The JNK Are Important for Development and Survival of Macrophages
Abstract
We report in this study that activation of the JNK by the growth factor, CSF-1 is critical for macrophage development, proliferation, and survival. Inhibition of JNK with two distinct classes of inhibitors, the pharmacological agent SP600125, or the peptide D-JNKI1 resulted in cell cycle inhibition with an arrest at the G2/M transition and subsequent apoptosis. JNK inhibition resulted in decreased expression of CSF-1R (c-fms) and Bcl-xL mRNA in mature macrophages and repressed CSF-1-dependent differentiation of bone marrow cells to macrophages. Macrophage sensitivity to JNK inhibitors may be linked to phosphorylation of the PU.1 transcription factor. Inhibition of JNK disrupted PU.1 binding to an element in the c-fms gene promoter and decreased promoter activity. Promoter activity could be restored by overexpression of PU.1. A comparison of expression profiles of macrophages with 22 other tissue types showed that genes that signal JNK activation downstream of tyrosine kinase receptors, such as focal adhesion kinase, Nck-interacting kinase, and Rac1 and scaffold proteins are highly expressed in macrophages relative to other tissues. This pattern of expression may underlie the novel role of JNK in macrophages.
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Signal transduction by the JNK group of MAP kinases
Davis, R. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00116-1 · Cited by 4,237 · see citing works
Schreiber, E. H., Matthias, P., Müller, M. M., & Schaffner, W. (1989) · Nucleic Acids Research · doi:10.1093/nar/17.15.6419 · Cited by 4,179 · see citing works
Vlahos, C. J., Matter, W. F., Hui, K. Y., & Brown, R. F. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37680-9 · Cited by 3,248 · see citing works
A synthetic inhibitor of the mitogen-activated protein kinase cascade.
Dudley, D. T., Pang, L., Decker, S. J., Bridges, A. J., & Saltiel, A. R. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.17.7686 · Cited by 2,679 · see citing works
Amino Acid Sequences Common to Rapidly Degraded Proteins: The PEST Hypothesis
Rogers, S. W., Wells, R., & RECHSTEINER, M. C. (1986) · Science · doi:10.1126/science.2876518 · Cited by 2,565 · see citing works
Signal transduction by the c-Jun N-terminal kinase (JNK) — from inflammation to development
Ip, Y. T., & Davis, R. J. (1998) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(98)80143-9 · Cited by 1,538 · see citing works
Selective interaction of JNK protein kinase isoforms with transcription factors.
Gupta, S., Barrett, T., Whitmarsh, A. J., Cavanagh, J., Sluss, H. K., Dérijard, B., & Davis, R. J. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00636.x · Cited by 1,341 · see citing works
Dai, X.-M., Ryan, G. R., Hapel, A. J., Dominguez, M. G., Russell, R. G., Kapp, S., Sylvestre, V., & Stanley, E. R. (2002) · Blood · doi:10.1182/blood.v99.1.111 · Cited by 1,184 · see citing works
Targeted disruption of the PU.1 gene results in multiple hematopoietic abnormalities
McKercher, S. R., Torbett, B. E., Anderson, K. L., Henkel, G. W., Vestal, D. J., Baribault, H., Klemsz, M., Feeney, A. J., Wu, G. E., Paige, C. J., et al. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00949.x · Cited by 1,130 · see citing works
Smeal, T., Binetruy, B., Mercola, D. A., Birrer, M., & Karin, M. (1991) · Nature · doi:10.1038/354494a0 · Cited by 789 · see citing works
Han, Z., Boyle, D. L., Chang, L., Bennett, B. L., Karin, M., Yang, L., Manning, A. M., & Firestein, G. S. (2001) · Journal of Clinical Investigation · doi:10.1172/jci12466 · Cited by 781 · see citing works
c‐Jun regulates cell cycle progression and apoptosis by distinct mechanisms
Wisdom, R., Johnson, R. S., & Moore, C. (1999) · The EMBO Journal · doi:10.1093/emboj/18.1.188 · Cited by 687 · see citing works
Sasmono, R. T., Oceandy, D., Pollard, J. W., Tong, W., Pavli, P., Wainwright, B. J., Ostrowski, M. C., Himes, S. R., & Hume, D. A. (2003) · Blood · doi:10.1182/blood-2002-02-0569 · Cited by 662 · see citing works
Self-citationDefective T Cell Differentiation in the Absence of Jnk1
Dong, C., Yang, D. D., Wysk, M., Whitmarsh, A. J., Davis, R. J., & Flavell, R. A. (1998) · Science · doi:10.1126/science.282.5396.2092 · Cited by 579 · see citing works
Control of cell cycle progression by c-Jun is p53 dependentPreprint
Schreiber, M., Kolbus, A., Piu, F., Szabowski, A., Möhle-Steinlein, U., Tian, J., Karin, M., Angel, P., & Wagner, E. F. (1999) · Genes & Development · doi:10.1101/gad.13.5.607 · Cited by 576 · see citing works
Cell-Permeable Peptide Inhibitors of JNK
Bonny, C., Oberson, A., Negri, S., Sauser, C., & Schorderet, D. F. (2001) · Diabetes · doi:10.2337/diabetes.50.1.77 · Cited by 571 · see citing works
Activation of c-Jun N-terminal kinase in bacterial lipopolysaccharide-stimulated macrophages.
Hambleton, J., Weinstein, S. L., Lem, L., & DeFranco, A. L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.7.2774 · Cited by 471 · see citing works
Statistical Issues in cDNA Microarray Data Analysis
Smyth, G. K., Yang, J. Y. H., & Speed, T. P. (2003) · Humana Press eBooks · doi:10.1385/1-59259-364-x:111 · Cited by 463 · see citing works
Differentiation of CD4+ T Cells to Th1 Cells Requires MAP Kinase JNK2
Yang, D. D., Conze, D. B., Whitmarsh, A. J., Barrett, T., Davis, R. J., Rincón, M., & Flavell, R. A. (1998) · Immunity · doi:10.1016/s1074-7613(00)80640-8 · Cited by 453 · see citing works
The jun and fos protein families are both required for cell cycle progression in fibroblasts.
Kovary, K., & Bravo, R. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.9.4466 · Cited by 436 · see citing works
p110δ, a novel phosphoinositide 3-kinase in leukocytes
Vanhaesebroeck, B., Welham, M. J., Kotani, K., Stein, R. C., Warne, P. H., Zvelebil, M., Higashi, K., Volinia, S., Downward, J., & Waterfield, M. D. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.9.4330 · Cited by 434 · see citing works
Zhang, D. E., Hetherington, C. J., Chen, H. M., & Tenen, D. G. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.1.373 · Cited by 411 · see citing works
Zhang, D.-E., Hetherington, C. J., Chen, H.-M., & Tenen, D. G. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.1.373-381.1994 · Cited by 411 · see citing works
Almeida, E. A. C., Ilić, D., Han, Q., Hauck, C. R., Jin, F., Kawakatsu, H., Schlaepfer, D. D., & Damsky, C. H. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.3.741 · Cited by 355 · see citing works
Chen, J., Fujii, K., Zhang, L., Roberts, T. M., & Fu, H. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.141224398 · Cited by 316 · see citing works
Oktay, M. H., Wary, K. K., Dans, M. J., Birge, R. B., & Giancotti, F. G. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.145.7.1461 · Cited by 276 · see citing works
Zheng, B., Fiumara, P. F., Li, Y. V., Georgakis, G. V., Snell, V., Younes, M., Vauthey, J., Carbone, A., & Younes, A. (2003) · Blood · doi:10.1182/blood-2002-11-3507 · Cited by 213 · see citing works
Transcription factors that regulate monocyte/macrophage differentiation
Valledor, A. F., Borràs, F. E., Cullell-Young, M., & Celada, A. (1998) · Journal of Leukocyte Biology · doi:10.1002/jlb.63.4.405 · Cited by 211 · see citing works
Miki, R., Kadota, K., Bono, H. U., Mizuno, Y., Tomaru, Y., Carninci, P., Itoh, M., Shibata, K., Kawai, J., Konno, H., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.041605498 · Cited by 200 · see citing works
Myeloid Development Is Selectively Disrupted in PU.1 Null Mice
Anderson, K. L., Smith, K. A., Conners, K., McKercher, S. R., Maki, R. A., & Torbett, B. E. (1998) · Blood · doi:10.1182/blood.v91.10.3702 · Cited by 193 · see citing works
Li, W., Hu, P. J., Skolnik, E. Y., Ullrich, A., & Schlessinger, J. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.12.5824 · Cited by 175 · see citing works
Survival signaling mediated by c-Jun NH2-terminal kinase in transformed B lymphoblasts
Hess, P., Pihan, G. A., Sawyers, C. L., Flavell, R. A., & Davis, R. J. (2002) · Nature Genetics · doi:10.1038/ng946 · Cited by 165 · see citing works
The transcription factor PU.1 is involved in macrophage proliferation.
Celada, A., Borràs, F. E., Soler, C., Lloberas, J., Klemsz, M., van Beveren, C., McKercher, S., & Maki, R. A. (1996) · The Journal of experimental medicine · doi:10.1084/jem.184.1.61 · Cited by 161 · cited 1× · see citing works
“1 transcription factor has been shown to effect proliferation of BMMs in a CSF-1-dependent manner, and decreased proliferation of BMMs in response to JNK inhibition may partially occur through repression of c-fms gene expression (54) (Fig.”
BackgroundLanger, S. J., Bortner, D. M., Roussel, M. F., Sherr, C. J., & Ostrowski, M. C. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.12.5355-5362.1992 · Cited by 146 · see citing works
Shurtleff, S. A., Downing, J. R., Rock, C. O., et al. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07417.x · Cited by 145 · see citing works
Valledor, A. F., Comalada, M., Xaus, J., & Celada, A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.10.7403 · Cited by 135 · see citing works
Stacey, K. J., Fowles, L., Colman, M. S., Ostrowski, M. C., & Hume, D. A. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.6.3430 · Cited by 128 · see citing works
Self-citationRescue of defective mitogenic signaling by D-type cyclins.
Roussel, M. F., Theodoras, A. M., Pagano, M., & Sherr, C. J. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.15.6837 · Cited by 111 · see citing works
Fowles, L., Martin, M. L., Nelsen, L., Stacey, K. J., Redd, D., Clark, Y. M., Nagamine, Y., McMahon, M., Hume, D. A., & Ostrowski, M. C. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.9.5148 · Cited by 104 · see citing works
Self-citationSevilla, L., Aperlo, C., Dulić, V., Chambard, J., Boutonnet, C., Pasquier, O., Pognonec, P., & Boulukos, K. E. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.4.2624 · Cited by 97 · see citing works
Rehli, M., den Elzen, N. R., Cassady, A. I., Ostrowski, M. C., & Hume, D. A. (1999) · Genomics · doi:10.1006/geno.1998.5588 · Cited by 95 · see citing works
Self-citationDreskin, S. C., Thomas, G. W., Dale, S. N., & Heasley, L. E. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.9.5646 · Cited by 95 · see citing works
Inhibition of c-jun causes reversible proliferative arrest and withdrawal from the cell cycle
Smith, M., & Prochownik, E. (1992) · Blood · doi:10.1182/blood.v79.8.2107.2107 · Cited by 84 · see citing works
Wang, J.-M., Lai, M.-Z., & Yang-Yen, H.-F. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.6.1896-1909.2003 · Cited by 83 · see citing works
A highly conserved c-fmsgene intronic element controls macrophage-specific and regulated expression
Himes, S. R., Tagoh, H., Goonetilleke, N., Sasmono, R. T., Oceandy, D., Clark, R. J., Bonifer, C., & Hume, D. A. (2001) · Journal of Leukocyte Biology · doi:10.1189/jlb.70.5.812 · Cited by 79 · see citing works
Self-citationRoss, I. L., Xie, Y., Ostrowski, M. C., & Hume, D. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.12.6662 · Cited by 78 · see citing works
Self-citationThe Jun and Fos Protein Families Are Both Required for Cell Cycle Progression in Fibroblasts
Kovary, K., & Bravo, R. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.9.4466-4472.1991 · Cited by 77 · see citing works
Smith, J. L., Schaffner, A. E., Hofmeister, J. K., Hartman, M. S., Guo, W., Forsthoefel, D. J., Hume, D. A., & Ostrowski, M. C. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.21.8026-8034.2000 · Cited by 72 · see citing works
Self-citationInhibition of c-jun causes reversible proliferative arrest and withdrawal from the cell cycle
Smith, M., & Prochownik, E. (1992) · Blood · doi:10.1182/blood.v79.8.2107.bloodjournal7982107 · Cited by 64 · see citing works
Jaworowski, A., Wilson, N. J., Christy, E., Byrne, R. A., & Hamilton, J. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.21.15127 · Cited by 61 · see citing works
Sevilla, L., Zaldumbide, A., Carlotti, F., Dayem, M. A., Pognonec, P., & Boulukos, K. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008270200 · Cited by 60 · see citing works
Caraglia, M., Tagliaferri, P., Marra, M., Giuberti, G., Budillon, A., Gennaro, E. D., Pepe, S., Vitale, G., Improta, S., Tassone, P., et al. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401131 · Cited by 59 · see citing works
Octamer Binding Factors and Their Coactivator Can Activate the Murine PU.1 (spi-1) Promoter
Chen, H.-M., Zhang, P., Radomska, H. S., Hetherington, C. J., Zhang, D.-E., & Tenen, D. G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.26.15743 · Cited by 59 · see citing works
c-Jun-NH2 Kinase (JNK) Contributes to the Regulation of c-Myc Protein Stability
Alarcon-Vargas, D., & Ronai, Z. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312054200 · Cited by 59 · see citing works
Ross, I. L., Dunn, T. L., Yue, X., Himes, S. R., Barnett, C. J. K., & Hume, D. A. (1994) · PubMed · Cited by 57 · see citing works
Self-citationSelective Involvement of p130Cas/Crk/Pyk2/c-Src in Endothelin-1-Induced JNK Activation
Kodama, H., Fukuda, K., Takahashi, E., et al. (2003) · Hypertension · doi:10.1161/01.hyp.0000069698.11814.f4 · Cited by 55 · see citing works
Colony‐stimulating factor‐1 receptor (c‐fms)
Sherr, C. J., Roussel, M. F., & Rettenmier, C. W. (1988) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240380305 · Cited by 55 · see citing works
Swenson, K. I., Winkler, K. E., & Means, A. R. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-02-0115 · Cited by 49 · see citing works
Differential phosphorylations of Spi-B and Spi-1 transcription factors.
Mao, C., Ray-Gallet, D., Tavitian, A., et al. (1996) · PubMed · Cited by 48 · see citing works
Jin, D. I., Jameson, S. B., Reddy, M. A., Schenkman, D., & Ostrowski, M. C. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.2.693 · Cited by 47 · see citing works
Cell Cycle Regulation of c-Jun N-Terminal Kinase Activity at the Centrosomes
MacCorkle-Chosnek, R. A., VanHooser, A., Goodrich, D. W., et al. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5948 · Cited by 38 · see citing works
Takino, T., Yoshioka, K., Miyamori, H., et al. (2003) · Kanazawa University Repository for Academic Resources (DSpace) (Kanazawa University) · Cited by 31 · see citing works
Li, W., Hu, P. J., Skolnik, E. Y., et al. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.12.5824-5833.1992 · Cited by 30 · see citing works
Fowles, L., Stacey, K. J., Marks, D. C., HAMILTON, J. A., & Hume, D. A. (2000) · Biochemical Journal · doi:10.1042/bj3470313 · Cited by 20 · see citing works
Self-citationLiu, R., Itoh, T., Arai, K., & Watanabe, S. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6643 · Cited by 16 · see citing works
Myeloid Development Is Selectively Disrupted in PU.1 Null Mice
Anderson, K. L., Smith, K. A., Conners, K., et al. (1998) · Blood · doi:10.1182/blood.v91.10.3702.3702_3702_3710 · Cited by 16 · see citing works
Regulation and functions of c-Jun N-terminal kinase/stress-activated protein kinase.
Wang, T. H., Wang, H. S., & Soong, Y. K. (2000) · PubMed · Cited by 11 · see citing works
Flagged first, then by citations
1 of the 69 references couldn’t be matched to a known paper.
Research works printed but not linked: 64
- 2000, J. Biol. Chem., 7403
- 1997, Biochem. Biophys. Res. Commun., 611
- 1998, Curr. Opin. Cell. Biol., 205
- 1996, EMBO J., 2760
- 1991, Nature, 494
- 1998, Immunity, 575
- 1998, Science, 2092
- 2000, Cell, 239
- 1996, Oncogene, 863
- 2000, Mol. Cell. Biol., 8026
- 1994, Mol. Cell. Biol., 373
- 1998, J. Leukocyte Biol., 405
- 1996, EMBO J., 5647
- 1997, Mol. Reprod. Dev., 4
- 1988, J. Cell. Biochem., 179
- 1990, EMBO J., 2415
- 1992, Mol. Cell. Biol., 5355
- 1995, Mol. Cell. Biol., 693
- 1999, Mol. Cell. Biol., 2624
- 2001, J. Clin. Invest., 73
- 2001, Diabetes, 77
- 2003, Blood, 1155
- 1989, Nucleic Acids Res., 6419
- 1998, J. Biol. Chem., 6662
- 2001, Proc. Natl. Acad. Sci. USA, 2199
- 2003, Methods Mol. Biol., 111
- 1999, J. Biol. Chem., 15127
- 1995, Proc. Natl. Acad. Sci. USA, 7686
- 1997, Proc. Natl. Acad. Sci. USA, 4330
- 1994, J. Biol. Chem., 5241
- 2003, Cell Death Differ., 218
- 2001, Proc. Natl. Acad. Sci. USA, 7783
- 2003, Blood, 1019
- 1999, Genomics, 111
- 2003, Mol. Cell. Biol., 1896
- 1986, Science, 364
- 1996, J. Biol. Chem., 15743
- 2001, J. Leukocyte Biol., 812
- 1994, Oncogene, 121
- 2001, J. Biol. Chem., 17800
- 2000, J. Cell Biol., 741
- 1999, J. Cell Biol., 1461
- 1992, Mol. Cell. Biol., 5824
- 1995, Mol. Cell. Biol., 3430
- 2000, Biochem. J., 313
- 1995, Proc. Natl. Acad. Sci. USA, 6837
- 1991, Mol. Cell. Biol., 4466
- 1992, Blood, 2107
- 1999, Genes Dev., 607
- 1999, EMBO J., 188
- 2004, J. Biol. Chem., 5008
- 2001, Biochem. Biophys. Res. Commun., 173
- 2003, Mol. Biol. Cell., 156
- 1996, J. Exp. Med., 61
- 1998, Mol. Cell. Biol., 5148
- 2000, Chang Gung Med. J., 57
- 1997, Mol. Reprod. Dev., 11
- 2002, Nat. Genet., 201
- 2003, Hypertension, 1372
- 2002, Oncogene, 6488
- 1998, Blood, 3702
- 2002, Blood, 111
- 1996, Proc. Natl. Acad. Sci. USA, 2774
- 2001, J. Immunol., 5646
Cited by
Sorted by citations
Zhang, Y., Choksi, S., Chen, K., Pobezinskaya, E. L., Linnoila, I. R., & Liu, Z.-G. (2013) · Cell Research · doi:10.1038/cr.2013.75 · Cited by 574 · see citing works
Inflammation in Diabetic Nephropathy
Lim, A. K. H., & Tesch, G. H. (2012) · Mediators of Inflammation · doi:10.1155/2012/146154 · Cited by 439 · see citing works
Transcriptional control of granulocyte and monocyte development
Friedman, A. D. (2007) · Oncogene · doi:10.1038/sj.onc.1210764 · Cited by 427 · see citing works
“The JNK inhibitor SP600125 reduces the number of macrophages developing from murine marrow cells cultured in the presence of M-CSF (Himes et al., 2006).”
BackgroundMajor pathways involved in macrophage polarization in cancer
Kerneur, C., Cano, C. E., & Olive, D. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1026954 · Cited by 348 · see citing works
JNK signaling in cancer cell survival
Wu, Q., Wu, W., Fu, B., Shi, L., Wang, X., & Kuca, K. (2019) · Medicinal Research Reviews · doi:10.1002/med.21574 · Cited by 322 · see citing works
Regulation of the immune response by stress‐activated protein kinases
Rincón, M., & Davis, R. J. (2009) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00744.x · Cited by 266 · see citing works
“Although pharmacological inhibitors and peptide inhibitors of JNK have been shown to induce apoptosis of macrophages and inhibit colony-stimulating factor (CSF-1)dependent differentiation of bone marrow cells into macrophages (37), no defect in macrophage differentiation has been reported in JNK-deficient mice.”
BackgroundJNK Pathway Signaling: A Novel and Smarter Therapeutic Target for Various Biological Diseases
Kumar, A., Singh, U. K., Kini, S. G., Garg, V., Agrawal, S., Tomar, P. K., Pathak, P., Chaudhary, A., Gupta, P., & Malik, A. (2015) · Future Medicinal Chemistry · doi:10.4155/fmc.15.132 · Cited by 200 · see citing works
Callens, C., Coulon, S., Naudin, J., Radford-Weiss, I., Boissel, N., Raffoux, E., Wang, P. H. M., Agarwal, S., Tamouza, H., Paubelle, E., et al. (2010) · Journal of Experimental Medicine · doi:10.1084/jem.20091488 · Cited by 197 · see citing works
“Given the high similarities shared between VD and iron deprivation agents to induce cell differentiation, we investi gated whether iron deprivation of cells could induce VDR signaling (Wang et al., 2003; Himes et al., 2006).”
BackgroundMAP4K Family Kinases in Immunity and Inflammation
Chuang, H., Wang, X., & Tan, T. (2015) · Advances in immunology · doi:10.1016/bs.ai.2015.09.006 · Cited by 200 · see citing works
“GCK is also detected in macrophages where its expression level is further increased upon LPS stimulation (Himes et al., 2006).”
BackgroundSelective inhibitors for JNK signalling: a potential targeted therapy in cancer
Wu, Q., Wu, W., Jacevic, V. M., França, T. C. C., Wang, X., & Kuča, K. (2020) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2020.1720013 · Cited by 172 · see citing works
Sehgal, A., Irvine, K. M., & Hume, D. A. (2021) · Seminars in Immunology · doi:10.1016/j.smim.2021.101509 · Cited by 155 · see citing works
Self-citationManipulation of host signalling pathways by anthrax toxins
Turk, B. E. (2007) · Biochemical Journal · doi:10.1042/bj20061891 · Cited by 149 · see citing works
Fang, L., Wu, H., Ding, P., & Liu, R. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2013.12.016 · Cited by 146 · see citing works
Guo, L., Bertola, D. R., Takanohashi, A., Saito, A., Segawa, Y., Yokota, T., Ishibashi, S., Nishida, Y., Yamamoto, G. L., Franco, J. F. D. S., et al. (2019) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2019.03.004 · Cited by 133 · see citing works
“It has previously been shown that phosphorylation of CSF1R-tyrosine triggered by the ligand binding to the receptor activates multiple kinase pathways including PI3K, ERK1/2, and JNK.(19,20) To evaluate the functional impacts of three CSF1R variants (c.”
BackgroundRegulation of the intestinal tight junction by natural polyphenols: A mechanistic perspective
Yang, G., Bibi, S., Du, ., Suzuki, T., & Zhu, M. J. (2016) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2016.1152230 · Cited by 132 · see citing works
“Members of the JNK family also play crucial roles in inflammation (Himes et al., 2006).”
BackgroundG-protein-coupled receptor expression, function, and signaling in macrophages
Lattin, J. E., Zidar, D. A., Schroder, K., Kellie, S., Hume, D. A., & Sweet, M. J. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0107051 · Cited by 115 · see citing works
“[263].”
Self-citationTLR4 signaling and macrophage inflammatory responses are dampened by GIV/Girdin
Swanson, L., Katkar, G. D., Tam, J. S., Pranadinata, R. F., Chareddy, Y. S., Coates, J., Anandachar, M. S., Castillo, V., Olson, J., Nizet, V., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2011667117 · Cited by 107 · see citing works
Lim, A. K. H., Ma, F. Y., Nikolic‐Paterson, D. J., Thomas, M. C., Hurst, L., & Tesch, G. H. (2009) · Diabetologia · doi:10.1007/s00125-009-1399-3 · Cited by 103 · see citing works
“Other studies have indicated that the activation of JNK following c-fms signalling is critical for the development, proliferation and survival of macrophages [35].”
BackgroundCurry, J. M., Eubank, T. D., Roberts, R. D., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003405 · Cited by 97 · see citing works
“Also, M-CSF activates the pro-survival mitogen-activated protein kinase (MAPK) pathway, including ERK, p38, and JNK [10–13].”
BackgroundT Cell Lineage Commitment: Identity and Renunciation
Rothenberg, E. V. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1003703 · Cited by 90 · see citing works
CSF-1, IGF-1, and the control of postnatal growth and development
Gow, D., Sester, D. P., & Hume, D. A. (2010) · Journal of Leukocyte Biology · doi:10.1189/jlb.0310158 · Cited by 90 · see citing works
“In the absence of CSF-1, mouse macrophages undergo programmed cell death [32].”
BackgroundSelf-citationJNK Signaling in Stem Cell Self-Renewal and Differentiation
Semba, T., Sammons, R. M., Wang, X., Xie, X., Dalby, K. N., & Ueno, N. T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072613 · Cited by 84 · see citing works
Quan, Y., Gong, L., He, J., Zhou, Y., Liu, M., Cao, Z., Li, Y., & Peng, C. Y. (2019) · Toxicology Letters · doi:10.1016/j.toxlet.2019.02.007 · Cited by 77 · see citing works
Kasper, B., Brandt, E., Brandau, S., & Petersen, F. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.4.2584 · Cited by 76 · see citing works
“Although for development and survival of murine macrophages the activation of JNK was reported to be more relevant than Erk (32), our findings confirm previous reports from Monick et al.”
ResultERK Signaling Is Essential for Macrophage Development
Richardson, E. T., Shukla, S., Nagy, N., Boom, W. H., Beck, R. C., Zhou, L., Landreth, G. E., & Harding, C. V. (2015) · PLoS ONE · doi:10.1371/journal.pone.0140064 · Cited by 73 · see citing works
Sester, D. P., Brion, K., Trieu, A., Goodridge, H. S., Roberts, T. L., Dunn, J. A., Hume, D. A., Stacey, K. J., & Sweet, M. J. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.7.4473 · Cited by 71 · see citing works
“This is in agreement with previous studies showing no role for MEK-dependent ERK1/2 activation in BMM survival promoted by CSF-1 (64, 65), nor in the antiapoptotic action of CpG ODN and LPS on murine splenic DC (4).”
ResultSelf-citationBonifer, C. (2007) · Frontiers in bioscience · doi:10.2741/2700 · Cited by 70 · see citing works
Tanel, A., & Averill‐Bates, D. A. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.10.014 · Cited by 65 · see citing works
Melcher, M., Unger, B., Schmidt, U., Rajantie, I., Alitalo, K. K., & Ellmeier, W. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.12.8048 · Cited by 63 · see citing works
“M-CSF starvation in macrophage cultures induces apoptosis (27).”
BackgroundTsai, C.-W., Chen, H., Yang, J., Sheen, L., & Lii, C. (2007) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf061874t · Cited by 63 · see citing works
Huber, R., Pietsch, D., Günther, J., Welz, B., Vogt, N., & Brand, K. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1322-4 · Cited by 59 · see citing works
“Inhibition of JNK leads to (i) decreased monocytic differentiation of 1,25(OH)2D3-treated HL-60 cells [144], (ii) a reduction of the protein tyrosine phosphatase (PTP) Shp2-induced increased monocytic precursor cell formation in Shp2-transduced murine hematopoietic progenitor cells [145], and (iii) to a markedly reduc…”
BackgroundSauter, K. A. D., Pridans, C., Sehgal, A., Bain, C. C., Scott, C. L., Moffat, L., Rojo, R., Stutchfield, B. M., Davies, C. L., Donaldson, D. S., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0105429 · Cited by 59 · see citing works
“1 to promote macrophage differentiation and expression of other macrophage-specific genes ([46] and references therein) and jun kinase is required for CSF1-dependent macrophage survival [47].”
BackgroundSelf-citationRojo, R., Pridans, C., Langlais, D., & Hume, D. A. (2017) · Clinical Science · doi:10.1042/cs20170238 · Cited by 60 · see citing works
Self-citationSurvival of monocytes and macrophages and their role in health and disease
Hunter, M. G. (2009) · Frontiers in bioscience · doi:10.2741/3514 · Cited by 56 · see citing works
“JNK inhibition also downregulates M-CSF receptor (c-fms) and Bcl-xL mRNA expression in mature macrophages and represses M-CSF-dependent differentiation of bone marrow cells to macrophages (97).”
BackgroundResultMaeyashiki, C., Melhem, H., Hering, L., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-57657-9 · Cited by 55 · see citing works
Monick, M. M., Powers, L. S., Gross, T. J., Flaherty, D. M., Barrett, C. W., & Hunninghake, G. W. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.3.1636 · Cited by 51 · see citing works
“(59) study uses murine bone marrow-derived macrophages instead of human primary tissue macrophages (alveolar).”
BackgroundResultInfluentialSpalinger, M. R., Lang, S., Vavricka, S. R., Fried, M., Rogler, G., & Scharl, M. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072384 · Cited by 50 · see citing works
Wu, H., Wang, J., Zhang, B., et al. (2016) · Life Sciences · doi:10.1016/j.lfs.2016.07.016 · Cited by 49 · see citing works
Exogenous heat shock protein 27 uniquely blocks differentiation of monocytes to dendritic cells
Laudański, K., De, A. K., & Miller‐Graziano, C. L. (2007) · European Journal of Immunology · doi:10.1002/eji.200636993 · Cited by 48 · see citing works
A Peptide Inhibitor of c-Jun N-Terminal Kinase for the Treatment of Endotoxin-Induced Uveitis
Touchard, E., Omri, S., Naud, M.-C., Berdugo, M., Deloche, C., Abadie, C., Jonet, L., Jeanny, J.-C., Crisanti, P., de Kozak, Y., et al. (2010) · Investigative Opthalmology & Visual Science · doi:10.1167/iovs.09-4733 · Cited by 43 · see citing works
Wei, Z. Z., Yu, S. P., Lee, J. H., Chen, D., Taylor, T. M., Deveau, T. C., Yu, A. C., & Wei, L. (2014) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-014-0067-4 · Cited by 43 · see citing works
“JNK is a sub-family member of mitogen-activated protein kinase (MAPK) and a multifunctional kinase involved in cell survival (Himes et al. 2006; Fraser et al. 2013), apoptosis (Ouyang and Shen 2006), proinflammatory cytokine production (Chang et al. 2006), and osmotic imbalance (Fanger et al. 1997).”
BackgroundInfection with Leishmania major Induces a Cellular Stress Response in Macrophages
Filardy, A. A., Costa-da-Silva, A. C., Koeller, C. M., Pinto, K. G., Ribeiro-Gomes, F. L., Lopes, M. F., Heise, N., Freire-de-Lima, C. G., Nunes, M. P., & DosReis, G. A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0085715 · Cited by 45 · see citing works
“However, the JNK pathway is also involved in non-apoptotic responses such as macrophage differentiation [16] and proinflammatory cytokine and chemokine production [17,18].”
BackgroundQuantitative Proteomic Characterization of Ethanol-Responsive Pathways in Rat Microglial Cells
Bell‐Temin, H., Zhang, P., Chaput, D., King, M. A., You, M., Liu, B., & Stevens, S. M. (2013) · Journal of Proteome Research · doi:10.1021/pr301038f · Cited by 41 · see citing works
Tang, J., Amin, M. A., & Campian, J. L. (2025) · Cells · doi:10.3390/cells14080562 · Cited by 50 · see citing works
“GSCs modulate the phenotype and function of antigen-presenting cells (APCs) such as dendritic cells and macrophages, inducing immunosuppression and impairing the initiation of effective immune responses [80].”
Lim, A. K. H., Ma, F. Y., Nikolic‐Paterson, D. J., Ozols, E., Young, M. J., Bennett, B. L., Friedman, G. C., & Tesch, G. H. (2011) · American Journal of Nephrology · doi:10.1159/000331058 · Cited by 38 · see citing works
JNK Signaling as a Key Modulator of Soft Connective Tissue Physiology, Pathology, and Healing
Nikoloudaki, G. E., Brooks, S., Peidl, A., Tinney, D., & Hamilton, D. W. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21031015 · Cited by 41 · see citing works
“In contrast to neutrophils, in monocyte and macrophage populations, which begin to infiltrate granulation tissue at 24 hours following injury, JNK signaling has been shown to regulate their survival [52,53].”
BackgroundWang, L., Liang, Q., Lin, A., Chen, X., Wu, Y., Zhang, B., Zhang, Y., Min, H., Wen, Y., Song, S., et al. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00560 · Cited by 35 · see citing works
Köröskényi, K., Kiss, B., & Szondy, Z. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.04.003 · Cited by 34 · see citing works
“Since macrophages express JNK1 and 2 [26], but the human phospho-MAPK array kit did not detect mouse JNK1, we tested its phosphorylation by Western blot analysis by using a mouse specific anti-JNK1 antibody.”
MethodHume, D. A. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.0312166 · Cited by 33 · see citing works
“required for macrophage viability [89].”
Self-citationLiu, Y., Verma, V. K., Malhi, H., Gores, G. J., Kamath, P. S., Sanyal, A. J., Chalasani, N., Gao, B., & Shah, V. H. (2017) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00005.2017 · Cited by 33 · see citing works
Chow, J., Shen, S., Wu, C.-Y., et al. (2006) · APOPTOSIS · doi:10.1007/s10495-006-0085-x · Cited by 31 · see citing works
“In macrophages, suppression of JNKs results in cell cycle arrest at G2/M and apoptosis in response to CSF-1 treatment [38].”
BackgroundGrasset, M.-F., Gobert, S., Mouchiroud, G., & Bourette, R. P. (2009) · Journal of Leukocyte Biology · doi:10.1189/jlb.0309151 · Cited by 28 · see citing works
“DUSP5 (also known as hVH-3 or B23) is a nuclear MKP that dephosphorylates ERK1/2, not ERK5, p38 MAPK, and JNK, through specific and direct interaction [23].”
BackgroundInfluentialTranscriptomic Analysis of Rat Macrophages
Pridans, C., Irvine, K. M., Davis, G. M., Lefèvre, L., Bush, S. J., & Hume, D. A. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.594594 · Cited by 29 · see citing works
Self-citationImpact of polyphenols in phagocyte functions
da Cunha, L. R., Muniz‐Junqueira, M. I., & Borges, T. K. D. S. (2019) · Journal of Inflammation Research · doi:10.2147/jir.s193749 · Cited by 26 · see citing works
“phages have a selective requirement of JNK for their survival, proliferation and differentiation.(99,100) Polyphenols might influence such mechanisms, as”
BackgroundYe, C., Li, R., Xu, L., Qiu, Y., Fu, S., Liu, Y., Wu, Z., Hou, Y., & Hu, C. A. (2019) · BMC Veterinary Research · doi:10.1186/s12917-019-1840-x · Cited by 26 · see citing works
“JNK plays an important role in regulating cell viability, and targeted disruption of JNK results in defects in apoptosis [26].”
BackgroundJoo, M., Kwon, M., Cho, Y.-J., Hu, N., Pedchenko, T. V., Sadikot, R. T., Blackwell, T. S., & Christman, J. W. (2009) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.90320.2008 · Cited by 25 · see citing works
Non-thermal plasma treatment induces MAPK signaling in human monocytes
Bundscherer, L., Nagel, S., Hasse, S., Tresp, H., Wende, K., Walther, R., Reuter, S., Weltmann, K., Masur, K., & Lindequist, U. (2014) · Open Chemistry · doi:10.1515/chem-2015-0071 · Cited by 24 · see citing works
“The mitogen-activated protein kinases (MAPK) extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38 MAPK are implicated in monocyte differentiation to macrophages [15-17].”
BackgroundThe Mononuclear Phagocyte System of the Rat
Hume, D. A., Caruso, M., Keshvari, S., Patkar, O. L., Sehgal, A., Bush, S. J., SUMMERS, K. M., Pridans, C., & Irvine, K. M. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2100136 · Cited by 21 · see citing works
Self-citationHung, C., Chen, M., DeArmond, D. T., Chiu, C. H.-L., Limboy, C. A., Tan, X., Kusi, M., Chou, C., Lin, L., Zhang, Z., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113067 · Cited by 26 · see citing works
Lutter, D., Ugocsai, P., Grandl, M., Orsó, E., Theis, F. J., Lang, E. W., & Schmitz, G. (2008) · BMC Bioinformatics · doi:10.1186/1471-2105-9-100 · Cited by 24 · see citing works
“The transcription factor JUN also known as c-Jun belongs to the family of c-Jun N-terminal kinases (JNKs) which are important for development and survival of macrophages [46].”
BackgroundVonghia, L., Herck, M. A. V., Weyler, J., & Francque, S. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00563 · Cited by 23 · see citing works
Kang, H., Lee, S. Y., Jeon, H.-S., Choi, Y. Y., Kim, S., Lee, W. K., Lee, H. C., Choi, J. E., Bae, E. Y., Yoo, S. S., et al. (2014) · Journal of Thoracic Oncology · doi:10.1097/jto.0000000000000310 · Cited by 23 · see citing works
“In addition, this SNP was found to increase the phosphorylation of a mitogen-activated protein kinase, JNK. Conclusions: Our results suggest that the three SNPs, particularly CSF1R rs10079250, may contribute to lung cancer susceptibility in never-smoking females.”
BackgroundInhibitory effects of Saururus chinensis and its components on stomach cancer cells
Jeong, H. J., Koo, B., Kang, T., et al. (2014) · Phytomedicine · doi:10.1016/j.phymed.2014.12.003 · Cited by 23 · see citing works
Anthocyanins and intestinal barrier function: a review
Valdez, J. C., & Bolling, B. W. (2019) · Journal of Food Bioactives · doi:10.31665/jfb.2019.5175 · Cited by 24 · see citing works
Lattin, J. E., Greenwood, K. P., Daly, N. L., et al. (2009) · Molecular Immunology · doi:10.1016/j.molimm.2009.09.012 · Cited by 22 · see citing works
Self-citationDeletion of JNK2 prevents vitamin-D-deficiency-induced hypertension and atherosclerosis in mice
Oh, J., Riek, A. E., Zhang, R. M., Williams, S. A. S., Darwech, I., & Bernal‐Mizrachi, C. (2017) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2017.09.014 · Cited by 22 · see citing works
Ontiveros‐Torres, M. Á., Labra‐Barrios, M. L., Díaz-Cintra, S. Y., Aguilar-Vázquez, A. R., Moreno-Campuzano, S., Flores-Rodríguez, P., Luna-Herrera, C., Mena, R., Perry, G. L., Florán, B., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-150837 · Cited by 21 · see citing works
Serum granulocyte macrophage-colony stimulating factor: a tumor marker in colorectal carcinoma?
Demırcı, U., Çoşkun, U., Sancak, B., et al. (2009) · PubMed · Cited by 21 · see citing works
Lo, S. Z. Y., Steer, J. H., & Joyce, D. A. (2011) · Cancer Letters · doi:10.1016/j.canlet.2011.03.020 · Cited by 19 · see citing works
c-Jun N-Terminal Kinase as a Therapeutic Target in Experimental Autoimmune Encephalomyelitis
Bagnoud, M., Briner, M., Remlinger, J., Meli, I., Schuetz, S., Pistor, M., Salmen, A., Chan, A., & Hoepner, R. (2020) · Cells · doi:10.3390/cells9102154 · Cited by 18 · see citing works
“In addition, it has been demonstrated that activation of the JNK pathway was essential for the development and the survival of macrophages [50].”
BackgroundGene-selective transcription promotes the inhibition of tissue reparative macrophages by TNF
Dichtl, S., Sanin, D. E., Koss, C. K., Willenborg, S., Petzold, A., Tanzer, M. C., Dahl, A., Kabat, A. M., Lindenthal, L., Zeitler, L., et al. (2022) · Life Science Alliance · doi:10.26508/lsa.202101315 · Cited by 16 · see citing works
“This was an identical observation to Himes et al (2006) who used different modes of JNK inhibition and concluded that JNK signaling was required for CSF1R activity and thus the normal development of BMDMs (Himes et al, 2006).”
ResultSinner or Saint?: Nck Adaptor Proteins in Vascular Biology
Alfaidi, M., Scott, M. L., & Orr, A. W. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.688388 · Cited by 16 · see citing works
Yamaori, S., Ishii, H., Chiba, K., Yamamoto, I., & Watanabe, K. (2013) · Toxicology · doi:10.1016/j.tox.2013.10.007 · Cited by 17 · see citing works
JNK1, but Not JNK2, Is Required in Two Mechanistically Distinct Models of Inflammatory Arthritis
Denninger, K., Rasmussen, S. B., Larsen, J. M., Ørskov, C., Poulsen, S. S., Sørensen, P., Christensen, J. P., Illges, H., Ødum, N., & Labuda, T. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.06.019 · Cited by 17 · see citing works
Cui, J., Zhu, N., Wang, Q., Yu, M., Feng, J., Li, Y., Zhang, J., & Shen, B. (2009) · Cellular Immunology · doi:10.1016/j.cellimm.2008.12.003 · Cited by 15 · see citing works
Oh, S. T., Lee, S., Hua, C., et al. (2019) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2019.23.1.29 · Cited by 15 · see citing works
Duan, C., Li, Y., Dong, X., et al. (2019) · Combinatorial Chemistry & High Throughput Screening · doi:10.2174/1386207322666190206163409 · Cited by 15 · see citing works
Concurrent protective and destructive signaling of JNK2 in neuroblastoma cells
Waetzig, V., Wacker, U., Haeusgen, W., et al. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.01.032 · Cited by 15 · see citing works
Yoo, B.-G., Hong, J.-P., Song, H.-Y., et al. (2022) · Journal of the Korean Society of Food Science and Nutrition · doi:10.3746/jkfn.2022.51.2.100 · Cited by 14 · see citing works
Enhanced Macrophage M1 Polarization and Resistance to Apoptosis Enable Resistance to Plague
Pachulec, E., Abdelwahed, R. B., Chevallier, L., O’Donnell, H., Guillas, C., Jaubert, J., Montagutelli, X., Carniel, É., & Demeure, C. E. (2017) · The Journal of Infectious Diseases · doi:10.1093/infdis/jix348 · Cited by 14 · see citing works
“The JNK factor is known to play a role in cell survival [27].”
BackgroundPérez‐Matute, P., Pichel, J. G., Íñiguez, M., et al. (2016) · Antiviral Therapy · doi:10.3851/imp3099 · Cited by 13 · see citing works
“In addition, JNK are also important for the development and survival of macrophages [15].”
BackgroundThe Spectrum of CAR Cellular Effectors: Modes of Action in Anti-Tumor Immunity
Nguyen, T., Müller, R., Briukhovetska, D., Weber, J., Feucht, J., Künkele, A., Hudecek, M., & Kobold, S. (2024) · Cancers · doi:10.3390/cancers16142608 · Cited by 13 · see citing works
“TRAF6 can also interact with IRF1, IRF5 and IRF7, leading to the transcription of TNF or type I IFN, and also links to the p38 and JNK pathway, influencing macrophage pro-or anti-inflammatory response, development, proliferation, and survival [159,161,162].”
BackgroundEarly Activation of MAP Kinases by Influenza A Virus X-31 in Murine Macrophage Cell Lines
Cannon, G., Callahan, M. A., Gronemus, J. Q., & Lowy, R. J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0105385 · Cited by 12 · see citing works
Choi, M. S., Jeong, H. J., Kang, T., et al. (2015) · Life Sciences · doi:10.1016/j.lfs.2015.09.003 · Cited by 12 · see citing works
Debbas, V., Arai, R. J., Ferderbar, S., Schindler, F., Stern, A., & Monteiro, H. P. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.09.091 · Cited by 11 · see citing works
“Specifically, the activation of the ERK pathway in differentiating cells is implicated in the induction of the p21 protein, a product of Waf1/Cip1/sdi-1 gene [19,2] while JNK and p38 are associated in the expression and posttranscriptional control of proteins such as TNFa [20–23].”
BackgroundLi, X., Liu, Z., Gao, T., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241411842 · Cited by 11 · see citing works
“JNK play an important role in regulating cell viability [68].”
BackgroundThompson, M. R., Xu, D., & Williams, B. R. G. (2013) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2013.0007 · Cited by 11 · see citing works
Montani, M. S. G., Falcinelli, L., Santarelli, R., Romeo, M. A., Granato, M., Faggioni, A., & Cirone, M. (2019) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2019.06.008 · Cited by 10 · see citing works
“Interestingly, JNK phosphorylation has been previously reported to promote macrophage development (Himes et al., 2006), therefore its de-phosphorylation by KSHV could contribute to the viral-mediated impairment of monocyte differentiation.”
BackgroundResultInfluentialPetit, M., Weber-Delacroix, E., Lanthiez, F., Barthélémy, S., Guillou, N., Firpion, M., Bonduelle, O., Hume, D. A., Combadière, C., & Boissonnas, A. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114847 · Cited by 9 · see citing works
Self-citationOsteopetrosis: Gene-Based Nosology and Significance SLC29A3, Dysosteosclerosis
Turan, S. (2022) · Bone · doi:10.1016/j.bone.2022.116615 · Cited by 8 · see citing works
Rodrigues, J. M., Lokhande, L., Olsson, L. M., Hassan, M., Johansson, A., Janská, A., Kumar, D., Schmidt, L., Nikkarinen, A., Hollander, P., et al. (2024) · Blood Advances · doi:10.1182/bloodadvances.2023012039 · Cited by 8 · see citing works
Analysis on degree distribution of tumor signaling networks
Huang, J., & Zhang, W. (2012) · DOAJ (DOAJ: Directory of Open Access Journals) · Cited by 8 · see citing works
Pulmonary Proteome and Protein Networks in Response to the Herbicide Paraquat in Rats
Jeong, I. K. C. M. (2015) · Journal of Proteomics & Bioinformatics · doi:10.4172/jpb.1000354 · Cited by 8 · see citing works
Han, J.-H., Jeong, H. J., Lee, H. N., et al. (2016) · Phytomedicine · doi:10.1016/j.phymed.2016.11.009 · Cited by 8 · see citing works
Fate of macrophages once having ingested apoptotic cells: Lymphatic clearance or in situ apoptosis?
Bellingan, G. J., & Laurent, G. J. (2008) · Birkhäuser Basel eBooks · doi:10.1007/978-3-7643-7506-5_5 · Cited by 8 · see citing works
Identification of crucial metabolites/reactions in tumor signaling networks
Li, J., & Zhang, W. (2013) · DOAJ (DOAJ: Directory of Open Access Journals) · Cited by 7 · see citing works
Liu, H., Jiang, Q., Ju, Z., Guan, S., & He, B. (2018) · Cell Biology International · doi:10.1002/cbin.11049 · Cited by 7 · see citing works
“JNK is a sub-family member of mitogen-activated protein kinase (MAPK) and a multifunctional kinase involved in cell survival (Himes et al., 2006; Fraser et al., 2013) and apoptosis (Ouyang and Shen, 2006).”
BackgroundGene expression profiles of human lung epithelial cells exposed to toluene
Kim, Y.-R., Kim, I. K., Lee, S., et al. (2012) · Toxicology and Environmental Health Sciences · doi:10.1007/s13530-012-0146-1 · Cited by 7 · see citing works
Unconventional codon usage bias mediates mRNA translational dynamics in macrophages
Luo, S., Wang, Q., Chen, A., Huang, L., Liu, Y., Zong, X., & Mao, Y. (2025) · PLoS Biology · doi:10.1371/journal.pbio.3003403 · Cited by 6 · see citing works
“Multiple signaling pathways [19], such as the C-Jun N-terminal kinase (JNK) [20], PI3K/Akt [21,22], Notch signaling cascades [23], and the mammalian target of rapamycin (mTOR) pathway [24,25], play critical roles in driving dynamic changes in the expression of macrophages.”
Honda, H., Nishimichi, N., Kaneko, M., Yamashita, M., Akimoto, Y., Tanimoto, H., Teramoto, M., 寺本, 秀., & Yokosaki, Y. (2023) · Reproductive Sciences · doi:10.1007/s43032-023-01181-4 · Cited by 3 · see citing works
- Authors
- Himes, S. R., Sester, D. P., Ravasi, T., Cronau, S. L., Sasmono, T., & Hume, D. A.
- Affiliations
- The University of Queensland (AU)
- Cooperative Research Centre for Chronic Inflammatory Disease, Institute for Molecular Biosciences, University of Queensland , Brisbane ,
- Venue
- The Journal of Immunology
- Publisher
- Oxford University Press (OUP)
- Published
- 2006-02
- Volume
- 176
- Issue
- 4
- Pages
- 2219-2228
- ISSN
- 0022-1767 (ISSN-L)
- 1550-6606
- OpenAlex
- W1582648966
- Cited by
- 117
- References
- 69
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 4 · 2023: 3 · 2022: 6 · 2021: 4 · 2020: 7 · 2019: 10 · 2018: 1 · 2017: 5 · 2016: 6 · 2015: 6 · 2014: 10 · 2013: 9 · 2012: 4
- FWCI
- 4.19
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The Journal of Immunology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
- Life Sciences › Immunology and Microbiology › Immunology › Immune cells in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Keywords
- JNK, macrophage development, macrophage survival, CSF-1, CSF-1 receptor, c-fms, Bcl-xL, apoptosis
- MeSH terms
- Proto-Oncogene Protein Spi-1, Animals, Bone Marrow Cells, Cell Differentiation, Cell Survival, Cells, Cultured, DNA
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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