白细胞介素-8在炎症反应中的作用及其表达调控机制
Role and Expression Regulation of Interleukin-8 in Inflammatory Reaction
DOI: 10.12677/HJBM.2023.132025, PDF,  被引量    国家自然科学基金支持
作者: 朱秀云, 吴 敏*:浙江师范大学生命科学学院,浙江 金华
关键词: 白细胞介素-8炎症信号通路激酶NF-κBInterleukin-8 Inflammation Signal Pathway Kinase NF-κB
摘要: 白细胞介素-8是诱导炎症反应发生的主要趋化因子。其前体含99个氨基酸残基,经裂解活化后则由细胞分泌释放。白细胞介素-8可与免疫细胞和肿瘤细胞的细胞膜上受体结合,主要经由偶联G蛋白来激活下游相关的信号通路,如丝裂原活化蛋白激酶、磷脂酰肌醇-3-激酶、蛋白激酶C等。本综述将重点阐述这些信号通路的活化机制及其生理和免疫功能。此外,也将概括说明诱导白细胞介素-8表达的转录因子和促进其分泌的机制,并详述主要转录因子,核因子-κB的作用机理。了解白细胞介素-8的功能和调控机制,有助于阐明炎症反应发生的过程和开发新的抗炎药物。
Abstract: Interleukin-8 (IL-8) is a major chemotaxin that elicits the inflammation response. The proprotein of IL-8 including 99 amino acid residues is activated by proteolysis and then secreted by the cell. IL-8 binds to the receptor on the cell membrane of immune or tumor cells and via G protein-coupled mechanisms stimulates downstream signaling pathways, such as mitogen-activated protein kinase, inositol phosphate-3 kinase and protein kinase C, etc. This review mainly focuses on the activation mechanism of these signaling pathways and related physiological function and immune system. In addition, the review covers the transcription factors that stimulate IL-8 expression and secretion with a great attention on the major factor, nuclear factor-κB. Understanding the function and regulation of IL-8 may elucidate the development of inflammation and discover new anti-inflammatory drugs.
文章引用:朱秀云, 吴敏. 白细胞介素-8在炎症反应中的作用及其表达调控机制[J]. 生物医学, 2023, 13(2): 219-227. https://doi.org/10.12677/HJBM.2023.132025

参考文献

[1] Bhusal, R.P., Foster, S.R. and Stone, M.J. (2020) Structural Basis of Chemokine and Receptor Interactions: Key Regulators of Leukocyte Recruitment in Inflammatory Responses. Protein Science, 29, 420-432. [Google Scholar] [CrossRef] [PubMed]
[2] Walz, A., Peveri, P., Aschauer, H. and Baggiolini, M. (1987) Purification and Amino Acid Sequencing of NAF, a Novel Neutrophil-Activating Factor Produced by Monocytes. Biochemical and Biophysical Research Communications, 149, 755-761. [Google Scholar] [CrossRef
[3] Kownatzki, E., Kapp, A. and Uhrich, S. (1986) Novel Neutrophil Chemotactic Factor Derived from Human Peripheral Blood Mononuclear Leucocytes. Clinical and Experimental Immunology, 64, 214-222.
[4] Yoshimura, T., Matsushima, K., Oppenheim, J.J. and Leonard, E.J. (1987) Neutrophil Chemotactic Factor Produced by Lipopolysaccharide (LPS)-Stimulated Human Blood Mononuclear Leukocytes: Partial Characterization and Separation from Interleukin 1 (IL 1). The Journal of Immunology, 139, 788-793. [Google Scholar] [CrossRef
[5] Proosti, P., Wuytsi, A. and Van Damme, J. (1996) The Role of Chemokines in Inflammation. International Journal of Clinical and Laboratory Research, 26, 211-223. [Google Scholar] [CrossRef
[6] Matsushima, K., Baldwin, E.T. and Mukaida, N. (1992) Interleukin-8 and MCAF Novel Leukocyte Recruitment and Activating Cytokines Inducible by IL 1 and TNF. Cytokine, 1, 2-13. [Google Scholar] [CrossRef] [PubMed]
[7] Kim, Y., Jo, A.R., Jang, D.H., et al. (2012) Toll-Like Receptor 9 Mediates Oral Bacteria-Induced IL-8 Expression in Gingival Epithelial Cells. Immunology & Cell Biology, 90, 655-663. [Google Scholar] [CrossRef] [PubMed]
[8] Zhou, C., Ma, F.Z., Deng, X.J., Yuan, H. and Ma, H.S. (2008) Lactobacilli Inhibit Interleukin-8 Production Induced by Helicobacter pylori Lipopolysaccharide-Activated Toll-Like Receptor 4. World Journal of Gastroenterology, 14, 5090-5095. [Google Scholar] [CrossRef] [PubMed]
[9] Utgaard, J.O., Jahnsen, F.L., Bakka, A., Brandtzaeg, P. and Haraldsen, G. (1998) Rapid Secretion of Prestored Interleukin 8 from Weibel-Palade Bodies of Microvascular Endothelial Cells. Brief Definitive Report, 188, 1751-1756. [Google Scholar] [CrossRef] [PubMed]
[10] Wolff, B., Burns, A.R., Middleton, J. and Rot, A. (1998) Endothelial Cell “Memory” of Inflammatory Stimulation: Human Venular Endothelial Cells Store Interleukin 8 in Weibel-Palade Bodies. Brief Definitive Report, 188, November 2, 1757-1762. [Google Scholar] [CrossRef] [PubMed]
[11] Marriott, H.M., Gascoyne, K.A., Gowda, R., et al. (2011) Interleukin-1β Regulates CXCL8 Release and Influences Disease Outcome in Response to Streptococcus pneumoniae, Defining Intercellular Cooperation between Pulmonary Epithelial Cells and Macrophages. Infection and Immunity, 80, 1140-1149. [Google Scholar] [CrossRef
[12] Schmid, J. and Weissmann, C. (1987) Induction of mRNA for a Serine Protease and a Beta-Thromboglobulin-Like Protein in Mitogen-Stimulated Human Leukocytes. The Journal of Immunology, 139, 250-256. [Google Scholar] [CrossRef
[13] Matsushima, K., Morishita, K., Yoshimura, T., et al. (1988) Molecular Cloning of a Human Monocyte-Derived Neutrophil Chemotactic Factor (MDNCF) and the Induction of MDNCF mRNA by Interleukin 1 and Tumor Necrosis Factor. Journal of Experimental Medicine, 167, 1883-1893. [Google Scholar] [CrossRef] [PubMed]
[14] Hébert, C.A., Luscinskas, F.W., Kiely, J.M., et al. (1990) Endothelial and Leukocyte Forms of IL-8. Conversion by Thrombin and Interactions with Neutrophils. The Journal of Immunology, 145, 3033-3040. [Google Scholar] [CrossRef
[15] Gimbrone and Baker, J.B. (1990) Endothelial and Leukocyte Forms of IL-8. Conversion by Thrombin and Interactions with Neutrophils. The Journal of Immunology, 145, 3033-3040. [Google Scholar] [CrossRef
[16] Baggiolini, M., Dewald, B. and Moser, B. (1993) Interleukin-8 and Related Chemotactic Cytokines—CXC and CC Chemokines. Advances in Immunology, 55, 97-179. [Google Scholar] [CrossRef
[17] Mukaida, N. and Matsushima, K. (1998) Interleukin 8 and Its Receptor. In: Delves, P.J., Ed., Encyclopedia of Immunology, 2nd Edition, Elsevier, Amsterdam, 1466-1471. [Google Scholar] [CrossRef
[18] Benakanakere, M.R., Finoti, L.S., Tanaka, U., et al. (2016) Investigation of the Functional Role of Human Interleukin-8 Gene Haplotypes by CRISPR/Cas9 Mediated Genome Editing. Scientific Reports, 6, Article No. 31180. [Google Scholar] [CrossRef] [PubMed]
[19] Remick, D.G. (2005) Interleukin-8. Critical Care Medicine, 33, S466-S467. [Google Scholar] [CrossRef
[20] Flannagan, R.S., Jaumouille, V. and Grinstein, S. (2012) The Cell Biology of Phagocytosis. Annual Review of Pathology, 7, 61-98. [Google Scholar] [CrossRef] [PubMed]
[21] Lee, W.L., Harrison, R.E. and Grinstein, S. (2003) Phagocytosis by Neutrophils. Microbes and Infection, 5, 1299-1306. [Google Scholar] [CrossRef] [PubMed]
[22] Kruskal, B.A. and Maxfield, F.R. (1987) Cytosolic Free Calcium Increases before and Oscillates during Frustrated Phagocytosis in Macrophages. The Journal of Cell Biology, 105, 2685-2693. [Google Scholar] [CrossRef] [PubMed]
[23] Sawyer, D.W., Sullivan, J.A. and Mandell, G.L. (1985) Intracellular Free Calcium Localization in Neutrophils during Phagocytosis. Science, 230, 663-666. [Google Scholar] [CrossRef] [PubMed]
[24] Murphy, P.M. and Tiffany, H.L. (1991) Share Cloning of Complementary DNA Encoding a Functional Human Interleukin-8 Receptor. Science, 253, 1280-1283. [Google Scholar] [CrossRef] [PubMed]
[25] Holmes, W.E., Lee, J., Kuang, W.J., Rice, G.C. and Wood, W.I. (1991) Structure and Functional Expression of a Human Interleukin-8 Receptor. Science, 253, 1278-1280. [Google Scholar] [CrossRef] [PubMed]
[26] Cerretti, D.P., Kozlosky, C.J., VandenBos, T., Nelson, N., Gearing, D.P. and Beckmann, M.P. (1993) Molecular Characterization of Receptors for Human Interleukin-8, GRO/Melanoma Growth-Stimulatory Activity and Neutrophil Activating Peptide-2. Molecular Immunology, 30, 359-367. [Google Scholar] [CrossRef
[27] Hammond, M.E., Shyamala, V., Siani, M.A., et al. (1996) Receptor Recognition and Specificity of Interleukin-8 Is Determined by Residues That Cluster near a Surface-Accessible Hydrophobic Pocket. Journal of Biological Chemistry, 271, 8228-8235. [Google Scholar] [CrossRef] [PubMed]
[28] Lee, J., Horuk, R., Rice, G.C., et al. (1992) Characterization of Two High Affinity Human Interleukin-8 Receptors. Journal of Biological Chemistry, 267, 16283-16287. [Google Scholar] [CrossRef
[29] Waugh, D.J.J. and Wilson, C. (2008) The Interleukin-8 Pathway in Cancer. Clinical Cancer Research, 14, 6735-6741. [Google Scholar] [CrossRef
[30] Knall, C., Worthen, G.S. and Johnson, G.L. (1997) Interleukin 8 Stimulated Phosphatidylinositol-3-Kinase Activity Regulates the Migration of Human Neutrophils Independent of Extracellular Signal-Regulated Kinase and p38 Mitogen-Activated Protein Kinases. Proceedings of the National Academy of Sciences of the United States of America, 94, 3052-3057. [Google Scholar] [CrossRef] [PubMed]
[31] MacManus, C.F., Pettigrew, J., Seaton, A., et al. (2007) Interleukin-8 Signaling Promotes Translational Regulation of Cyclin D in Androgen-Independent Prostate Cancer Cells. Molecular Cancer Research, 5, 737-748. [Google Scholar] [CrossRef
[32] Xing, H.M., Kornfeld, K. and Muslin, A.J. (1997) The Protein Kinase KSR Interacts with 14-3-3 Protein and Raf. Current Biology, 7, 294-300. [Google Scholar] [CrossRef
[33] Knall, C., Young, S., Nick, J.A., et al. (1996) Interleukin-8 Regulation of the Ras/Raf/Mitogen-Activated Protein Kinase Pathway in Human Neutrophils. Journal of Biological Chemistry, 271, 2832-2838. [Google Scholar] [CrossRef] [PubMed]
[34] Luppi, F., Longo, A.M., de Boer, W.I., Rabe, K.F. and Hiemstra, P.S. (2007) Interleukin-8 Stimulates Cell Proliferation in Nonsmall Cell Lung Cancer through Epidermal Growth Factor Receptor Transactivation. Lung Cancer, 56, 25-33. [Google Scholar] [CrossRef] [PubMed]
[35] Venkatakrishnan, G., Salgia, R. and Groopman, J.E. (2000) Chemokine Receptors CXCR-1/2 Activate Mitogen-Activated Protein Kinase via the Epidermal Growth Factor Receptor in Ovarian Cancer Cells. Journal of Biological Chemistry, 275, 6868-6875. [Google Scholar] [CrossRef] [PubMed]
[36] Richardson, R.M., Ali, H., Pridgen, B.C., Haribabu, B. and Snyderman, R. (1998) Multiple Signaling Pathways of Human Interleukin-8 Receptor A. Independent Regulation by Phosphorylation. Journal of Biological Chemistry, 273, 10690-10695. [Google Scholar] [CrossRef] [PubMed]
[37] Nasser, M.W., Marjoram, R.J., Brown, S.L. and Richardson, R.M. (2005) Cross-Desensitization among CXCR1, CXCR2, and CCR5: Role of Protein Kinase C-ε. The Journal of Immunology, 174, 6927-6933. [Google Scholar] [CrossRef] [PubMed]
[38] Takami, M., Terry, V. and Petruzzelli, L. (2002). Signaling Pathways Involved in IL-8-Dependent Activation of Adhesion through Mac-1. The Journal of Immunology, 168, 4559-4566.[CrossRef] [PubMed]
[39] Lang, K., Niggemann, B., Zanker, K.S. and Entschladen, F. (2002) Signal Processing in Migrating T24 Human Bladder Carcinoma Cells: Role of the Autocrine Interleukin-8 Loop. International Journal of Cancer, 99, 673-680. [Google Scholar] [CrossRef] [PubMed]
[40] Schraufstatter, I.U., Trieu, K., Zhao, M., Rose, D.M., Terkeltaub, R.A. and Burger, M. (2003) IL-8 Mediated Cell Migration in Endothelial Cells Depends on Cathepsin B Activity and Transactivation of the Epidermal Growth Factor Receptor. The Journal of Immunology, 171, 6714-6722. [Google Scholar] [CrossRef] [PubMed]
[41] Hennequin, L.F., Thomas, A.P., Johnstone, C., et al. (1999) Design and Structure-Activity Relationship of a New Class of Potent VEGF Receptor Tyrosine Kinase Inhibitors. Journal of Medicinal Chemistry, 42, 5369-5389. [Google Scholar] [CrossRef] [PubMed]
[42] Fukumoto, T., Matsukawa, A., Yoshimura, T., et al. (1998) IL-8 Is an Essential Mediator of the Increased Delayed-Phase Vascular Permeability in LPS-Induced Rabbit Pleurisy. Journal of Leukocyte Biology, 63, 584-590. [Google Scholar] [CrossRef] [PubMed]
[43] Yamamoto, T., Kajikawa, O., Martin, T.R., et al. (1998) The Role of Leukocyte Emigration and IL-8 on the Development of Lipopolysaccharide-Induced Lung Injury in Rabbits. The Journal of Immunology, 161, 5704-5709. [Google Scholar] [CrossRef
[44] Petreaca, M.L., Yao, M., Lui, Y., Defea, K. and Martins-Green, M. (2007) Transactivation of Vascular Endothelial Growth Factor Receptor-2 by Interleukin-8 (IL-8/CXCL8) Is Required for IL-8/CXCL8-Induced Endothelial Permeability. Molecular Biology of the Cell, 18, 5014-5023. [Google Scholar] [CrossRef] [PubMed]
[45] Cohen-Hillel, E., Yron, I., Meshel, T., Soria, G., Attal, H. and Ben-Baruch, A. (2006) CXCL8-Induced FAK Phosphorylation via CXCR1 and CXCR2: Cytoskeleton- and Integrin-Related Mechanisms Converge with FAK Regulatory Pathways in a Receptor-Specific Manner. Cytokine, 33, 1-16. [Google Scholar] [CrossRef] [PubMed]
[46] Lee, L.F., Louie, M.C., Desai, S.J., et al. (2004) Interleukin-8 Confers Androgen-Independent Growth and Migration of LNCaP: Differential Effects of Tyrosine Kinases Src and FAK. Oncogene, 23, 2197-2205. [Google Scholar] [CrossRef] [PubMed]
[47] McFarlane, S., Seaton, A., Chacko, A., et al. (2006) Focal Adhesion Kinase Is a Key Signaling Intermediate in Interleukin-8 Promoted Chemotaxis and Adhesion of Prostate Cancer Cells to Bone Marrow Endothelium. EJC Supplements, 4, 18.
[48] Kopetz, S., Shah, A.N. and Gallick, G.E. (2007) Src Continues Aging: Current and Future Clinical Directions. Clinical Cancer Research, 13, 7232-7236. [Google Scholar] [CrossRef
[49] Siesser, P.M. and Hanks, S.K. (2006) The Signaling and Biological Implications of FAK Overexpression in Cancer. Clinical Cancer Research, 12, 3233-3237. [Google Scholar] [CrossRef
[50] Hecker, T.P., Grammer, J.R., Gillespie, G.Y., Stewart, J. and Gladson, C.L. (2002) Focal Adhesion Kinase Enhances Signaling through the Shc/Extracellular Signal-Regulated Kinase Pathway in Anaplastic Astrocytoma Tumor Biopsy Samples. Cancer Research, 62, 2699-2707.
[51] Pories, S.E., Hess, D.T., Swenson, K., et al. (1998) Overexpression of pp60c-src Elicits Invasive Behavior in Rat Colon Epithelial Cells. Gastroenterology, 114, 1287-1295. [Google Scholar] [CrossRef
[52] Irby, R., Mao, W., Coppola, D., et al. (1997) Overexpression of Normal c-Src in Poorly Metastatic Human Colon Cancer Cells Enhances Primary Tumor Growth but Not Metastatic Potential. Cell Growth and Differentiation, 8, 1287-1295.
[53] Ning, Y., Manegold, P.C., Hong, Y.K., et al. (2011) Interleukin-8 Is Associated with Proliferation, Migration, Angiogenesis and Chemosensitivity in Vitro and in Vivo in Colon Cancer Cell Line Models. International Journal of Cancer, 128, 2038-2049. [Google Scholar] [CrossRef] [PubMed]
[54] Roche, S., Fumagalli, S. and Courtneidge, S.A. (1995) Requirement for Src Family Protein Tyrosine Kinases in GZ for Fibroblast Cell Division. Science, 269, 1567-1569. [Google Scholar] [CrossRef] [PubMed]
[55] Legård, G.E. and Pedersen, B.K. (2019) Muscle as an Endocrine Organ. In: Zoladz, J.A., Ed., Muscle and Exercise Physiology, Elsevier, Amsterdam, 285-307. [Google Scholar] [CrossRef
[56] Hoffmann, E., Dittrich-Breiholz, O., Holtmann, H. and Kracht, M. (2002) Multiple Control of Interleukin-8 Gene Expression. Journal of Leukocyte Biology, 72, 847-855. [Google Scholar] [CrossRef
[57] Kasahara, T., Mukaida, N., Yamashita, K., et al. (1991) IL-1 and TNF-Alpha Induction of IL-8 and Monocyte Chemotactic and Activating Factor (MCAF) mRNA Expression in a Human Astrocytoma Cell Line. Immunology, 74, 60-67.
[58] Brasier, A.R., Jamaluddin, M., Casola, A., et al. (1998) A Promoter Recruitment Mechanism for Tumor Necrosis Factor-Alpha-Induced Interleukin-8 Transcription in Type II Pulmonary Epithelial Cells. Dependence on Nuclear Abundance of Rel A, NF-kappaB1, and c-Rel Transcription Factors. The Journal of Biological Chemistry, 273, 3551-3561. [Google Scholar] [CrossRef] [PubMed]
[59] Brat, D.J., Bellail, A.C. and van Meir, E.G. (2005) The Role of Interleukin-8 and Its Receptors in Gliomagenesis and Tumoral Angiogenesis. Neuro-Oncology, 7, 122-133. [Google Scholar] [CrossRef
[60] Yuzhalin, A.E. and Kutikhin, A.G. (2015) The Rest of Interleukins. In: Yuzhalin, A.E. and Kutikhin, A.G., Eds., Interleukins in Cancer Biology, Elsevier, Amsterdam, 291-318. [Google Scholar] [CrossRef
[61] Aihara, M., Tsuchimoto, D., Takizawa, H., et al. (1997) Mechanisms Involved in Helicobacter pylori-Induced Interleukin-8 Production by a Gastric Cancer Cell Line, MKN45. Infection and Immunity, 65, 3218-3224. [Google Scholar] [CrossRef] [PubMed]
[62] Hobbie, S., Chen, L.M., Davis, R.J. and Galán, J.E. (1997) Involvement of Mitogen-Activated Protein Kinase Pathways in the Nuclear Responses and Cytokine Production Induced by Salmonella typhimurium in Cultured Intestinal Epithelial Cells. The Journal of Immunology, 159, 5550-5559. [Google Scholar] [CrossRef
[63] Murayama, T., Ohara, Y., Obuchi, M., et al. (1997) Human Cytomegalovirus Induces Interleukin-8 Production by a Human Monocytic Cell Line, THP-1, through Acting Concurrently on AP-1- and NF-kappaB-Binding Sites of the Interleukin-8 Gene. Journal of Virology, 71, 5692-5695. [Google Scholar] [CrossRef] [PubMed]
[64] Shi, Q., Xiong, Q., Le, X. and Xie, K. (2001) Regulation of Interleukin-8 Expression by Tumor-Associated Stress Factors. Journal of Interferon & Cytokine Research, 21, 553-566. [Google Scholar] [CrossRef] [PubMed]
[65] Sparmann, A. and Bar-Sagi, D. (2004) Ras-Induced Interleukin-8 Expression Plays a Critical Role in Tumor Growth and Angiogenesis. Cancer Cell, 6, 447-458. [Google Scholar] [CrossRef] [PubMed]
[66] Lin, Y., Huang, R., Chen, L., Li, S., Shi, Q., Jordan, C. and Huang, R.P. (2004) Identification of Interleukin-8 as Estrogen Receptor-Regulated Factor Involved in Breast Cancer Invasion and Angiogenesis by Protein Arrays. International Journal of Cancer, 109, 507-515. [Google Scholar] [CrossRef] [PubMed]
[67] Mantovani, A., Bonecchi, R. and Locati, M. (2006) Tuning Inflammation and Immunity by Chemokine Sequestration: Decoys and More. Nature Reviews Immunology, 6, 907-918. [Google Scholar] [CrossRef] [PubMed]
[68] Greten, F.R., Eckmann, L., Greten, T.F., Park, J.M., Li, Z.W., Egan, L.J., Kagnoff, M.F. and Karin, M. (2004) IKKβ Links Inflammation and Tumorigenesis in a Mouse Model of Colitis-Associated Cancer. Cell, 118, 285-296. [Google Scholar] [CrossRef] [PubMed]
[69] Terzic, J., Grivennikov, S., Karin, E. and Karin, M. (2010) Inflammation and Colon Cancer. Gastroenterology, 138, 2101-2114e2105. [Google Scholar] [CrossRef] [PubMed]
[70] Pikarsky, E., Porat, R.M., Stein, I., Abramovitch, R., Amit, S., Kasem, S., Gutkovich-Pyest, E., Urieli-Shoval, S., Galun, E. and Ben-Neriah, Y. (2004) NF-kappaB Functions as a Tumour Promoter in Inflammation-Associated Cancer. Nature, 431, 461-466. [Google Scholar] [CrossRef] [PubMed]
[71] Karin, M., Cao, Y., Greten, F.R. and Li, Z.W. (2002) NF-kappaB in Cancer: From Innocent Bystander to Major Culprit. Nature Reviews Cancer, 2, 301-310. [Google Scholar] [CrossRef] [PubMed]
[72] Zhang, Y., Wang, L., Zhang, M., Jin, M., Bai, C. and Wang, X. (2012) Potential Mechanism of Interleukin-8 Production from Lung Cancer Cells: An Involvement of EGF-EGFR-PI3KAkt-Erk Pathway. Journal of Cellular Physiology, 227, 35-43. [Google Scholar] [CrossRef] [PubMed]
[73] Akira, S., Isshiki, H., Sugita, T., et al. (1990) A Nuclear Factor for IL-6 Expression (NF-IL6) Is a Member of a C/EBP Family. The EMBO Journal, 9, 1897-1906. [Google Scholar] [CrossRef] [PubMed]
[74] Mukaida, N., Okamoto, S., Ishikawa, Y. and Matsushima, K. (1994) Molecular Mechanism of Interleukin-8 Gene Expression. Journal of Leukocyte Biology, 56, 554-558. [Google Scholar] [CrossRef] [PubMed]
[75] Mukaida, N., Morita, M., Ishikawa, Y., Rice, N., Okamoto, S., Kasahara, T. and Matsushima, K. (1994) Novel Mechanism of Glucocorticoid-Mediated Gene Repression. Nuclear Factor-Kappa B Is Target for Glucocorticoid-Mediated Interleukin 8 Gene Repression. Journal of Biological Chemistry, 269, 13289-13295. [Google Scholar] [CrossRef
[76] Matsukaka, T., Fujikawa, K., Nishio, Y., Mukaida, N., Matsushima, K., Kishimoto, T. and Akira, S. (1993) Transcription Factors NF-IL6 and NF-kappa B Synergistically Activate Transcription of the Inflammatory Cytokines, Interleukin 6 and Interleukin 8. Proceedings of the National Academy of Sciences of the United States of America, 90, 10193-10197. [Google Scholar] [CrossRef] [PubMed]
[77] Lawrence, T. (2009) The Nuclear Factor NF-kappaB Pathway in Inflammation. Cold Spring Harbor Perspectives in Biology, 1, a001651. [Google Scholar] [CrossRef] [PubMed]
[78] Tak, P.P. and Firestein, G.S. (2001) NF-kappaB: A Key Role in Inflammatory Diseases. Journal of Clinical Investigation, 107, 7-11. [Google Scholar] [CrossRef
[79] De Zoete, M.R., Palm, N.W., Zhu, S. and Flavell, R.A. (2014) Inflammasomes. Cold Spring Harbor Perspectives in Biology, 6, a016287. [Google Scholar] [CrossRef] [PubMed]
[80] Ghosh, S., May, M.J. and Kopp, E.B. (1998) NF-κB and Rel Proteins: Evolutionarily Conserved Mediators of Immune Responses. Annual Review of Immunology, 16, 225-260. [Google Scholar] [CrossRef] [PubMed]
[81] Shi, C.S., Shenderov, K., Huang, N.N., et al. (2012) Activation of Autophagy by Inflammatory Signals Limits IL-1beta Production by Targeting Ubiquitinated Inflammasomes for Destruction. Nature Immunology, 13, 255-263. [Google Scholar] [CrossRef] [PubMed]
[82] Beinke, S. and Ley, S.C. (2004) Functions of NF-kappaB1 and NF-kappaB2 in Immune Cell Biology. Biochemical Journal, 382, 393-409. [Google Scholar] [CrossRef
[83] Lienhard Schmitz, M., Bacher, S. and Kracht, M. (2001) IκB-Independent Control of NF-κB Activity by Modulatory Phosphorylations. Trends in Biochemical Sciences, 26, 186-190. [Google Scholar] [CrossRef
[84] Neumann, M., et al. (1992) Identification of Complex Formation between Two Intracellular Tyrosine Kinase Substrates: Human c-Rel and the p105 Precursor of p50 NF-κB. Oncogene, 7, 2095-2104.
[85] Li, C.C., et al. (1994) NF-κB/Rel Family Members Are Physically Associated Phosphoproteins. Biochemical Journal, 303, 499-506. [Google Scholar] [CrossRef] [PubMed]
[86] Naumann, M. and Scheidereit, C. (1994) Activation of NF-κB in Vivo Is Regulated by Multiple Phosphorylations. EMBO Journal, 13, 4597-4607. [Google Scholar] [CrossRef] [PubMed]
[87] Heissmeyer, V., Krappmann, D., Wulczyn, F.G. and Scheidereit, C. (1999) NF-kappaB p105 Is a Target of IkappaB Kinases and Controls Signal Induction of Bcl-3-p50 Complexes. EMBO Journal, 18, 4766-4778. [Google Scholar] [CrossRef] [PubMed]
[88] Baeuerle, P.A. and Baltimore, D. (1996) NF-κB: Ten Years after. Cell, 87, 13-20. [Google Scholar] [CrossRef
[89] Sonoda, Y., Kasahara, T., Yamaguchi, Y., Kuno, K., Matsushima, K. and Mukaida, N. (1997) Stimulation of Interleukin-8 Production by Okadaic Acid and Vanadate in a Human Promyelocyte Cell Line, an HL-60 Subline. Possible Role of Mitogen-Activated Protein Kinase on the Okadaic Acid-Induced NF-kappaB Activation. Journal of Biological Chemistry, 272, 15366-15372. [Google Scholar] [CrossRef] [PubMed]
[90] DeLarco, J.E., Wuertz, B.R. and Furcht, L.T. (2004) The Potential Role of Neutrophils in Promoting the Metastatic Phenotype of Tumors Releasing Interleukin-8. Clinical Cancer Research, 10, 4895-4900. [Google Scholar] [CrossRef