Src is required for migration, phagocytosis, and interferon beta production in Toll-like receptor-engaged macrophages

BioMedicine - Tập 6 - Trang 1-5 - 2016
Ming-Chei Maa1, Tzeng-Horng Leu2,3,4,5
1Graduate Institute of Basic Medical Science, China Medical University, Taichung, Taiwan
2Institute of Basic Medical Sciences, China Medical University, Taichung, Taiwan
3Department of Pharmacology, China Medical University, Taichung, Taiwan
4Center of Infectious Disease and Signaling Research, College of Medicine, National Cheng Kung University, Tainan, Taiwan
5Department of Pharmacology, College of Medicine, National Cheng Kung University, Tainan, Taiwan

Tóm tắt

As an evolutionarily conserved mechanism, innate immunity controls self-nonself discrimination to protect a host from invasive pathogens. Macrophages are major participants of the innate immune system. Through the activation of diverse Toll-like receptors (TLRs), macrophages are triggered to initiate a variety of functions including locomotion, phagocytosis, and secretion of cytokines that requires the participation of tyrosine kinases. Fgr, Hck, and Lyn are myeloid-specific Src family kinases. Despite their constitutively high expression in macrophages, their absence does not impair LPS responsiveness. In contrast, Src, a barely detectable tyrosine kinase in resting macrophages, becomes greatly inducible in response to TLR engagement, implicating its role in macrophage activation. Indeed, silencing Src suppresses the activated TLR-mediated migration, phagocytosis, and interferon-beta (IFN-β) secretion in macrophages. And these physiological defects can be restored by the introduction of siRNA-resistant Src. Notably, the elevated expression and activity of Src is inducible nitric oxide synthase (iNOS)-dependent. Due to (1) iNOS being a NF-κB target, which can be induced by various TLR ligands, (2) Src can mediate NF-κB activation, therefore, there ought to exist a loop of signal amplification that regulates macrophage physiology in response to the engagement of TLRs.

Tài liệu tham khảo

Weiss RA, Vogt PK. 100 years of Rous sarcoma virus. J Exp Med 2011; 208: 2351-5. Ishizawar R, Parsons SJ. C-Src and cooperation partners in human cancer. Cancer Cell 2004; 6: 209-14. Soriano P, Montgomery C, Geske R, Bradley A. Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice. Cell 1991; 64: 693-702. Marks SCJr. Congenital osteopetrotic mutations as probes of the origin, structure, and function of osteoclasts. Clin Orthop Relat Res 1984; 189: 239-63. Ash P, Loutit JF, Townsend KM. Osteoclasts derived from haematopoietic stem cells. Nature 1980; 283: 669-70. Sanjay A, Houghton A, Neff L, Didomenico E, Bardelay C, Antoine E, et al. Cbl associates with Pyk2 and Src to regulate Src kinase activity, alpha(v)beta(3) integrin-mediated signaling, cell adhesion, and osteoclast motility. J Cell Biol 2001; 152: 181-95. Maa MC, Chanf MY, Li J, Li YY, Hsieh MY, Yang CJ, et al. The iNOS/Src/FAK axis is critical in Toll-like receptor-mediated cell motility in macrophages. Biochim Biophys Acta 2011; 1813: 136-47. Maa MC, Chang MY, Chen YJ, Lin CH, Yu CJ, Yang YL, et al. Requirement of inducible nitric-oxide synthase in lipopolysaccharidemediated Src induction and macrophage migration. J Biol Chem 2008; 283: 31408-16. Chen YJ, Hsieh MY, Chang MY, Chen HC, Jan MS, Maa MC, et al. Eps8 protein facilitates phagocytosis by increasing TLR4-MyD88 protein interaction in lipopolysaccharide-stimulated macrophages. J Biol Chem 2012; 287: 18806-19. Hsieh MY, Chang MY, Chen YJ, Li YK, Chuang TH, Yu GY, et al. The inducible nitric-oxide synthase (iNOS)/Src axis mediates Tolllike receptor 3 Tyrosine 759 phosphorylation and enhances its signal transduction, leading to interferon-β synthesis in macrophages. J Biol Chem 2014; 289: 9208-20. Plowden J, Renshaw-Hoelscher M, Engleman C, Katz J, Sambhara S. Innate immunity in aging: impact on macrophage function. Aging Cell 2004; 3: 161-7. Gordon S, Fraser I, Nath D, Hughes D, Clarje S. Macrophages in tissues and in vitro. Curr Opin Immunol 1992; 4: 25-32. Lemaitre B, Nicolas E, Michaut L, Reichhart JM, Hoffmann JA. The dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell 1996; 86: 973-83. Medzhitov R, Preston-Hurlburt P, Janeway CAJr. A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature 1997; 388: 94. Akira S, Uematsu S, Takeuchi O. Pathogen recognition and innate immunity. Cell 2006; 124: 783-801. Takeuchi O, Akira S. Pattern recognition receptors and inflammation. Cell 2010; 140: 805-20. Jin MS, Lee JO. Structures of the toll-like receptor family and its ligand complexes. Immunity 2008; 29: 182-91. Akira S, Sato S. Toll-like receptors and their signaling mechanisms. Scand J Infect Dis 2003; 35: 555-62. Kopp E, Medzhitov R. Recognition of microbial infection by Tolllike receptors. Curr Opin Immunol 2003; 15: 396-401. Krieg AM. Development of TLR9 agonists for cancer therapy. J Clin Invest 2007; 117: 1184-94. Kawai T, Akira S. Signaling to NF-κB by toll-like receptors. Trends Mol Med 2007; 13: 460-9. Leu TH, Maa MC. Functional implication of the interaction between EGF receptor and c-Src. Front Biosci 2003; 8: s28-38. Xu W, Harrison SC, Eck MJ. Three-dimensional structure of the tyrosine kinase c-Src. Nature 1997; 383: 595-602. Lowell CA. Src-family kinases: rheostats of immune cell signaling. Mol Immunol 2003; 41: 631-43. Weinstein SL, Gold MR, DeFranco AL. Bacterial lipopolysaccharide stimulates protein tyrosyl phosphorylation in macrophages. Proc Natl Acad Sci USA 1991; 88: 4148-52. Meng F, Lowell CA. Lipopolysaccharide (LPS)-induced macrophage activation and signal transduction in the absence of Src-family kinases Hck, Fgr and Lyn. J Exp Med 1997; 185: 1661-70. Leu TH, Charoenfuprasert S, Yen CK, Fan CW, Maa MC. Lipopolysaccharide- induced c-Src expression plays a role in nitric oxide and TNF alpha secretion in macrophages. Mol Immunol 2006; 43: 308-16. Miyazaki T, Sanjay A, Neff L, Tanaka S, Horne WC, Baron R. Src kinase activity is essential for osteoclast function. J Biol Chem. 2004; 279: 17660-6. Parsons JT. Focal adhesion kinase: the first ten years. J Cell Sci 2003; 116: 1409-16. Leu TH, Maa MC. Tyr-863 phosphorylation enhances focal adhesion kinase autophosphorylation at Tyr-397. Oncogene 2002; 21: 6992-7000. Owen KA, Pixley FJ, Thomas KS, Vicente-Manzanares M, Ray BJ, Horwitz AF, et al. Regulation of lamellipodial persistence, adhesion turnover, and motility in macrophages by focal adhesion kinase. J Cell Biol 2007; 179: 1275-87. Underhill DM, Ozinsky A. Phagocytosis of microbes: complexity in action. Annu Rev Immunol 2002; 20: 825-52. Kawai T, Akira S. The roles of TLRs, RLRs and NLRs in pathogen recognition. Int Immunol 2009; 21: 317-37. Owen KA, Thomas KS, Bouton AH. The differential expression of Yersinia pseudotuberculosis adhesins determines the requirement for FAK and/or Pyk2 during bacterial phagocytosis by macrophages. Cell Microbiol 2007; 9: 596-609. Borden EC, Sen GC, Uze G, Silverman RH, Ransohoff RM, Foster GR, et al. Interferons at age 50: past, current and future impact on biomedicine. Nat Rev Drug Discov 2007; 6: 975-90. De Maeyer E, De Maeyer-Guignard J. Type I interferons. Int Rev Immunol 1998; 17: 53-73. Farrar JD, Murphy KM. Type I interferons and T helper development. Immunol Today 2000; 21: 484-9. Hiscott J. Triggering the innate antiviral response through IRF-3 activation. J Biol Chem 2007; 282: 15325-9. Sarkar SN, Peters KL, Elco CP, Sakamoto S, Pal S, Sen GC. Novel roles of TLR3 tyrosine phosphorylation and PI3 kinase in doublestranded RNA signaling. Nat Struct Mol Biol 2004; 11: 1060-7.