated regulation of neutrophil NADPH oxidase. In a semirecombinant cell‐free system, PDI inhibitors scrRNase (100 μg/mL) or bacitracin (1 mM) near totally suppressed superoxide generation. Exogenously incubated, oxidized PDI increased (by ∼40%), whereas PDIred diminished (by ∼60%) superoxide generation. No change occurred after incubation with PDI serine‐mutated in all four redox cysteines. Moreover, a mimetic CxxC PDI inhibited superoxide production by ∼70%. Thus, oxidized PDI supports, whereas reduced PDI down‐regulates, intrinsic membrane NADPH oxidase complex activity. In whole neutrophils, immunoprecipitation and colocalization experiments demonstrated PDI association with membrane complex subunits and prominent thiol‐mediated interaction with p47phox in the cytosol fraction. Upon PMA stimulation, PDI was mobilized from azurophilic granules to cytosol but did not further accumulate in membranes, contrarily to p47phox. PDI‐p47phox association in cytosol increased concomitantly to opposite redox switches of both proteins; there was marked reductive shift of cytosol PDI and maintainance of predominantly oxidized PDI in the membrane. Pulldown assays further indicated predominant association between PDIred and p47phox in cytosol. Incubation of purified PDI (>80% reduced) and p47phox in vitro promoted their arachidonate‐dependent association. Such PDI behavior is consistent with a novel cytosolic regulatory loop for oxidase complex (re)cycling. Altogether, PDI seems to exhibit a supportive effect on NADPH oxidase activity by acting as a redox‐dependent enzyme complex organizer. |
| Author | Célio X. C. Santos Francisco R. M. Laurindo Júlia T. Takiuti Mariano Janiszewski Antonio Marcus de A. Paes Luciana Lopes Guimarães Sidney Veríssimo-Filho Ana Carolina B. Silva Lucia R. Lopes |
| Author_xml | – sequence: 1 givenname: Antonio Marcus surname: de A. Paes fullname: de A. Paes, Antonio Marcus – sequence: 2 givenname: Sidney surname: Veríssimo-Filho fullname: Veríssimo-Filho, Sidney – sequence: 3 givenname: Luciana Lopes surname: Guimarães fullname: Guimarães, Luciana Lopes – sequence: 4 givenname: Ana Carolina B surname: Silva fullname: Silva, Ana Carolina B – sequence: 5 givenname: Júlia T surname: Takiuti fullname: Takiuti, Júlia T – sequence: 6 givenname: Célio X C surname: Santos fullname: Santos, Célio X C – sequence: 7 givenname: Mariano surname: Janiszewski fullname: Janiszewski, Mariano – sequence: 8 givenname: Francisco R M surname: Laurindo fullname: Laurindo, Francisco R M – sequence: 9 givenname: Lucia R surname: Lopes fullname: Lopes, Lucia R |
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| Snippet | Leukocyte NADPH oxidase activity is regulated by associated protein disulfide isomerase via redox mechanisms involving p47phox.
Mechanisms of leukocyte NADPH... ABSTRACT Mechanisms of leukocyte NADPH oxidase regulation remain actively investigated. We showed previously that vascular and macrophage oxidase complexes are... Mechanisms of leukocyte NADPH oxidase regulation remain actively investigated. We showed previously that vascular and macrophage oxidase complexes are... |
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| Title | Protein disulfide isomerase redox-dependent association with p47phox: evidence for an organizer role in leukocyte NADPH oxidase activation |
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