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  1. Article: Src kinase-mediated signaling in leukocytes.

    Korade-Mirnics, Z / Corey, S J

    Journal of leukocyte biology

    2000  Volume 68, Issue 5, Page(s) 603–613

    Abstract: ... their different receptors mediate leukocyte development and inflammatory responses. Regardless of the stimulus and ... in initiating the numerous intracellular signaling pathways. Recruited and activated by the receptor, these Src ... receptor type, members of the Src family of protein tyrosine kinases (PTKs) play a critical role ...

    Abstract A concert of antigens, antibodies, cytokines, adhesion molecules, lipid factors, and their different receptors mediate leukocyte development and inflammatory responses. Regardless of the stimulus and receptor type, members of the Src family of protein tyrosine kinases (PTKs) play a critical role in initiating the numerous intracellular signaling pathways. Recruited and activated by the receptor, these Src PTKs amplify and diversify the signal. Multiple pathways arise, which affect cell migration, adhesion, phagocytosis, cell cycle, and cell survival. Essential nonredundant properties of Src PTKs have been identified through the use of gene targeting in mice or in the somatic cell line DT40. Because of their role in mediating leukocyte proliferation and activation, Src PTKs serve as excellent drug targets. Inhibitors of Src family members and dependent pathways may be useful in the treatment of human diseases similar to drugs known to inhibit other signal transduction pathways.
    MeSH term(s) Leukocytes/enzymology ; Leukocytes/physiology ; Signal Transduction/physiology ; src-Family Kinases/physiology
    Chemical Substances src-Family Kinases (EC 2.7.10.2)
    Language English
    Publishing date 2000-11
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 605722-6
    ISSN 1938-3673 ; 0741-5400
    ISSN (online) 1938-3673
    ISSN 0741-5400
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    Zs.A 603: Show issues Location:
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  2. Article ; Online: Polymorphonuclear neutrophil activation by Src phosphorylation contributes to HLA-A2 antibody-induced transfusion-related acute lung injury.

    Le, Aiping / Liu, Wei / Wu, Chenggao / Hu, Piaoping / Zou, Juan / Wu, Yize / Kuang, Linju

    Molecular immunology

    2022  Volume 150, Page(s) 9–19

    Abstract: ... highlights promising target for the treatment of antibody-mediated TRALI. ... acute lung injury (TRALI) via polymorphonuclear neutrophil (PMN) activation, but the signaling pathways involved ... this process remain largely undefined. In this study, we sought to study the signaling pathways involved ...

    Abstract Human leukocyte antigen (HLA)-A2 antibody contributes to the pathogenesis of transfusion-related acute lung injury (TRALI) via polymorphonuclear neutrophil (PMN) activation, but the signaling pathways involved this process remain largely undefined. In this study, we sought to study the signaling pathways involved in the pathogenesis of HLA-A2-induced TRALI. Lipopolysaccharide (LPS), and the plasma from the HLA-A2 antibody-positive donors were utilized to establish a rat model of TRALI. Human pulmonary endothelial cells (HPMECs) were in vitro co-cultured with HLA-A2 antibody-treated PMNs and then treated with LPS to induce a cytotoxicity model. The effects of HLA-A2 antibody on HPMEC injury were evaluated in this model. Besides, dasatinib was used to block the Src phosphorylation to explore whether Src involved in the TRALI or HPMEC injury induced by HLA-A2 antibody. The HLA-A2 antibody plus LPS induced TRALI and stimulated PMN activation in rats. HLA-A2 antibody-induced TRALI could be attenuated via depletion of PMN. HLA-A2 antibody activated NF-κB and NLRP3 inflammasome. In addition, HLA-A2 antibody aggravated the HPMEC injuries and the release of PMN surfaces makers, but dasatinib treatment reversed this effect, indicating that HLA-A2 antibody activated PMNs and exacerbated TRALI by stimulating phosphorylation of Src followed by activation of NF-κB and NLRP3 inflammasome, which was validated in vivo. In summary, HLA-A2 induced PMNs by activating NF-κB/NLRP3 inflammasome via phosphorylated-Src elevation, thereby exacerbating TRALI. This study highlights promising target for the treatment of antibody-mediated TRALI.
    MeSH term(s) Animals ; Antibodies ; Dasatinib/metabolism ; Dasatinib/pharmacology ; Endothelial Cells ; HLA Antigens ; HLA-A2 Antigen ; Humans ; Inflammasomes/metabolism ; Lipopolysaccharides/metabolism ; Lipopolysaccharides/pharmacology ; NF-kappa B/metabolism ; NLR Family, Pyrin Domain-Containing 3 Protein/metabolism ; Neutrophils ; Phosphorylation ; Rats ; Transfusion Reaction/metabolism ; Transfusion-Related Acute Lung Injury/metabolism ; src-Family Kinases/metabolism
    Chemical Substances Antibodies ; HLA Antigens ; HLA-A2 Antigen ; Inflammasomes ; Lipopolysaccharides ; NF-kappa B ; NLR Family, Pyrin Domain-Containing 3 Protein ; src-Family Kinases (EC 2.7.10.2) ; Dasatinib (RBZ1571X5H)
    Language English
    Publishing date 2022-07-30
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 424427-8
    ISSN 1872-9142 ; 0161-5890
    ISSN (online) 1872-9142
    ISSN 0161-5890
    DOI 10.1016/j.molimm.2022.04.010
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    Zs.A 166: Show issues Location:
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  3. Article ; Online: A possible way to prevent the progression of bone lesions in multiple myeloma via Src-homology-region-2-domain-containing-phosphatase-1 activation.

    Kanegasaki, Shiro / Tsuchiya, Tomoko

    Journal of cellular biochemistry

    2021  Volume 122, Issue 10, Page(s) 1313–1325

    Abstract: ... an Src-family-kinase, most probably Lck (lymphocyte-specific-protein-tyrosine-kinase). Dephosphorylation ... On the basis of our recent findings, in which multiple receptor-mediated mast cell functions are ... of LAT. In both osteoclasts and MM cells, therefore, activated SHP-1 acts negatively in receptor-mediated ...

    Abstract On the basis of our recent findings, in which multiple receptor-mediated mast cell functions are regulated via a common signaling cascade, we posit that the formation and functioning of osteoclasts are also controlled by a similar common mechanism. These cells are derived from the same granulocyte/monocyte progenitors and share multiple receptors except those that are cell-specific. In both types of cells, all known receptors reside in lipid rafts, form multiprotein complexes with recruited signaling molecules, and are internalized upon receptor engagement. Signal transduction proceeds in a chain of protein phosphorylations, where adaptor protein LAT (linker-for-activation-of-T-cells) plays a central role. The key kinase that associates LAT phosphorylation and lipid raft internalization is Syk (spleen-tyrosine-kinase) and/or an Src-family-kinase, most probably Lck (lymphocyte-specific-protein-tyrosine-kinase). Dephosphorylation of phosphorylated Syk and Lck by activated SHP-1 (Src-homology-region-2-domain-containing-phosphatase-1) terminates the signal transduction and endocytosis of receptors, resulting in inhibition of osteoclast differentiation and other functions. In malignant plasma cells (MM cells) too, SHP-1 plays a similar indispensable role in controlling signal transduction required for survival and proliferation, though BLNK (B-cell-linker-protein), a functional equivalent of LAT and SLP-76 (SH2-domain-containing-leukocyte-protein-of-76-kDa) in B cells, is used instead of LAT. In both osteoclasts and MM cells, therefore, activated SHP-1 acts negatively in receptor-mediated cellular functions. In osteoblasts, however, activated SHP-1 promotes differentiation, osteocalcin generation, and mineralization by preventing both downregulation of transcription factors, such as Ostrix and Runx2, and degradation of β-catenin required for activation of the transcription factors. SHP-1 is activated by tyrosine phosphorylation and micromolar doses (M-dose) of CCRI-ligand-induced SHP-1 activation. Small molecular compounds, such as A770041, Sorafenib, Nitedanib, and Dovitinib, relieve the autoinhibitory conformation. Activation of SHP-1 by M-dose CCRI ligands or the compounds described may prevent the progression of bone lesions in MM.
    MeSH term(s) Animals ; Bone Diseases/etiology ; Bone Diseases/metabolism ; Bone Diseases/pathology ; Bone Diseases/prevention & control ; Humans ; Multiple Myeloma/complications ; Phosphorylation ; Protein Tyrosine Phosphatase, Non-Receptor Type 6/chemistry ; Protein Tyrosine Phosphatase, Non-Receptor Type 6/metabolism ; Small Molecule Libraries/pharmacology ; src Homology Domains
    Chemical Substances Small Molecule Libraries ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 (EC 3.1.3.48)
    Language English
    Publishing date 2021-05-10
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 392402-6
    ISSN 1097-4644 ; 0730-2312
    ISSN (online) 1097-4644
    ISSN 0730-2312
    DOI 10.1002/jcb.29949
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  4. Article ; Online: Src family kinase-mediated vesicle trafficking is critical for neutrophil basement membrane penetration.

    Rohwedder, Ina / Kurz, Angela R M / Pruenster, Monika / Immler, Roland / Pick, Robert / Eggersmann, Tanja / Klapproth, Sarah / Johnson, Jennifer L / Alsina, Sergi Masgrau / Lowell, Clifford A / Mócsai, Attila / Catz, Sergio D / Sperandio, Markus

    Haematologica

    2019  Volume 105, Issue 7, Page(s) 1845–1856

    Abstract: ... referred to as outside-in signaling. Src family kinases (SFK) are the central players in the outside ... of integrins to their respective ligands, followed by the induction of various signaling events within the cell ... in signaling process, assigning them a critical role for proper immune cell function. Our study investigated ...

    Abstract Leukocyte recruitment into inflamed tissue is highly dependent on the activation and binding of integrins to their respective ligands, followed by the induction of various signaling events within the cell referred to as outside-in signaling. Src family kinases (SFK) are the central players in the outside-in signaling process, assigning them a critical role for proper immune cell function. Our study investigated the role of SFK on neutrophil recruitment
    MeSH term(s) Animals ; Basement Membrane ; Mice ; Mice, Knockout ; Neutrophils ; Proto-Oncogene Proteins ; src-Family Kinases/genetics
    Chemical Substances Proto-Oncogene Proteins ; src-Family Kinases (EC 2.7.10.2)
    Language English
    Publishing date 2019-11-07
    Publishing country Italy
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2333-4
    ISSN 1592-8721 ; 0017-6567 ; 0390-6078
    ISSN (online) 1592-8721
    ISSN 0017-6567 ; 0390-6078
    DOI 10.3324/haematol.2019.225722
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  5. Article ; Online: Ang-(1-7)/ MAS1 receptor axis inhibits allergic airway inflammation via blockade of Src-mediated EGFR transactivation in a murine model of asthma.

    El-Hashim, Ahmed Z / Khajah, Maitham A / Babyson, Rhema S / Renno, Waleed M / Ezeamuzie, Charles I / Benter, Ibrahim F / Akhtar, Saghir

    PloS one

    2019  Volume 14, Issue 11, Page(s) e0224163

    Abstract: ... in increased phosphorylation of Src kinase, EGFR, and ERK1/2. In addition, OVA challenge increased airway ... airway hyperresponsiveness (AHR). Treatment with Ang-(1-7) inhibited phosphorylation of Src kinase, EGFR ... anti-inflammatory signaling pathway. However, the mechanisms by which its mediates the anti-inflammatory effects are ...

    Abstract The angiotensin-(1-7) [Ang-(1-7)]/MAS1 receptor signaling axis is a key endogenous anti-inflammatory signaling pathway. However, the mechanisms by which its mediates the anti-inflammatory effects are not completely understood. Using an allergic murine model of asthma, we investigated whether Ang-1(1-7)/MAS1 receptor axis a): inhibits allergic inflammation via modulation of Src-dependent transactivation of the epidermal growth factor receptor (EGFR) and downstream signaling effectors such as ERK1/2, and b): directly inhibits neutrophil and/or eosinophil chemotaxis ex vivo. Ovalbumin (OVA)-induced allergic inflammation resulted in increased phosphorylation of Src kinase, EGFR, and ERK1/2. In addition, OVA challenge increased airway cellular influx, perivascular and peribronchial inflammation, fibrosis, goblet cell hyper/metaplasia and airway hyperresponsiveness (AHR). Treatment with Ang-(1-7) inhibited phosphorylation of Src kinase, EGFR, ERK1/2, the cellular and histopathological changes and AHR. Ang-(1-7) treatment also inhibited neutrophil and eosinophil chemotaxis ex vivo. These changes were reversed following pre-treatment with A779. These data show that the anti-inflammatory actions of Ang-(1-7)/ MAS1 receptor axis are mediated, at least in part, via inhibition of Src-dependent transactivation of EGFR and downstream signaling molecules such as ERK1/2. This study therefore shows that inhibition of the Src/EGRF/ERK1/2 dependent signaling pathway is one of the mechanisms by which the Ang-(1-7)/ MAS1 receptor axis mediates it anti-inflammatory effects in diseases such as asthma.
    MeSH term(s) Angiotensin I/metabolism ; Animals ; Asthma/metabolism ; Blotting, Western ; Bronchoalveolar Lavage Fluid/cytology ; Chemotaxis, Leukocyte ; Disease Models, Animal ; ErbB Receptors/metabolism ; Fluorescent Antibody Technique ; Lung/pathology ; Male ; Mice ; Mice, Inbred BALB C ; Peptide Fragments/metabolism ; Proto-Oncogene Proteins/metabolism ; Receptors, G-Protein-Coupled/metabolism ; Respiratory Hypersensitivity/metabolism ; Respiratory Hypersensitivity/pathology ; Signal Transduction ; src-Family Kinases/metabolism
    Chemical Substances Peptide Fragments ; Proto-Oncogene Proteins ; Receptors, G-Protein-Coupled ; proto-oncogene proteins c-mas-1 ; Angiotensin I (9041-90-1) ; EGFR protein, mouse (EC 2.7.10.1) ; ErbB Receptors (EC 2.7.10.1) ; src-Family Kinases (EC 2.7.10.2) ; angiotensin I (1-7) (IJ3FUK8MOF)
    Language English
    Publishing date 2019-11-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0224163
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  6. Article ; Online: Src family kinase expression and subcellular localization in macrophages: implications for their role in CSF-1-induced macrophage migration.

    Dwyer, Amy R / Mouchemore, Kellie A / Steer, James H / Sunderland, Andrew J / Sampaio, Natalia G / Greenland, Eloise L / Joyce, David A / Pixley, Fiona J

    Journal of leukocyte biology

    2016  Volume 100, Issue 1, Page(s) 163–175

    Abstract: ... kinase p110δ is a critical mediator of colony-stimulating factor-1-stimulated motility ... We report a comprehensive analysis of individual Src family kinase expression in macrophage cell lines and ... primary macrophages and demonstrate colony-stimulating factor-1-induced changes in Src family kinase ...

    Abstract A major role of colony-stimulating factor-1 is to stimulate the differentiation of mononuclear phagocytic lineage cells into adherent, motile, mature macrophages. The colony-stimulating factor-1 receptor transduces colony-stimulating factor-1 signaling, and we have shown previously that phosphatidylinositol 3-kinase p110δ is a critical mediator of colony-stimulating factor-1-stimulated motility through the colony-stimulating factor-1 receptor pY721 motif. Src family kinases are also implicated in the regulation of macrophage motility and in colony-stimulating factor-1 receptor signaling, although functional redundancy of the multiple SFKs expressed in macrophages makes it challenging to delineate their specific functions. We report a comprehensive analysis of individual Src family kinase expression in macrophage cell lines and primary macrophages and demonstrate colony-stimulating factor-1-induced changes in Src family kinase subcellular localization, which provides clues to their distinct and redundant functions in macrophages. Moreover, expression of individual Src family kinases is both species specific and dependent on colony-stimulating factor-1-induced macrophage differentiation. Hck associated with the activated colony-stimulating factor-1 receptor, whereas Lyn associated with the receptor in a constitutive manner. Consistent with this, inhibitor studies revealed that Src family kinases were important for both colony-stimulating factor-1 receptor activation and colony-stimulating factor-1-induced macrophage spreading, motility, and invasion. Distinct colony-stimulating factor-1-induced changes in the subcellular localization of individual SFKs suggest specific roles for these Src family kinases in the macrophage response to colony-stimulating factor-1.
    MeSH term(s) Animals ; Cell Differentiation/drug effects ; Cell Movement/drug effects ; Cells, Cultured ; Humans ; Macrophage Colony-Stimulating Factor/pharmacology ; Macrophages/cytology ; Macrophages/drug effects ; Macrophages/metabolism ; Mice ; Mice, Inbred C57BL ; Phosphorylation ; Receptor, Macrophage Colony-Stimulating Factor/metabolism ; Signal Transduction/drug effects ; Subcellular Fractions ; src-Family Kinases/metabolism
    Chemical Substances Macrophage Colony-Stimulating Factor (81627-83-0) ; Receptor, Macrophage Colony-Stimulating Factor (EC 2.7.10.1) ; src-Family Kinases (EC 2.7.10.2)
    Language English
    Publishing date 2016-07
    Publishing country United States
    Document type Journal Article
    ZDB-ID 605722-6
    ISSN 1938-3673 ; 0741-5400
    ISSN (online) 1938-3673
    ISSN 0741-5400
    DOI 10.1189/jlb.2A0815-344RR
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    Zs.A 603: Show issues Location:
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  7. Article ; Online: Pharmacological Inactivation of Src Family Kinases Inhibits LPS-Induced TNF-α Production in PBMC of Patients with Behçet's Disease.

    Irtegun, Sevgi / Pektanc, Gulsum / Akkurt, Zeynep M / Bozkurt, Mehtap / Turkcu, Fatih M / Kalkanli-Tas, Sevgi

    Mediators of inflammation

    2016  Volume 2016, Page(s) 5414369

    Abstract: ... the role of Src family kinases (SFKs) in production of some LPS-induced proinflammatory cytokines ... diseases. Revealing a key signaling regulatory mechanism involved in proinflammatory cytokines/chemokines ...

    Abstract Behçet's disease (BD) is a multisystemic chronic inflammatory disease characterized by relapsing oral and genital ulcers, uveitis, and skin lesions. The pathogenesis of BD is still unknown. Aberrant production of some cytokines/chemokines plays an important role in the pathogenesis of various inflammatory diseases. Revealing a key signaling regulatory mechanism involved in proinflammatory cytokines/chemokines production is critical for understanding of the pathogenesis of BD. The aim of this study was to determine the role of Src family kinases (SFKs) in production of some LPS-induced proinflammatory cytokines/chemokines in peripheral blood mononuclear cells (PBMC) of active BD patients. Chemical inhibition of SFKs activity impaired LPS-induced TNF-α production in PBMC of active BD patients, suggesting that modulating SFKs activity may be a potential target for BD treatment.
    MeSH term(s) Adult ; Behcet Syndrome/metabolism ; Blotting, Western ; Cells, Cultured ; Enzyme-Linked Immunosorbent Assay ; Female ; Humans ; Leukocytes, Mononuclear/drug effects ; Leukocytes, Mononuclear/metabolism ; Lipopolysaccharides/pharmacology ; Male ; Tumor Necrosis Factor-alpha/metabolism ; Young Adult ; src-Family Kinases/metabolism
    Chemical Substances Lipopolysaccharides ; Tumor Necrosis Factor-alpha ; src-Family Kinases (EC 2.7.10.2)
    Language English
    Publishing date 2016
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1137605-3
    ISSN 1466-1861 ; 0962-9351
    ISSN (online) 1466-1861
    ISSN 0962-9351
    DOI 10.1155/2016/5414369
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    Zs.A 3575: Show issues Location:
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  8. Article ; Online: MUC1-mediated motility in breast cancer: a review highlighting the role of the MUC1/ICAM-1/Src signaling triad.

    Haddon, Lacey / Hugh, Judith

    Clinical & experimental metastasis

    2015  Volume 32, Issue 4, Page(s) 393–403

    Abstract: ... receptor kinase Src, a signaling molecule involved in cell differentiation, proliferation, adhesion and ... adhesion pathways used by leukocytes during the inflammatory response. MUC1 is a type 1 transmembrane ... protein whose cytoplasmic tail acts as a scaffold for several signaling pathways including the non ...

    Abstract Breast cancer is the most common cancer in women with the leading cause of death being metastasis, the spread of cancer to distant organs. For those patients with high-risk estrogen receptor positive (ER+) breast cancer, an increased expression of the glycoprotein MUC1 is associated with resistance to anti-hormonal therapy, metastasis and death. Tumor cells may use MUC1 to metastasize by exploiting the vascular adhesion pathways used by leukocytes during the inflammatory response. MUC1 is a type 1 transmembrane protein whose cytoplasmic tail acts as a scaffold for several signaling pathways including the non-receptor kinase Src, a signaling molecule involved in cell differentiation, proliferation, adhesion and motility. This review will highlight our current knowledge of how MUC1/ICAM-1 binding can lead to the recruitment and activation of Src and propose a novel role for lipid raft microdomains in this promigratory signaling. Improved understanding of the mechanism of metastases and the underlying signaling cascade is a prerequisite to the discovery of therapeutic targets to prevent metastasis and death in ER+ breast cancer patients.
    MeSH term(s) Amino Acid Sequence ; Breast Neoplasms/pathology ; Cell Movement ; Female ; Humans ; Intercellular Adhesion Molecule-1/metabolism ; Membrane Microdomains/metabolism ; Molecular Sequence Data ; Mucin-1/metabolism ; Neoplasm Metastasis/pathology ; Protein Binding ; Receptors, Estrogen/metabolism ; Signal Transduction ; src-Family Kinases/metabolism
    Chemical Substances MUC1 protein, human ; Mucin-1 ; Receptors, Estrogen ; Intercellular Adhesion Molecule-1 (126547-89-5) ; src-Family Kinases (EC 2.7.10.2)
    Language English
    Publishing date 2015-04
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ZDB-ID 604952-7
    ISSN 1573-7276 ; 0262-0898
    ISSN (online) 1573-7276
    ISSN 0262-0898
    DOI 10.1007/s10585-015-9711-8
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  9. Article ; Online: Niacin decreases leukocyte myeloperoxidase: mechanistic role of redox agents and Src/p38MAP kinase.

    Ganji, Shobha H / Kamanna, Vaijinath S / Kashyap, Moti L

    Atherosclerosis

    2014  Volume 235, Issue 2, Page(s) 554–561

    Abstract: ... with specific inhibitors suggest that ROS-dependent Src and p38MAP kinase mediate decreased MPO activity ... through reactive oxygen species (ROS)-mediated signaling, decreases neutrophil MPO release and its activity, protects ... of leukocyte MPO release and MPO-mediated formation of dysfunctional HDL. Niacin and niacin-related chemical ...

    Abstract Objectives: Leukocyte myeloperoxidase (MPO) is a major player in the pathogenesis of various chronic diseases including atherosclerosis. This study proposes the novel concept that niacin, through reactive oxygen species (ROS)-mediated signaling, decreases neutrophil MPO release and its activity, protects apolipoprotein-AI (apo-AI) modification and improves HDL function.
    Methods: Human blood leukocytes and leukocytic cell line HL-60 cells were treated with niacin, and stimulated with phorbol myristate acetate (PMA). Cellular and released MPO activity in the medium was measured by assessing chlorination of MPO-specific substrate. MPO protein release in the medium and apo-AI degradation was measured by Western blot analysis. Monocyte adhesion to human aortic primary endothelial cells was measured to assess biological function of HDL/apo-AI.
    Results: PMA significantly increased leukocyte MPO activity in both intracellular extract and medium. Niacin (0.25-0.5 mM) decreased PMA-induced MPO activity (cellular and released in the media). Niacin also decreased MPO protein mass in the medium without affecting its mRNA expression. Increased NADPH oxidase and ROS production by PMA were also significantly inhibited by niacin. Studies with specific inhibitors suggest that ROS-dependent Src and p38MAP kinase mediate decreased MPO activity by niacin. Niacin blocked apo-AI degradation, and apo-AI from niacin treated cells decreased monocyte adhesion to aortic endothelial cells.
    Conclusions: These findings identify niacin as a potent inhibitor of leukocyte MPO release and MPO-mediated formation of dysfunctional HDL. Niacin and niacin-related chemical entities may form important therapeutic agents for MPO-mediated inflammatory diseases.
    MeSH term(s) Apolipoprotein A-I/metabolism ; HL-60 Cells ; Humans ; Leukocytes/drug effects ; Leukocytes/enzymology ; NADPH Oxidases/antagonists & inhibitors ; Niacin/pharmacology ; Peroxidase/secretion ; Reactive Oxygen Species/metabolism ; Tetradecanoylphorbol Acetate/pharmacology ; p38 Mitogen-Activated Protein Kinases/metabolism ; src-Family Kinases/metabolism
    Chemical Substances Apolipoprotein A-I ; Reactive Oxygen Species ; Niacin (2679MF687A) ; Peroxidase (EC 1.11.1.7) ; NADPH Oxidases (EC 1.6.3.-) ; src-Family Kinases (EC 2.7.10.2) ; p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Tetradecanoylphorbol Acetate (NI40JAQ945)
    Language English
    Publishing date 2014-08
    Publishing country Ireland
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 80061-2
    ISSN 1879-1484 ; 0021-9150
    ISSN (online) 1879-1484
    ISSN 0021-9150
    DOI 10.1016/j.atherosclerosis.2014.05.948
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  10. Article ; Online: Redox and Src family kinase signaling control leukocyte wound attraction and neutrophil reverse migration.

    Tauzin, Sebastien / Starnes, Taylor W / Becker, Francisco Barros / Lam, Pui-ying / Huttenlocher, Anna

    The Journal of cell biology

    2014  Volume 207, Issue 5, Page(s) 589–598

    Abstract: Tissue damage induces early recruitment of neutrophils through redox-regulated Src family kinase ... migration. We found that redox-SFK signaling through p22phox and Yes-related kinase is necessary ... wound attraction and repulsion through pathways that involve contact-mediated guidance. ...

    Abstract Tissue damage induces early recruitment of neutrophils through redox-regulated Src family kinase (SFK) signaling in neutrophils. Redox-SFK signaling in epithelium is also necessary for wound resolution and tissue regeneration. How neutrophil-mediated inflammation resolves remains unclear. In this paper, we studied the interactions between macrophages and neutrophils in response to tissue damage in zebrafish and found that macrophages contact neutrophils and induce resolution via neutrophil reverse migration. We found that redox-SFK signaling through p22phox and Yes-related kinase is necessary for macrophage wound attraction and the subsequent reverse migration of neutrophils. Importantly, macrophage-specific reconstitution of p22phox revealed that macrophage redox signaling is necessary for neutrophil reverse migration. Thus, redox-SFK signaling in adjacent tissues is essential for coordinated leukocyte wound attraction and repulsion through pathways that involve contact-mediated guidance.
    MeSH term(s) Animals ; Cell Communication/immunology ; Chemotaxis, Leukocyte ; Kinetics ; Macrophages/immunology ; NADPH Oxidases/metabolism ; Neutrophil Infiltration ; Oxidation-Reduction ; Reactive Oxygen Species/metabolism ; Signal Transduction/immunology ; Wound Healing/immunology ; Zebrafish ; Zebrafish Proteins/metabolism ; src-Family Kinases/metabolism
    Chemical Substances Reactive Oxygen Species ; Zebrafish Proteins ; NADPH Oxidases (EC 1.6.3.-) ; src-Family Kinases (EC 2.7.10.2)
    Language English
    Publishing date 2014-12-08
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.201408090
    Database MEDical Literature Analysis and Retrieval System OnLINE

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