Regulation of macrophage nitric oxide production by the protein tyrosine phosphatase Src homology 2 domain phosphotyrosine phosphatase 1 (SHP-1)

Nitric oxide (NO) is a potent molecule involved in the cytotoxic effects mediated by macrophages (MØ) against microorganisms. We previously reported that Src homology 2 domain phosphotyrosine phosphatase 1 (SHP-1)-deficient cells generate a greater amount of NO than wild-type cells in response to in...

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Veröffentlicht in:Immunology 2009-05, Vol.127 (1), p.123-133
Hauptverfasser: Blanchette, Julie, Abu-Dayyeh, Issa, Hassani, Kasra, Whitcombe, Lorie, Olivier, Martin
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container_issue 1
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creator Blanchette, Julie
Abu-Dayyeh, Issa
Hassani, Kasra
Whitcombe, Lorie
Olivier, Martin
description Nitric oxide (NO) is a potent molecule involved in the cytotoxic effects mediated by macrophages (MØ) against microorganisms. We previously reported that Src homology 2 domain phosphotyrosine phosphatase 1 (SHP-1)-deficient cells generate a greater amount of NO than wild-type cells in response to interferon-γ (IFN-γ). We also reported that the Leishmania-induced MØ SHP-1 activity is needed for the survival of the parasite within phagocytes through the attenuation of NO-dependent and NO-independent mechanisms. In the present study, we investigated the role of SHP-1 in regulating key signalling molecules important in MØ NO generation. Janus tyrosine kinase 2 (JAK2), mitogen-activated extracellular signal-regulated protein kinase kinase (MEK), extracellular signal-regulated kinases 1 and 2 (Erk1/Erk2) mitogen-activated protein kinases, p38 and stress-activated mitogen-activated protein kinases/c-Jun NH₂-terminal kinase (SAPK/JNK) were examined in immortalized bone marrow-derived MØ (BMDM) from both SHP-1-deficient motheaten mice (me-3) and their respective littermates (LM-1). The results indicated that Erk1/Erk2 and SAPK/JNK are the main kinases regulated by SHP-1 because the absence of SHP-1 caused an increase in their phosphorylation. Moreover, only Apigenin, the specific inhibitor of Erk1/Erk2, was able to block IFN-γ-induced inducible nitric oxide synthase (iNOS) transcription and translation in me-3 cells. Transcription factor analyses revealed that in the absence of SHP-1, activator protein-1 (AP-1) was activated. The activation of AP-1, and not nuclear factor-κB (NF-κB) or signal transducer and activator of transcription-1α (STAT-1α), may explain the enhanced NO generation in SHP-1-deficent cells. These observations emphasize the involvement of the MAPKs Erk1/Erk2 and SAPK/JNK in NO generation via AP-1 activation. Collectively, our findings suggest that SHP-1 plays a pivotal role in the negative regulation of signalling events leading to iNOS expression and NO generation. Furthermore, our observations underline the importance of SHP-1-mediated negative regulation in maintaining NO homeostasis and thus preventing the abnormal generation of NO that can be detrimental to the host.
doi_str_mv 10.1111/j.1365-2567.2008.02929.x
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We previously reported that Src homology 2 domain phosphotyrosine phosphatase 1 (SHP-1)-deficient cells generate a greater amount of NO than wild-type cells in response to interferon-γ (IFN-γ). We also reported that the Leishmania-induced MØ SHP-1 activity is needed for the survival of the parasite within phagocytes through the attenuation of NO-dependent and NO-independent mechanisms. In the present study, we investigated the role of SHP-1 in regulating key signalling molecules important in MØ NO generation. Janus tyrosine kinase 2 (JAK2), mitogen-activated extracellular signal-regulated protein kinase kinase (MEK), extracellular signal-regulated kinases 1 and 2 (Erk1/Erk2) mitogen-activated protein kinases, p38 and stress-activated mitogen-activated protein kinases/c-Jun NH₂-terminal kinase (SAPK/JNK) were examined in immortalized bone marrow-derived MØ (BMDM) from both SHP-1-deficient motheaten mice (me-3) and their respective littermates (LM-1). The results indicated that Erk1/Erk2 and SAPK/JNK are the main kinases regulated by SHP-1 because the absence of SHP-1 caused an increase in their phosphorylation. Moreover, only Apigenin, the specific inhibitor of Erk1/Erk2, was able to block IFN-γ-induced inducible nitric oxide synthase (iNOS) transcription and translation in me-3 cells. Transcription factor analyses revealed that in the absence of SHP-1, activator protein-1 (AP-1) was activated. The activation of AP-1, and not nuclear factor-κB (NF-κB) or signal transducer and activator of transcription-1α (STAT-1α), may explain the enhanced NO generation in SHP-1-deficent cells. These observations emphasize the involvement of the MAPKs Erk1/Erk2 and SAPK/JNK in NO generation via AP-1 activation. Collectively, our findings suggest that SHP-1 plays a pivotal role in the negative regulation of signalling events leading to iNOS expression and NO generation. 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We previously reported that Src homology 2 domain phosphotyrosine phosphatase 1 (SHP-1)-deficient cells generate a greater amount of NO than wild-type cells in response to interferon-γ (IFN-γ). We also reported that the Leishmania-induced MØ SHP-1 activity is needed for the survival of the parasite within phagocytes through the attenuation of NO-dependent and NO-independent mechanisms. In the present study, we investigated the role of SHP-1 in regulating key signalling molecules important in MØ NO generation. Janus tyrosine kinase 2 (JAK2), mitogen-activated extracellular signal-regulated protein kinase kinase (MEK), extracellular signal-regulated kinases 1 and 2 (Erk1/Erk2) mitogen-activated protein kinases, p38 and stress-activated mitogen-activated protein kinases/c-Jun NH₂-terminal kinase (SAPK/JNK) were examined in immortalized bone marrow-derived MØ (BMDM) from both SHP-1-deficient motheaten mice (me-3) and their respective littermates (LM-1). The results indicated that Erk1/Erk2 and SAPK/JNK are the main kinases regulated by SHP-1 because the absence of SHP-1 caused an increase in their phosphorylation. Moreover, only Apigenin, the specific inhibitor of Erk1/Erk2, was able to block IFN-γ-induced inducible nitric oxide synthase (iNOS) transcription and translation in me-3 cells. Transcription factor analyses revealed that in the absence of SHP-1, activator protein-1 (AP-1) was activated. The activation of AP-1, and not nuclear factor-κB (NF-κB) or signal transducer and activator of transcription-1α (STAT-1α), may explain the enhanced NO generation in SHP-1-deficent cells. These observations emphasize the involvement of the MAPKs Erk1/Erk2 and SAPK/JNK in NO generation via AP-1 activation. Collectively, our findings suggest that SHP-1 plays a pivotal role in the negative regulation of signalling events leading to iNOS expression and NO generation. Furthermore, our observations underline the importance of SHP-1-mediated negative regulation in maintaining NO homeostasis and thus preventing the abnormal generation of NO that can be detrimental to the host.</abstract><cop>Oxford, UK</cop><pub>Oxford, UK : Blackwell Publishing Ltd</pub><pmid>18793215</pmid><doi>10.1111/j.1365-2567.2008.02929.x</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record>
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source MEDLINE; Wiley Online Library Free Content; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Access via Wiley Online Library; IngentaConnect Free/Open Access Journals; PubMed Central
subjects activator protein-1 (AP-1)
Animals
Cells, Cultured
Dose-Response Relationship, Drug
Interferon-gamma - immunology
interferon-γ
Macrophages - drug effects
Macrophages - immunology
MAP Kinase Signaling System - immunology
Mice
Mice, Inbred C3H
mitogen-activated protein kinase
Mitogen-Activated Protein Kinases - immunology
NF-kappa B - metabolism
nitric oxide
Nitric Oxide - biosynthesis
Nitric Oxide Synthase Type II - metabolism
Original
Protein Kinase Inhibitors - pharmacology
Protein Tyrosine Phosphatase, Non-Receptor Type 6 - deficiency
Protein Tyrosine Phosphatase, Non-Receptor Type 6 - immunology
Src homology 2 domain phosphotyrosine phosphatase 1 (SHP-1)
Transcription Factor AP-1 - metabolism
Translocation, Genetic - immunology
title Regulation of macrophage nitric oxide production by the protein tyrosine phosphatase Src homology 2 domain phosphotyrosine phosphatase 1 (SHP-1)
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