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Regulation of Neutrophil Adhesion by Pituitary Growth Hormone Accompanies Tyrosine Phosphorylation of Jak2, p125^FAK, and Paxillin¹

Hoon Ryu^2,3,*,§, Jung-Hee Lee^2,*,, Kwon Seop Kim, Seong-Min Jeong^§, Pyeung-Hyeun Kim and Hun-Taeg Chung^4,¶

^* Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, and Department of Cell Biology, Harvard Medical School, Boston, MA 02115; Department of Microbiology, Kangwon National University College of Natural Science, Chunchon, Kangwon, Republic of Korea; and ^§ Department of Immunology and Bioenergy (Qi) Medicine, Institute of Biotechnology, and ^¶ Department of Microbiology and Immunology, Wonkwang University School of Medicine, Iksan, Chonbuk, Republic of Korea

Neutrophil adhesion is fundamentally important during the onset of inflammatory responses. The adhesion signaling pathways control neutrophil arrest and extravasation and influence neutrophil shape and function at sites of inflammation. In the present study the intracellular signaling pathways for the adhesion of human neutrophils by pituitary growth hormone (GH) were examined. Pituitary GH triggered the tyrosine phosphorylation of Janus kinase 2 (Jak2) and STAT3 in neutrophils. In addition, pituitary GH treatment resulted in the morphological changes and the tyrosine phosphorylation of focal adhesion kinase (p125^FAK) and paxillin. Preincubation with genistein, a tyrosine kinase inhibitor, blocked the GH-stimulated adhesion and Jak2, STAT3, p125^FAK, and paxillin phosphorylation. Confocal microscopy revealed that pituitary GH stimulates the focal localization of p125^FAK, paxillin, phosphotyrosine, and filamentous actin filament into the membrane rufflings and uropods of human neutrophils. Immunoprecipitation experiments revealed a physical association of Jak2 with p125^FAK via STAT3 in vivo. Also an in vitro kinase assay showed an augmentation of p125^FAK autophosphorylation as a result of pituitary GH treatment. These results suggest that pituitary GH modulates neutrophil adhesion through tyrosine phosphorylation of Jak2, p125^FAK, and paxillin and actin polymerization.

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