Đường dẫn JAK/STAT và cơ chế phân tử trong quá trình tái tạo xương

Kawamura M, Mcvicar DW, Johnston JA, Blake TB, Chen YQ, Lal BK, Lloyd AR, Kelvin DJ, Staples JE, Ortaldo JR (1994) Molecular cloning of L-JAK, a Janus family protein-tyrosine kinase expressed in natural killer cells and activated leukocytes. Proc Natl Acad Sci USA 91:6374–6378 O’Shea JJ, Pesu M, Borie DC, Changelian PS (2004) A new modality for immunosuppression: targeting the JAK/STAT pathway. Nat Rev Drug Discov 3:555–564 Jaime-figueroa S, De Vicente J, Hermann J, Jahangir A, Jin S, Kuglstatter A, Lynch SM, Menke J, Niu L, Patel V, Shao A, Soth M, Vu MD, Yee C (2013) Discovery of a series of novel 5Hpyrrolo[2,3-b]pyrazine-2-phenyl ethers, as potent JAK3 kinase inhibitors. Bioorg Med Chem Lett 23:2522–2526 O’Shea JJ, Schwartz DM, Villarino AV, Gadina M, Mclnnes IB, Laurence A (2015) The JAK-STAT pathway: impact on human disease and therapeutic intervention. Annu Rev Med 66:311–328 Velazquez L, Fellous M, Stark GR, Pellegrini S (1992) A protein tyrosine kinase in the interferon-alpha/beta signaling pathway. Cell 70:313–322 Wilks AF (1989) Two putative protein-tyrosine kinases identified by application of the polymerase chain reaction. Proc Natl Acad Sci USA 86:1603–1607 Wilks AF, Harpur AG, Kurban RR, Ralph SJ, Zurcher G, Ziemiecki A (1991) Two novel proteintyrosine kinases, each with a second phosphotransferase- related catalytic domain, define a new class of protein kinase. Mol Cell Biol 11:2057–2065 Firmbach-Kraft I, Byers M, Shows T, Dalla-Favera R, Krolewski JJ (1990) tyk2, prototype of a novel class of non-receptor tyrosine kinase genes. Oncogene 5:1329–1336 David M, Petricoin EF, Igarashi KI, Feldman GM, Finbloom D, Larner AC (1994) Prolactin activates the Interferon-Regulated p91 transcription factor and the Jak2 Kinase by tyrosine phosphorylation. Proc Natl Acad Sci USA 91:7174–7178 Yu H, Pardoll DM, Jove R (2009) STATs in cancer inflammation and immunity: a leading role for STAT3. Nat Rev Cancer 9:798–809 Boengler K, Hilfikerkleiner D, Drexler H, Heusch G, Schulz R (2008) The myocardial JAK/STAT pathway: from protection to failure. Pharmacol Ther 120:172–185 Saeid A, Najmaldin S, Mohammad A, Asghari F, Salari F, Rahim F (2015) STATs: an old story, yet mesmerizing. Cell J 17:395–411 Gao Q, Liang X, Shaikh AS, Zang J, Xu W, Zhang Y (2018) JAK/STAT signal transduction: promising attractive targets for immune, inflammatory and hematopoietic diseases. Curr Drug Targ 19:487–500 Darnel JR (1997) STATs and gene regulation. Science 277:1630–1635 Kim SK, Park KY, Yoon WC, Park SH, Park KK, Yoo DH, Choe JY (2011) Melittin enhances apoptosis through suppression of IL-6/sIL-6R complex-induced NF-κB and STAT3 activation and Bcl-2 expression for human fibroblast-like synoviocytes in rheumatoid arthritis. Joint Bone Spine 78:471–477 Seif F, Khoshmirsafa M, Aazami H, Mohsenzadegan M, Sedighi G, Bahar M (2017) The role of JAK-STAT signaling pathway and its regulators in the fate of T helper cells. Cell Commun Sign 15:1–13 Babon JJ, Sabo JK, Zhang JG, Nicola NA, Norton RS (2009) The SOCS box encodes a hierarchy of affinities for Cullin5: implications for ubiquitin ligase formation and cytokine signalling suppression. J Mol Biol 387:162–174 Baker BJ, Akhtar LN, Benveniste EN (2009) SOCS1 and SOCS3 in the control of CNS immunity. Trends Immunol 30:392–400 Yoshimura A, Naka T, Kubo M (2007) SOCS proteins, cytokine signalling and immune regulation. Nat Rev Immunol 7:454–465 Bullock AN, Rodriguez M, Debreczeni JE, Songyang Z, Knapp S (2007) Structure of the Socs4-elonginb/C complex reveals a distinct socs box interface and the molecular basis for socs-dependent EGFR degradation. Structure 15:1493–1504 Kamura T, Maenaka K, Kotoshiba S, Matsumoto M, Kohda D, Conaway RC, Conaway JW, Nakayama KI (2004) VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases. Genes Dev 18:3055–3065 Vuong BQ, Arenzana TL, Showalter MB, Losman J, Chen XP, Mostecki J, Banks AS, Limnander A, Fernandez N, Rothman PB (2004) SOCS-1 localizes to the microtubule organizing complex-associated 20S proteasome. Mol CelL Biol 24:9092–9101 Yu ZH, Zhang ZY (2017) Regulatory mechanisms and novel therapeutic targeting strategies for protein tyrosine phosphatases. Chem Rev 118:1069–1091 Alonso A, Sasin J, Bottini N, Friedberg I, Friedberg I, Osterman A, Godzik A, Hunter T, Dixon J, Mustelin T (2004) Protein tyrosine phosphatases in the human genome. Cell 117:699–711 Huang Y, Zhang Y, Ge L, Lin Y, Kwok HF (2018) The roles of protein tyrosine phosphatases in hepatocellular carcinoma. Cancers 10:82–102 Zhang ZY (2003) Chemical and mechanistic approaches to the study of protein tyrosine phosphatases. Acc Chem Res 36:385–392 Heppler LN, Frank DA (2017) Targeting oncogenic transcription factors: therapeutic implications of endogenous STAT inhibitors. Trends Cancer 3:816–827 Hunter T (1995) Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell 80:225–236 Shuai K (2006) Regulation of cytokine signaling pathways by PIAS proteins. Cell Res 16:196–202 Dagvadorj A, Tan SH, Liao Z, Xie J, Nurmi M, Alanen K, Rui H, Mirtti T, Nevalainen MT (2010) N-terminal truncation of Stat5a/b circumvents PIAS3-mediated transcriptional inhibition of Stat5 in prostate cancer cells. Int J Biochem Cell Biol 42:2037–2046 Kipp M, Göhring F, Ostendorp T, van Drunen CM, van Driel R, Przybylski M, Fackelmayer FO (2000) SAF-Box, a conserved protein domain that specifically recognizes scaffold attachment region DNA. Mol Cell Biol 20:7480–7489 Yuan J, Zhang F, Niu R (2015) Multiple regulation pathways and pivotal biological functions of STAT3 in cancer. Sci Rep 5:17663–17672 Orsolini G, Bertoldi I, Rossini M (2020) Osteoimmunology in rheumatoid and psoriatic arthritis: potential effects of tofacitinib on bone involvement. Clin Rheumatol 39:727–736 Maruotti N, Corrado A, Rotondo C, Cantatore FP (2020) Janus kinase inhibitors role in bone remodeling. J Cell Physiol J Cell Physiol 235:1915–1920 Li J (2013) JAK-STAT and bone metabolism. JAK-STAT 2(3):e23930 Corry KA, Zhou H, Brustovetsky T, Himes ER, Bivi N, Hornd MR, Kitase Y, Wallace JM, Bellido T, Brustovetsky N, Li J (2019) Stat3 in osteocytes mediates osteogenic response to loading. Bone Rep 11:100218 Cheon YH, Kim JY, Baek JM, Ahn SJ, Jun HY, Erkhembaatar M, Kim MS, Lee MS, Oh J (2016) WHI-131 promotes osteoblast differentiation and prevents osteoclast formation and resorption in mice. J Bone Miner Res 31:403–415 Boyle WJ, Simonet WS, Lacey DL (2003) Osteoclast differentiation and activation. Nature 423:337–342 Corrado A, Sanpaolo ER, Di Bello S, Cantatore FP (2017) Osteoblast as a target of anti-osteoporotic treatment. Postgrad Med 129:858–865 Maruotti N, Corrado A, Cantatore FP (2017) Osteoblast role in osteoarthritis pathogenesis. J Cell Physiol 232:2957–2963 Otto F, Thornell AP, Crompton T, Denzel A, Gilmour KG, Rosewell IR, Stamp GW, Beddington RS, Mundlos S, Olsen BR, Selby PB, Owen MJ (1997) Cbfa1, a candidate gene for cleidocranial dysplasia syndrome, is essential for osteoblast differentiation and bone development. Cell 89:765–771 Nakashima K, Zhou X, Kunkel G, Zhang Z, Deng JM, Behringer RR, de Crombrugghe B (2002) The novel zinc fingercontaining transcription factor osterix is required for osteoblast differentiation and bone formation. Cell 108:17–29 Corrado A, Neve A, Macchiarola A, Gaudio A, Marucci A, Cantatore FP (2013) RANKL/OPG ratio and DKK-1 expression in primary osteoblastic cultures from osteoarthritic and osteoporotic subjects. J Rheumatol 40:684–694 Chen X, Wang Z, Duan N, Zhu G, Schwarz EM, Xie C (2018) Osteoblast–osteoclast interactions. Connect Tissue Res 59:99–107 Corrado A, Neve A, Cantatore FP (2013) Expression of vascular endothelial growth factor in normal, osteoarthritic and osteoporotic osteoblasts. Clin Exp Med 13:81–84 Davidson KD, Himes RE, Takigawa S, Chen A, Horn MR, Meijome T, Wallace MT, Kacena MA, Yokota H, Nguyen AV, Li J (2020) The loss of STAT3 in mature osteoclasts has detrimental effects on bone structure. PLoS ONE 15(7):e0236891 Lee ZH, Kim HH (2003) Signal transduction by receptor activator of nuclear factor kappa B in osteoclasts. Biochem Biophys Res Commun 305:211–214 Takahashi N, Yamana H, Yoshiki S, Roodman GD, Mundy GR, Jones SJ, Boyde A, Suda T (1988) Osteoclast-like cell formation and its regulation by osteotropic hormones in mouse bone marrow cultures. Endocrinology 122:1373–1382 Yasuda H, Shima N, Nakagawa N, Yamaguchi K, Kinosaki M, Mochizuki S, Tomoyasu A, Yano K, Goto M, Murakami A, Tsuda E, Morinaga T, Higashio K, Udagawa N, Takahashi N, Suda T (1998) Osteoclast differentiation factor is a ligand for osteoprotegerin/osteoclastogenesis inhibitory factor and is identical to TRANCE/RANKL. Proc Natl Acad Sci USA 95:3597–3602 Lacey DL, Timms E, Tan HL, Kelley MJ, Dunstan CR, Burgess T, Elliott R, Colombero A, Elliott G, Scully S, Hsu H, Sullivan J, Hawkins N, Davy E, Capparelli C, Eli A, Qian YX, Kaufman S, Sarosi I, Shalhoub V, Senaldi G, Guo J, Delaney J, Boyle WJ (1998) Osteoprotegerin ligand is a cytokine that regulates osteoclast differentiation and activation. Cell 93:165–176 Byung-Chul J, Jung Ha K, Kabsun K, Inyoung K, Semun S, Nacksung K (2017) ATF3 modulates calcium signaling in osteoclast differentiation and activity by associating with c-Fos and NFATc1 proteins. Bone 95:33–40 Hikata T, Takaishi H, Takito J, Hakozaki A, Furukawa M, Uchikawa S, Kimura T, Okada Y, Matsumoto M, Yoshimura A, Nishimura R, Reddy SV, Asahara H, Toyama Y (2009) PIAS3 negatively regulates RANKL-mediated osteoclastogenesis directly in osteoclast precursors and indirectly via osteoblasts. Blood 113:2202–2212 Kim K, Lee J, Kim JH, Jin HM, Zhou B, Lee SY, Kim N (2007) Protein inhibitor of activated STAT 3 modulates osteoclastogenesis by down-regulation of NFATc1 and osteoclast-associated receptor. J Immunol 178:5588–5594 Takayanagi H, Kim S, Koga T, Nishina H, Isshiki M, Yoshida H, Saiura A, Isobe M, Yokochi T, Inoue J, Wagner EF, Mak TW, Kodama T, Taniguchi T (2002) Induction and activation of the transcription factor NFATc1 (NFAT2) integrate RANKL signaling in terminal differentiation of osteoclasts. Dev Cell 3:889–901 Levy JB, Schindler C, Raz R, Levy DE, Baron R, Horowitz MC (1996) Activation of the JAK-STAT signal transduction pathway by oncostatin-M cultured human and mouse osteoblastic cells. Endocrinology 137:1159–1165 Verbsky JW, Bach EA, Fang YF, Yang L, Randolph DA, Fields LE (1996) Expression of Janus kinase 3 in human endothelial and other non-lymphoid and non-myeloid cells. J Biol Chem 271:13976–13980 Tortolani PJ, Lal BK, Riva A, Johnston JA, Chen YQ, Reaman GH, Beckwith M, Longo D, Ortaldo JR, Bhatia K, McGrath I, Kehrl J, Tuscano J, McVicar DW, O’Shea JJ (1995) Regulation of JAK3 expression and activation in human B cells and B cell malignancies. J Immunol 155:5220–5226 Sharfe N, Dadi HK, O’Shea JJ, Roifman CM (1997) Jak3 activation in human lymphocyte precursor cells. Clin Exp Immunol 108:552–556. https://doi.org/10.1046/j.1365-2249.1997.4001304.x Musso T, Johnston JA, Linnekin D, Varesio L, Rowe TK, O’Shea JJ, McVicar DW (1995) Regulation of JAK3 expression in human monocytes: phosphorylation in response to interleukins 2, 4, and 7. J Exp Med 181:1425–1431 Rodig SJ, Meraz MA, White JM, Lampe PA, Riley JK, Arthur CD, King KL, Sheehan KC, Yin L, Pennica D, Johnson EM, Schreiber RD (1998) Disruption of the Jak1 gene demonstrates obligatory and nonredundant roles of the Jaks in cytokine-induced biologic responses. Cell 93:373–383 Parganas E, Wang D, Stravopodis D, Topham DJ, Marine JC, Teglund S, Vanin EF, Bodner S, Colamonici OR, van Deursen JM, Grosveld G, Ihle JN (1998) Jak2 is essential for signaling through a variety of cytokine receptors. Cell 93:385–395 Neubauer H, Cumano A, Müller M, Wu H, Huffstadt U, Pfeffer K (1998) Jak2 deficiency defines an essential developmental checkpoint in definitive hematopoiesis. Cell 93:397–409 Joung YH, Lim EJ, Pramod D, Chung SC, Jang JW, Do Park J, Lee HK, Kim HS, Cho BW, Park T, Chung S, Park JH, Yang YM (2013) HSE enhances BMP7 and GH signaling through the activation of Jak2/STAT5B in osteoblastic MC3T3-E1 cells. Mol Med Rep 8:891–896 Laviola L, Natalicchio A, Giorgino F (2007) The IGF-I signaling pathway. Curr Pharm Des 13:663–669 Rosen CJ (2004) Insulin-like growth factor I and bone mineral density: experience from animal models and human observational studies. Best Pract Res Clin Endocrinol Metab 18:423–435 Miyazono K, Maeda S, Imamura T (2004) Coordinate regulation of cell growth and differentiation by TGFbeta superfamily and Runx proteins. Oncogene 23:4232–4237 Ziros PG, Georgakopoulos T, Habeos I, Basdra EK, Papavassiliou AG (2004) Growth hormone attenuates the transcriptional activity of Runx2 by facilitating its physical association with Stat3β. J Bone Miner Res 19:1892–1904 Govoni KE, Lee SK, Chadwick RB, Yu H, Kasukawa Y, Baylink DJ, Mohan S (2006) Whole genome microarray analysis of growth hormone-induced gene expression in bone: T-box3, a novel transcription factor, regulates osteoblast proliferation. Am J Physiol Endocrinol Metab 291:E128–E136 Govoni KE, Linares GR, Chen ST, Pourteymoor S, Mohan S (2009) T-box 3 negatively regulates osteoblast differentiation by inhibiting expression of osterix and runx2. J Cell Biochem 106:482–490 Walker JG, Ahern MJ, Coleman M, Weedon H, Papangelis V, Beroukas D, Roberts-Thomson PJ, Smith MD (2006) Expression of Jak3, STAT1, STAT4, and STAT6 in inflammatory arthritis: unique Jak3 and STAT4 expression in dendritic cells in seropositive rheumatoid arthritis. Ann Rheum Dis 65:149–156 LaBranche TP, Jesson MI, Radi ZA, Storer CE, Guzova JA, Bonar SL, Thompson JM, Happa FA, Stewart ZS, Zhan Y, Bollinger CS, Bansal PN, Wellen JW, Wilkie DP, Bailey SA, Symanowicz PT, Hegen M, Head RD, Kishore N, Mbalaviele G, Meyer DM (2012) JAK inhibition with Tofacitinib suppresses arthritic joint structural damage through decreased RANKL production. Arthritis Rheum 64(11):3531–3542 Vidal B, Cascão R, Finnilä MAJ, Lopes IP, da Glória VG, Saarakkala S, Zioupos P, Canhão H, Fonseca JE (2019) Effects of tofacitinib in early arthritis-induced bone loss in an adjuvant-induced arthritis rat model. Rheumatology (Oxford) 58(2):371 Li CH, Xu LL, Jian LL, Yu RH, Zhao JX, Sun L, Du GH, Liu XY (2018) Stattic inhibits RANKL-mediated osteoclastogenesis by suppressing activation of STAT3 and NF-κB pathways. Int Immunopharmacol 58:136–144 Park JS, Kwok SK, Lim MA, Kim EK, Ryu JG, Kim SM, Oh HJ, Ju JH, Park SH, Kim HY, Cho ML (2014) STA-21, a promising STAT-3 inhibitor that reciprocally regulates Th17 and Treg cells, inhibits osteoclastogenesis in mice and humans and alleviates autoimmune inflammation in an experimental model of rheumatoid arthritis. Arthritis Rheumatol 66(4):918–929 Takayanagi H, Kim S, Matsuo K, Suzuki H, Suzuki T, Sato K, Yokochi T, Oda H, Nakamura K, Ida N, Wagner EF, Taniguchi T (2002) RANKL maintains bone homeostasis through c-Fos-dependent induc-tion of interferon-beta. Nature 416:744–749 Takayanagi H, Ogasawara K, Hida S, Chiba T, Murata S, Sato K, Takaoka A, Yokochi T, Oda H, Tanaka K, Nakamura K, Taniguchi T (2000) T-cell-mediated regulation of osteoclastogenesis by signalling cross-talk between RANKL and IFN-gamma. Nature 408:600–605 Kim S, Koga T, Isobe M, Kern BE, Yokochi T, Chin YE, Karsenty G, Taniguchi T, Takayanagi H (2003) Stat1 functions as acytoplasmic attenuator of Runx2 in the transcriptionalprogram of osteoblast differentiation. Genes Dev 17:1979–1991 Tajima K, Takaishi H, Takito J, Tohmonda T, Yoda M, Ota N, Kosaki N, Matsumoto M, Ikegami H, Nakamura T, Kimura T, Okada Y, Horiuchi K, Chiba K, Toyama Y (2010) Inhibition of STAT1 Accelerates Bone Fracture Healing. Wiley Periodicals Inc J OrthopRes 28:937–941 Xu L, Zhang L, Zhang H, Yang Z, Qi L, Wang Y, Ren S (2018) The participation of fibroblast growth factor 23 (FGF23) in the progression of osteoporosis via JAK/STAT pathway. J Cell Biochem 119(5):3819–3828 Nadiminty N, Lou W, Lee SO, Lin X, Trump DL, Gao AC (2006) Stat3 activation of NF-kappaB p100 processing involves CBP/p300-mediated acetylation. Proc Natl Acad Sci USA 103:7264–7269 Nicolaidou V, Wong MM, Redpath AN, Ersek A, Baban DF, Williams LM, Cope AP, Horwood NJ (2012) Monocytes induce STAT3 activation in human mesenchymal stem cells to promote osteoblast formation. PLoS ONE 7(7):e39871. https://doi.org/10.1371/journal.pone.0039871 Pan J, Fukuda K, Saito M, Matsuzaki J, Kodama H, Sano M, Takahashi T, Kato T, Ogawa S (1999) Mechanical stretch activates the JAK/STAT pathway in rat cardiomyocytes. Circ Res 84:1127–1136 Zhou H, Newnum AB, Martin JR, Li P, Nelson MT, Moh A, Fu Y, Yokota H, Li J (2011) Osteoblast/osteocyte-specific inactivation of Stat3 decreases load-driven bone formation and accumulates reactive oxygen species. Bone 49:404–411 Itoh S, Udagawa N, Takahashi N, Yoshitake F, Narita H, Ebisu S, Ishihara K (2006) A critical role for interleukin-6 family-mediated Stat3 activation in osteoblast differentiation and bone formation. Bone 39:505–512 Welte T, Zhang SS, Wang T, Zhang Z, Hesslein DG, Yin Z, Kano A, Iwamoto Y, Li E, Craft JE, Bothwell ALM, Fikrig E, Koni P, Flavell RA, Fu XY (2003) STAT3 deletion during hematopoiesis causes Crohn’s disease-like pathogenesis and lethality: a critical role of STAT3 in innate immunity. Proc Natl Acad Sci USA 100:1879–1884 Grimbacher B, Holland SM, Gallin JI, Greenberg F, Hill SC, Malech HL, Miller JA, O’Connell AC, Puck JM (1999) Hyper-IgE syndrome with recurrent infections–an autosomal dominant multisystem disorder. N Engl J Med 340:692–702 Holland SM, DeLeo FR, Elloumi HZ, Hsu AP, Uzel G, Brodsky N, Freeman AF, Demidowich A, Davis J, Turner ML, Anderson VL, Darnell DN, Welch PA, Kuhns D, Frucht DM, Malech HL, Gallin JI, Kobayashi SD, Whitney AR, Voyich JM, Musser JM, Woellner C, Schäffer AS, Puck JM, Grimbacher B (2007) STAT3 mutations in the hyper-IgE syndrome. N Engl J Med 357:1608–1619 Grimbacher B, Puck JM, Holland SM (2007) Hyper-IgE recurrent infections syndrome. In: Ochs HD, Smith CIE, Puck JM (eds) Primary immunodeficiency diseases: a molecular & cellular approach. Oxford University Press Inc, New York City, pp 496–504 Minegishi Y, Saito M, Tsuchiya S, Tsuge I, Takada H, Hara T, Kawamura N, Ariga T, Pasic S, Stojkovic O, Metin A, Karasuyama H (2007) Dominant-negative mutations in the DNA-binding domain of STAT3 cause hyper-IgE syndrome. Nature 448:1058–1062 Yang Y, Chung MR, Zhou S, Gong X, Xu H, Hong Y, Jin A, Huang X, Zou W, Dai Q, Jiang J (2019) STAT3 controls osteoclast differentiation and bone homeostasis by regulating NFATc1 transcription. J Biol Chem 294:15395–15407 Gadina M, Johnson C, Schwartz D, Bonelli M, Hasni S, Kanno Y, O’Shea JJ (2018) Translational and clinical advances in JAK-STAT biology: the present and future of jakinibs. J Leukoc Biol 104:499–514 Villarino AV, Kanno Y, Ferdinand JR, O’Shea JJ (2015) Mechanisms of Jak/STAT signaling in immunity and disease. J Immunol 194:21–27 Manolagas SC, Jilka RL (1995) Bone marrow, cytokines, and bone remodeling. Emerging insights into the pathophysiology of osteoporosis. N Engl J Med 332:305–311 McGregor NE, Murat M, Elango J, Poulton IJ, Walker EC, Crimeen-Irwin B, Ho PWM, Gooi JH, Martin TJ, Sims NA (2019) IL-6 exhibits both cis and trans signaling in osteocytes and osteoblasts, but only trans signaling promotes bone formation and osteoclastogenesis. J Biol Chem 294:7850–7863 Bellido T, Stahl N, Farruggella TJ, Borba V, Yancopoulos GD, Manolagas SC (1996) Detection of receptors for interleukin-6, interleukin-11, leukemia inhibitory factor, oncostatin M, and ciliary neurotrophic factor in bone marrow stromal/osteoblastic cells. J Clin Invest 97:431–437 Kishimoto T (1989) The biology of interleukin-6. Blood 74:1–10 Wu Q, Zhou X, Huang D, Ji Y, Kang F (2017) IL-6 enhances osteocyte-mediated osteoclastogenesis by promoting JAK2 and RANKL activity in vitro. Cell Physiol Biochem 41(1360):1369 Romas E, Udagawa N, Zhou H, Tamura T, Saito M, Taga T, Hilton DJ, Suda T, Ng KW, Martin TJ (1996) The role of gp130-mediated signals in osteoclast development: regulation of interleukin 11 production by osteoblasts and distribution of its receptor in bone marrow cultures. J Exp Med 183:2581–2591 Ishimi Y, Miyaura C, Jin CH, Akatsu T, Abe E, Nakamura Y, Yamaguchi A, Yoshiki S, Matsuda T, Hirano T (1990) IL-6 is produced by osteoblasts and induces bone resorption. J Immunol 145:3297–3303 Kim JH, Jin HM, Kim K, Song I, Youn BU, Matsuo K, Kim K (2009) The mechanism of osteoclast differentiation induced by IL-1. J Immunol 183:1862–1870 Khapli SM, Mangashetti LS, Yogesha SD, Wani MR (2003) IL-3 acts directly on osteoclast precursors and irreversibly inhibits receptor activator of NF-kB ligand-induced osteoclast differentiation by diverting the cells to macrophage lineage. J Immunol 171:142–151 Yogesha SD, Khapli SM, Srivastava RK, Mangashetti LS, Pote ST, Mishra GC, Wani MR (2009) IL-3 inhibits TNF-a-induced bone resorption and prevents inflammatory arthritis. J Immunol 182:361–370 Singh K, Piprode V, Mhaske ST, Barhanpurkar-Naik A, Wani MR (2018) IL-3 differentially regulates membrane and soluble RANKL in osteoblasts through metalloproteases and the JAK2/STAT5 pathway and improves the RANKL/OPG ratio in adult mice. J Immunol 200:595–606 Gupta N, Barhanpurkar AP, Tomar GB, Srivastava RK, Kour S, Pote ST, Mishra GC, Wani MR (2010) IL-3 inhibits human osteoclastogenesis and bone resorption through downregulation of c-Fms and diverts the cells to dendritic cell lineage. J Immunol 185:2261–2272 Barhanpurkar AP, Gupta N, Srivastava RK, Tomar GB, Naik SN, Joshi SR, Pote ST, Mishra GC, Wani MR (2012) IL-3 promotes osteoblast differentiation and bone formation in human mesenchymal stem cells. Biochem Biophys Res Commun 418:669–675 Abu-Amer Y (2001) IL-4 abrogates osteoclastogenesis through STAT6-dependent inhibition of NF-kappaB. J Clin Invest 107:1375–1385 Yamada A, Takami M, Kawawa T, Yasuhara R, Zhao B, Mochizuki A, Miyamoto Y, Eto T, Yasuda H, NakamichI Y, Kim N, Katagiri T, Suda T, Kamijo R (2007) Interleukin-4 inhibition of osteoclast differentiation is stronger than that of interleukin-13 and they are equivalent for induction of osteoprotegerin production from osteoblasts. Immunology 120:573–579 Kim J-H, Sim JH, Lee S, Seol MA, Ye S-K, Shin HM, Lee EB, Lee YJ, Choi YJ, Yoo W-H, Kim JH, Kim W-U, Lee D-S, Kim J-H, Kang I, Kang SW, Kim H-R (2017) Interleukin-7 induces osteoclast formation via STAT5, independent of receptor activator of NF-kappaB ligand. Front Immunol 8:1376 Nagata N, Kitaura H, Yoshida N, Nakayama K (2003) Inhibition of RANKL-induced osteoclast formation in mouse bone marrow cells by IL-12: involvement of IFN-gamma possibly induced from non-T cell population. Bone 33:721–732 Horwood NJ, Elliott J, Martin TJ, Gillespie MT (2001) IL- 12 alone and in synergy with IL-18 inhibits osteoclast formation in vitro. J Immunol 166:4915–4921 Zou J, Presky DH, Wu CY, Gubler U (1997) Differential associations between the cytoplasmic regions of the interleukin-12 receptor subunits beta1 and beta2 and JAK kinases. J Biol Chem 272:6073–6077 Djaafar S, Pierroz DD, Chicheportiche R, Zheng XX, Ferrari SL, Ferrari-Lacraz S (2010) Inhibition of T cell-dependent and RANKL-dependent osteoclastogenic processes associated with high levels of bone mass in interleukin-15 receptor-deficient mice. Arthritis Rheum 62:3300–3310 Raychaudhuri SP, Raychaudhuri SK (2017) Mechanistic rationales for targeting interleukin-17A in spondyloarthritis. Arthritis Res Ther 19:51 Lubberts E (2015) The IL-23-IL-17 axis in inflammatory arthritis. Nat Rev Rheumatol 11:415–429 Jo S, Wang SE, Lee YL, Kang S, Lee B, Han J, Sung IH, Park YS, Bae SC, Kim TH (2018) IL-17A induces osteoblast differentiation by activating JAK2/STAT3 in ankylosing spondylitis. Arthritis Res Ther 20:115 Kamiya S, Nakamura C, Ono TFK, Ohwaki T, Wada TYS (2007) Effects of IL-23 and IL-27 on osteoblasts and osteoclasts: inhibitory effects on osteoclast differentiation. J Bone Miner Metab 25:277–285