Regulation of Neutrophil Adhesion by Pituitary Growth Hormone Accompanies Tyrosine Phosphorylation of Jak2, p125FAK, and Paxillin

Ryu, Hoon; Lee, Jung‐Hee; Kim, Kwon Seop; Jeong, Seong-Min; Kim, Pyeung-Hyeun; Chung, Hun‐Taeg

doi:10.4049/jimmunol.165.4.2116

Cited by 39 publications

(26 citation statements)

References 64 publications

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“…Maximal stimulation (67%) is lower than the reported increase (220%) in the adhesion of splenocytes to HUVEC induced by IL-2, 40 but higher than the increase (32%) in neutrophil adhesion induced by growth hormone, 32 a PRL-related hormone with well-known immune functions. 41 Similar to the effect of growth hormone on cell adhesion, 32 the dose-response curve of PRL on leukocyte adhesion was 'bell-shaped.' Such a shape is a common observation for PRL stimulation of the PRL receptor, 4 and it has been explained on the basis that signal transduction by PRL requires binding of one PRL molecule to two receptor molecules.…”

Section: Discussionmentioning

confidence: 95%

“…Immunoprecipitation and Western blot analyses were performed as described elsewhere. 32 Briefly, cells were lysed in 100 ml ice-cold lysis buffer (50 mM Tris pH 7.4, 0.5% NP-40, 0.2% sodium deoxycholate, 100 mM NaCl, 1 mM EGTA, 1 mM PMSF, 1 mg/ml aprotinin, 1 mM sodium orthovanadate, and 1 mM NaF), and centrifuged (15 000 r.p.m.) at 41C for 30 min to separate the insoluble fraction.…”

Section: Immunoprecipitation and Western Blotmentioning

confidence: 99%

“…6 This pathway can be functionally linked to the focal adhesion kinase (FAK)/paxillin pathway involved in integrin-mediated cell adhesion and migration. 31,32 In fact, PRL activates JAK-2/STAT-5 and induces tyrosine phosphorylation of FAK and of paxillin in breast carcinoma cells. 31 Moreover, growth hormone, which is structurally related to PRL and has receptors belonging to the same superfamily, 6 stimulates neutrophil adhesion through tyrosine phosphorylation of JAK-2, STAT-3, FAK, and paxillin.…”

mentioning

confidence: 99%

“…31 Moreover, growth hormone, which is structurally related to PRL and has receptors belonging to the same superfamily, 6 stimulates neutrophil adhesion through tyrosine phosphorylation of JAK-2, STAT-3, FAK, and paxillin. 32 This study was undertaken to investigate whether PRL stimulates integrin-mediated adhesion of leukocytes to endothelial cells. Herein, we demonstrate that PRL promotes the adhesion of peripheral blood mononuclear cells (PBMC) to human umbilical vein endothelial cells (HUVEC), and that this stimulation is mediated by the integrins leukocyte functional antigen-1 (LFA-1) (also known as CD11a/CD18) and very late antigen-4 (VLA-4) (or CD49d/CD29).…”

mentioning

confidence: 99%

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Prolactin stimulates integrin-mediated adhesion of circulating mononuclear cells to endothelial cells

Macotela

Nava

et al. 2005

Laboratory Investigation

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Attachment of leukocytes to endothelial cells is an essential step for the extravasation and recruitment of cells at sites of inflammation. The pituitary hormone prolactin (PRL) is involved in the inflammatory process. Here, we show that treatment with PRL of human peripheral blood mononuclear cells (PBMC) stimulates their adhesion to human umbilical vein endothelial cells (HUVEC) activated by interleukin-1b. Stimulation of adhesion by PRL is mediated via integrins leukocyte functional antigen-1 (LFA-1) and very late antigen-4 (VLA-4), because immunoneutralization of both integrins prevents PRL action. Also, PRL promotes the adhesion of PBMC to immobilized intercellular adhesion molecule-1 and fibronectin, ligands for LFA-1 and VLA-4, respectively. Stimulation of integrin-mediated cell adhesion by PRL may involve the activation of chemokine receptors, because PRL upregulates the expression of the G-protein-coupled chemokine receptor CXCR3 in PBMC, and pertussis toxin, a specific G-protein inhibitor, blocks PRL stimulation of PBMC adhesion to HUVEC. In addition, PRL stimulates tyrosine phosphorylation pathways leading to leukocyte adhesion. PRL triggered the tyrosine phosphorylation of Janus kinase-2, of signal transducer and activator of transcription-3 and 5, and of the focal adhesion protein paxillin. Furthermore, genistein, a tyrosine kinase inhibitor, blocked PRLstimulated adhesion of PBMC and Jurkat T-cells to HUVEC. These results suggest that PRL promotes integrinmediated leukocyte adhesion to endothelial cells via chemokine receptors and tyrosine phosphorylation signaling pathways.

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Section: Discussionmentioning

confidence: 95%

Section: Immunoprecipitation and Western Blotmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Prolactin stimulates integrin-mediated adhesion of circulating mononuclear cells to endothelial cells

Macotela

Nava

et al. 2005

Laboratory Investigation

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“…We first evaluated the protein content by a flow cytometric approach to answer whether or not VAA-I alters the expression of a particular protein in comparison with normal neutrophils undergoing spontaneous or constitutive apoptosis. Proteins belonging to the MFAP (gelsolin, paxillin, and vinculin), intermediate filament (vimentin), or microtubule (␣-and ␤-tubulin) families were selected in the present study based on their importance in neutrophil cell physiology (35)(36)(37)(38)(39)(40)(41)(42). As illustrated in Fig.…”

Section: Use Of Flow Cytometry To Evaluate Cytoskeletal Protein Contentmentioning

confidence: 99%

Mechanisms Involved in Spontaneous and Viscum album Agglutinin-I-Induced Human Neutrophil Apoptosis: Viscum album Agglutinin-I Accelerates the Loss of Antiapoptotic Mcl-1 Expression and the Degradation of Cytoskeletal Paxillin and Vimentin Proteins Via Caspases

Lavastre

Pelletier

Saller

et al. 2002

The Journal of Immunology

137

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Viscum album agglutinin-I (VAA-I) is a plant lectin that possesses interesting potential therapeutic properties and immunomodulatory activities. We have recently found that VAA-I is a potent inducer of human neutrophil apoptosis, but the mechanism(s) involved require further elucidation. In this study, we found that VAA-I alters mitochondrial transmembrane potential and increases intracellular levels of reactive oxygen species (ROS). Despite these observations, treatment with the mitochondrial stabilizer, bongkrekic acid, or with catalase, known to degrade H2O2, fails to reverse VAA-I-induced apoptosis. Moreover, VAA-I was found to induce apoptosis in PLB-985 cells deficient in gp91phox, indicating that the lectin acts via an ROS-independent mechanism. Pretreatment of neutrophils with brefeldin A, an inhibitor of vesicular transport, was found to reverse VAA-I-induced apoptosis. Protein expression of Mcl-1 was decreased by VAA-I. The role of caspases in the degradation of cytoskeletal proteins during both spontaneous and VAA-I-induced neutrophil apoptosis was also investigated. Paxillin and vimentin were markedly degraded by VAA-I when compared with neutrophils that undergo spontaneous apoptosis, but not vinculin or α- and β-tubulin. Caspases were involved in cytoskeletal protein degradation because preincubation with the pan-caspase inhibitor N-benzyloxycarbonyl-V-A-D-O-methylfluoromethyl ketone was found to reverse protein cleavage. We conclude that VAA-I needs to be internalized to mediate apoptosis and that its activity is not dependent on a cell surface receptor-mediated pathway. Also, we conclude that VAA-I induces apoptosis by ROS-independent and Mcl-1-dependent mechanisms and that caspases are involved in cytoskeletal protein degradation in both spontaneous and VAA-I-induced neutrophil apoptosis.

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Expression and tyrosine phosphorylation of Crk‐associated substrate lymphocyte type (Cas‐L) protein in human neutrophils

Nakamoto

Seo

Sakai³

et al. 2008

J of Cellular Biochemistry

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Crk-associated substrate lymphocyte type (Cas-L) protein, also known as human enhancer of filamentation 1 (Hef1) or neural precursor cell-expressed, developmentally down-regulated gene 9 (Nedd9), belongs to the Cas family of adapter proteins, which are involved in integrin signaling. Previous reports showed that Cas-L is expressed preferentially in lymphocytes and epithelial cells. Cas-L mediates signals from integrins, T-cell receptors, B-cells receptors, and transforming growth factor beta, leading to cell movement and cell division. Here, we report the expression of Cas-L in neutrophils. Cas-L was tyrosine-phosphorylated when human neutrophils were stimulated by fMLP, tumor necrosis factor-alpha (TNF), or lipopolysaccharide. The tyrosine phosphorylation of Cas-L in fMLP- or TNF- stimulated neutrophils was further enhanced by adhesion of the cells to their substrates. Cas-L was found to be localized at focal adhesions in stimulated neutrophils based on immunofluorescence microscopy. These findings suggest that Cas-L is one of the targets of inflammatory cytokines and is also modulated by cell adhesion process in neutrophils.

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Regulation of Neutrophil Adhesion by Pituitary Growth Hormone Accompanies Tyrosine Phosphorylation of Jak2, p125FAK, and Paxillin

Cited by 39 publications

References 64 publications

Prolactin stimulates integrin-mediated adhesion of circulating mononuclear cells to endothelial cells

Prolactin stimulates integrin-mediated adhesion of circulating mononuclear cells to endothelial cells

Mechanisms Involved in Spontaneous and Viscum album Agglutinin-I-Induced Human Neutrophil Apoptosis: Viscum album Agglutinin-I Accelerates the Loss of Antiapoptotic Mcl-1 Expression and the Degradation of Cytoskeletal Paxillin and Vimentin Proteins Via Caspases

Expression and tyrosine phosphorylation of Crk‐associated substrate lymphocyte type (Cas‐L) protein in human neutrophils

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