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Journal articles on the topic 'Tumour necrosis factor receptor I'

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Published: 10 December 2022

Last updated: 28 January 2023

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1

Nezu, M., H. Iwagaki, H. Aoki, N. Tanaka, and K. Orita. "Tumour Necrosis Factor-α Upregulates Transferrin Receptors in K 562 Cells." Journal of International Medical Research 22, no. 3 (May 1994): 145–52. http://dx.doi.org/10.1177/030006059402200302.

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The effects of tumour necrosis factor-α on transferrin receptor expression in a human chronic myelocytic leukaemia cell line, K 562 cells, were studied. Cytofluorometry studies showed that the numbers of transferrin receptors in exponentially growing K 562 cells were increased when the cells were incubated with tumour necrosis factor-α for 24 h. The induction of transferrin receptors by tumour necrosis factor-α may be mediated by a mechanism that is independent of growth since cell growth in treated cultures did not differ from that in the controls. The DNA contents of K 562 cells treated with tumour necrosis factor-α showed that after 24 h there were less cells in the G1 and S phases and more cells in the G2/M phase than in the control group. The phase of upregulation of transferrin receptors induced by tumour necrosis factor-α may be dependent on the cell cycle. This new evidence that tumour necrosis factor-α upregulates transferrin receptors suggests a cancer-anaemia cascade in which the cancer burden state activates macrophage release of tumour necrosis factor-α as a result of transferrin receptor expression.

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2

Süttmann, U., O. Selberg, H. Gallati, J. Ockenga, H. Deicher, and M. J. Müller. "Tumour Necrosis Factor Receptor Levels Are Linked to the Acute-Phase Response and Malnutrition in Human-Immunodeficiency-Virus-Infected Patients." Clinical Science 86, no. 4 (April 1, 1994): 461–67. http://dx.doi.org/10.1042/cs0860461.

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1. Increased release of tumour necrosis factor is thought to contribute to human-immunodeficiency-virus-associated wasting syndrome. Elevated serum concentrations of tumour necrosis factor have, however, mainly been found during acute opportunistic infections and were not correlated with the degree of wasting. This finding may be explained by the paracrine release and the rapid inactivation of tumour necrosis factor. Serum levels of the two recently detected soluble tumour necrosis factor receptor proteins (p55 and p75) are assumed to reflect tumour necrosis factor release. 2. Serum levels of soluble tumour necrosis factor receptors 55 and 75 were measured by an enzyme-linked immunological and biological binding assay in 45 human-immunodeficiency-virus-infected patients and seven healthy control subjects. Patients were followed up for survival. Serum albumin, prealbumin, total iron-binding capacity (transferrin) and C-reactive protein concentrations were measured using standard laboratory methods. Body composition was determined by bioelectrical impedance analysis. 3. Serum concentrations of soluble tumour necrosis factor receptor 55 and 75 were both significantly increased in human-immunodeficiency-virus-infected patients as compared with the healthy control subjects (P < 0.05); soluble tumour necrosis factor receptor concentrations were even more increased in patients with elevated C-reactive protein levels (≥ 5 mg/l) as compared with those with normal C-reactive protein levels (< 5 mg/l; P < 0.0001 and P < 0.01, respectively). An association was observed between serum soluble tumour necrosis factor receptor 55 and 75 concentration and (i) serum albumin concentration (r = −0.46, P < 0.005 and r = −0.63, P < 0.001, respectively), (ii) serum prealbumin concentration (r = −0.42, P < 0.005 and r = −0.57, P < 0.001, respectively), and (iii) serum total iron-binding capacity (transferrin; r = −0.31, P < 0.05 and r = −0.44, P < 0.005, respectively). A correlation was also found between serum soluble tumour necrosis factor receptor 55 level and the extracellular mass-body cell mass quotient (r = 0.63, P < 0.001). 4. The present data provide evidence that the tumour necrosis factor system is involved in the genesis of human-immunodeficiency-virus-associated malnutrition. Serum levels of soluble tumour necrosis factor receptors may be useful for diagnosis and management of the wasting syndrome.

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3

BARBER, Matthew D., Kenneth C. H. FEARON, and James A. ROSS. "Relationship of serum levels of interleukin-6, soluble interleukin-6 receptor and tumour necrosis factor receptors to the acute-phase protein response in advanced pancreatic cancer." Clinical Science 96, no. 1 (January 1, 1999): 83–87. http://dx.doi.org/10.1042/cs0960083.

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The level of the acute-phase response is a major predictor of survival in patients with advanced pancreatic cancer. This study examines the association between the acute-phase protein response, as determined by serum C-reactive protein, and serum levels of interleukin-6, soluble interleukin-6 receptor and the soluble tumour necrosis factor receptors in patients with pancreatic cancer. Thirty-four blood samples were collected from 13 patients with advanced pancreatic cancer. Samples were also collected from six healthy subjects. Levels of C-reactive protein, interleukin-6, soluble interleukin-6 receptor and soluble tumour necrosis factor receptors 55 and 75 were measured by indirect ELISA. Serum levels of C-reactive protein, interleukin-6 and soluble tumour necrosis factor receptors 55 and 75 were significantly higher in cancer patients than in controls. Levels of serum soluble interleukin-6 receptor were not significantly different between the two groups. In cancer patients, a significant positive association was found between the level of the acute-phase protein response and serum levels of interleukin-6, soluble tumour necrosis factor receptor 55 and soluble tumour necrosis factor receptor 75. No association was found between levels of soluble interleukin-6 receptor and any other factor. There is no significant relationship between the level of soluble interleukin-6 receptor and the acute-phase protein response in vivo and the biological role of soluble interleukin-6 receptor in the chronic inflammatory component of cachexia remains unclear.

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4

XU, Duorong, Zhenqi SHI, Jay McDONALD, George PAN, Xuemei CAO, Xueqing YU, and Xu FENG. "Development of a chimaeric receptor approach to study signalling by tumour necrosis factor receptor family members." Biochemical Journal 383, no. 2 (October 8, 2004): 219–25. http://dx.doi.org/10.1042/bj20040961.

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Members of the tumour necrosis factor receptor family play a pivotal role in cell differentiation, function and apoptosis. However, signalling by many members of the family remains to be elucidated. In the present study, we developed a chimaeric receptor approach for studying signalling by receptors belonging to this family. The chimaeric receptor comprises the human Fas external domain linked to the transmembrane and cytoplasmic domains of a tumour necrosis factor receptor family member of interest. When the chimaera is expressed in mouse cells, the clustering of the chimaera induced by a human Fas-activating antibody activates the intracellular domain of the chimaera without affecting its endogenous counterpart. Since the antibody recognizes only human Fas, this approach can be used to dissect signalling by any tumour necrosis factor family member using any type of mouse cell including those endogenously expressing Fas. Moreover, we also showed that the chimaeric receptor approach can be used to study signalling at any stage of cell differentiation or function.

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5

Westbrook, A. M., B. Wei, K. Hacke, M. Xia, J. Braun, and R. H. Schiestl. "The role of tumour necrosis factor- and tumour necrosis factor receptor signalling in inflammation-associated systemic genotoxicity." Mutagenesis 27, no. 1 (October 6, 2011): 77–86. http://dx.doi.org/10.1093/mutage/ger063.

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6

Holbrook, Jonathan, Samuel Lara-Reyna, Heledd Jarosz-Griffiths, and Michael F. McDermott. "Tumour necrosis factor signalling in health and disease." F1000Research 8 (January 28, 2019): 111. http://dx.doi.org/10.12688/f1000research.17023.1.

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The master pro-inflammatory cytokine, tumour necrosis factor (TNF), has been shown to modulate multiple signalling pathways, with wide-ranging downstream effects. TNF plays a vital role in the typical immune response through the regulation of a number of pathways encompassing an immediate inflammatory reaction with significant innate immune involvement as well as cellular activation with subsequent proliferation and programmed cell death or necrosis. As might be expected with such a broad spectrum of cellular effects and complex signalling pathways, TNF has also been implicated in a number of disease states, such as rheumatoid arthritis, ankylosing spondylitis, and Crohn’s disease. Since the time of its discovery over 40 years ago, TNF ligand and its receptors, TNF receptor (TNFR) 1 and 2, have been categorised into two complementary superfamilies, namely TNF (TNFSF) and TNFR (TNFRSF), and 19 ligands and 29 receptors have been identified to date. There have been significant advances in our understanding of TNF signalling pathways in the last decade, and this short review aims to elucidate some of the most recent advances involving TNF signalling in health and disease.

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7

Trentin, L., R. Zambello, P. Bulian, A. Cerutti, C. Enthammer, M. Cassatella, D. Nitti, M. Lise, C. Agostini, and G. Semenzato. "Tumour-infiltrating lymphocytes bear the 75 kDa tumour necrosis factor receptor." British Journal of Cancer 71, no. 2 (February 1995): 240–45. http://dx.doi.org/10.1038/bjc.1995.50.

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8

Rasmussen, C. A., J. L. Pace, S. Banerjee, T. A. Phillips, and J. S. Hunt. "Trophoblastic Cell Lines Generated from Tumour Necrosis Factor Receptor-deficient Mice Reveal Specific Functions for the Two Tumour Necrosis Factor Receptors." Placenta 20, no. 2-3 (March 1999): 213–22. http://dx.doi.org/10.1053/plac.1998.0356.

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9

Deuren, M. "Kinetics of tumour necrosis factor-alpha, soluble tumour necrosis factor receptors, interleukin 1-beta and its receptor antagonist during serious infections." European Journal of Clinical Microbiology & Infectious Diseases 13, S1 (January 1994): S12—S16. http://dx.doi.org/10.1007/bf02390680.

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10

Hehlgans, Thomas, and Klaus Pfeffer. "The intriguing biology of the tumour necrosis factor/tumour necrosis factor receptor superfamily: players, rules and the games." Immunology 115, no. 1 (May 2005): 1–20. http://dx.doi.org/10.1111/j.1365-2567.2005.02143.x.

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11

Pang, Xuan-Ping, Jerome M. Hershman, Vierka Smith, A. Eugene Pekary, and Masahiro Sugawara. "The mechanism of action of tumour necrosis factor-α and interleukin 1 on FRTL-5 rat thyroid cells." Acta Endocrinologica 123, no. 2 (August 1990): 203–10. http://dx.doi.org/10.1530/acta.0.1230203.

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Abstract. Previous work showed that treatment of rats with tumour necrosis factor-α produced a model of nonthyroid illness in which there was reduction of circulating thyroid hormones and TSH, reduced thyroid response to TSH, and reduced thyroid iodide uptake. In vitro studies showed that tumour necrosis factor-α binds to a specific receptor on FRTL-5 rat thyroid cells, that TSH increases the number of tumour necrosis factor-α receptors, and that tumour necrosis factor-α inhibits iodide uptake by these cells. In the present study, we obtained additional data on the effects of tumour necrosis factor-α on FRTL-5 cells and studied the mechanism of action of tumour necrosis factor-α in these cells. Tumour necrosis factor-α inhibited both basal and TSH-stimulated [125I]iodide uptake; tumour necrosis factor-α slowed the recovery of [125I]iodide trapping after the cells were exposed to TSH and augmented the loss of the [125I]iodide trapping function after the cells were deprived of TSH; tumour necrosis factor-α inhibited [125I]iodide trapping in a noncompetitive manner; tumour necrosis factor-α did not affect cell growth of FRTL-5 cells. Interleukin-1 (IL-1) also inhibited basal and TSH-stimulated [125I]iodide uptake, but it stimulated cell growth. Tumour necrosis factor-α and IL-1 did not affect the generation of cAMP in the presence or absence of TSH; these cytokines blocked the cAMP-induced stimulation of [125I]iodide uptake. Tumour necrosis factor-α did not affect [3H]arachidonic acid uptake or release by FRTL-5 cells. The inhibitors of the phospholipase A2-arachidonic acid pathway did not affect the action of tumour necrosis factor-α. The H2O2 scavenger, catalase, did not block the action of tumour necrosis factor-α. The results show that both tumour necrosis factor-α and IL-1 inhibit FRTL-5 function and that the site of action of these cytokines is distal to the production of cAMP. The actions of tumour necrosis factor-α on FRTL-5 cells do not appear to be mediated by the phospholipase A2-arachidonic acid pathway or by H2O2.

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12

Godfried, Mieke H., Tom van der Poll, Jaap Jansen, Johannes A. Romijin, Jan K. M. Eeftinck Schattenkerk, Erik Endert, Sander J. H. van Deventer, and Hans P. Sauerwein. "Soluble receptors for tumour necrosis factor." AIDS 7, no. 1 (January 1993): 33–36. http://dx.doi.org/10.1097/00002030-199301000-00005.

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13

Bradley, John R., and Jordan S. Pober. "Tumor necrosis factor receptor-associated factors (TRAFs)." Oncogene 20, no. 44 (October 2001): 6482–91. http://dx.doi.org/10.1038/sj.onc.1204788.

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14

Mukai, Yohei, Teruya Nakamura, Yasuo Yoshioka, Shin-ichi Tsunoda, Haruhiko Kamada, Shinsaku Nakagawa, Yuriko Yamagata, and Yasuo Tsutsumi. "Crystallization and preliminary X-ray analysis of the tumour necrosis factor α–tumour necrosis factor receptor type 2 complex." Acta Crystallographica Section F Structural Biology and Crystallization Communications 65, no. 3 (February 26, 2009): 295–98. http://dx.doi.org/10.1107/s1744309109004461.

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15

Darnay, B. G., and B. B. Aggarwal. "Signal transduction by tumour necrosis factor and tumour necrosis factor related ligands and their receptors." Annals of the Rheumatic Diseases 58, Supplement 1 (November 1, 1999): i2—i13. http://dx.doi.org/10.1136/ard.58.2008.i2.

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16

Roy, Urmi. "3D Modeling of Tumor Necrosis Factor Receptor and Tumor Necrosis Factor‐bound Receptor Systems." Molecular Informatics 38, no. 5 (January 11, 2019): 1800011. http://dx.doi.org/10.1002/minf.201800011.

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17

Noguchi, M., N. Hiwatashi, Z. Liu, and T. Toyota. "Secretion imbalance between tumour necrosis factor and its inhibitor in inflammatory bowel disease." Gut 43, no. 2 (August 1, 1998): 203–9. http://dx.doi.org/10.1136/gut.43.2.203.

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Background—Tumour necrosis factor (TNF) α and TNF-β are soluble ligands binding to TNF receptors with similar activities; soluble TNF receptors neutralise TNF activity by acting as inhibitors. Little is known about the cytokine/soluble receptor role in inflammatory bowel disease (IBD).Aims—To test the hypothesis that an imbalance in secretion between TNF and TNF inhibitors plays a role in gut inflammation in patients with IBD.Methods—The secretion of TNF-α, TNF-β, and soluble TNF receptors was compared in the culture supernatants of colonic biopsy specimens and isolated lamina propria mononuclear cells from patients with active colonic IBD.Results—Spontaneous secretion of TNF-α in involved IBD mucosa was higher than in normal control and self limited colitis mucosa. Secretion of TNF-β was higher in patients with Crohn’s disease than in those with ulcerative colitis. Soluble TNF receptor in IBD mucosa inhibited TNF activity. Type 2 soluble receptor release from IBD mucosa was increased in active inflammation; release from lamina propria cells was not increased. Mucosal TNF-α production correlated with severity of disease.Conclusions—Results showed enhanced secretion of TNF-α but failure to release enhanced amounts of soluble TNF receptor in lamina propria mononuclear cells of patients with IBD. An imbalance in secretion between TNF and TNF inhibitor may be implicated in the pathogenesis of IBD.

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18

Munker, R., J. DiPersio, and HP Koeffler. "Tumor necrosis factor: receptors on hematopoietic cells." Blood 70, no. 6 (December 1, 1987): 1730–34. http://dx.doi.org/10.1182/blood.v70.6.1730.1730.

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Abstract Tumor necrosis factor (TNF) is a monokine that is cytotoxic/cytostatic for a variety of tumor cells and has multiple effects on normal cells. We demonstrate that normal and malignant human myeloid cells express a single class of high-affinity receptors (400 to 1,900 per cell, KD 20 to 90 pmol/L) for TNF. Mitogen-stimulated lymphocytes have a similar number of TNF receptors, whereas resting lymphoid cells have fewer receptors. RBCs and platelets have no detectable TNF receptors. No correlation is observed between the receptor number, receptor affinity, and the cytotoxic effect of TNF on myeloid cell lines. Significant cytotoxic effects of TNF on the most sensitive myeloid cell line (HL-60 promyelocytes) could be seen at concentrations tenfold lower than those concentrations at which one half of the TNF receptors were occupied. Our data show that significant biologic effects of TNF can occur at low levels of receptor occupancy and resistance to TNF is not related to the absence of TNF receptors on certain myeloid leukemic cell lines.

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19

Munker, R., J. DiPersio, and HP Koeffler. "Tumor necrosis factor: receptors on hematopoietic cells." Blood 70, no. 6 (December 1, 1987): 1730–34. http://dx.doi.org/10.1182/blood.v70.6.1730.bloodjournal7061730.

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Tumor necrosis factor (TNF) is a monokine that is cytotoxic/cytostatic for a variety of tumor cells and has multiple effects on normal cells. We demonstrate that normal and malignant human myeloid cells express a single class of high-affinity receptors (400 to 1,900 per cell, KD 20 to 90 pmol/L) for TNF. Mitogen-stimulated lymphocytes have a similar number of TNF receptors, whereas resting lymphoid cells have fewer receptors. RBCs and platelets have no detectable TNF receptors. No correlation is observed between the receptor number, receptor affinity, and the cytotoxic effect of TNF on myeloid cell lines. Significant cytotoxic effects of TNF on the most sensitive myeloid cell line (HL-60 promyelocytes) could be seen at concentrations tenfold lower than those concentrations at which one half of the TNF receptors were occupied. Our data show that significant biologic effects of TNF can occur at low levels of receptor occupancy and resistance to TNF is not related to the absence of TNF receptors on certain myeloid leukemic cell lines.

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20

Zhu, Xiao-juan, Yan Shi, Feng Zhang, Qing-min Yao, Yan-xia Liu, Ning-ning Shan, Dan Wang, Jun Peng, Jian Xu, and Ming Hou. "Reduced tumour necrosis factor receptor superfamily 13C inversely correlated with tumour necrosis factor superfamily 13B in patients with immune thrombocytopenia." British Journal of Haematology 166, no. 5 (May 30, 2014): 783–91. http://dx.doi.org/10.1111/bjh.12958.

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21

Zeggini, E. "Tumour necrosis factor receptor II polymorphism and juvenile idiopathic arthritis." Rheumatology 41, no. 4 (April 1, 2002): 462–65. http://dx.doi.org/10.1093/rheumatology/41.4.462.

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22

Jones, E. Yvonne. "The tumour necrosis factor receptor family: life or death choices." Current Opinion in Structural Biology 10, no. 6 (December 2000): 644–48. http://dx.doi.org/10.1016/s0959-440x(00)00149-4.

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23

stojanov, silvia, and michael f. mcdermott. "the tumour necrosis factor receptor-associated periodic syndrome: current concepts." Expert Reviews in Molecular Medicine 7, no. 22 (October 10, 2005): 1–18. http://dx.doi.org/10.1017/s1462399405009749.

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the tumour necrosis factor receptor (tnfr)-associated periodic syndrome (traps) is an autosomal dominant, multisystemic, autoinflammatory disorder caused by mutations in the tnfr1 gene (tnfrsf1a). traps seems to be the most common hereditary periodic fever (hpf) syndrome in some western populations, and the second most prevalent hpf worldwide, behind familial mediterranean fever (fmf). the proteins involved in susceptibility to traps (tnfrsf1a) and fmf (pyrin) are both members of the death-domain-fold superfamily. mutations affecting these proteins might cause dysregulation of innate immune responses, with a propensity to autoinflammation. most traps patients have reduced blood levels of soluble tnfrsf1a between attacks, with an inappropriately small increase during bouts of fever. the pathogenesis of the ‘hyperinflammatory state’ in traps has been variously ascribed to a shedding defect of tnfrsf1a from the cell surface resulting in increased tnf inflammatory signalling, or impaired tnf apoptotic signalling. some low-penetrance tnfrsf1a variants also contribute to the clinical phenotype in individuals carrying other hpf-associated mutations, and have been reported in several disorders such as behçet's disease and systemic lupus erythematosus. synthetic anti-tnf agents provide a rational form of therapy for traps, and have been shown to delay or indeed prevent development of systemic amyloidosis (aa type), a life-threatening complication in this condition.

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24

Eades, Diane K., Peter Cornelius, and Phillip H. Pekala. "Characterization of the tumour necrosis factor receptor in human placenta." Placenta 9, no. 3 (May 1988): 247–51. http://dx.doi.org/10.1016/0143-4004(88)90032-x.

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25

Graham, Stephen C., Mohammad W. Bahar, Nicola G. A. Abrescia, Geoffrey L. Smith, David I. Stuart, and Jonathan M. Grimes. "Structure of CrmE, a Virus-encoded Tumour Necrosis Factor Receptor." Journal of Molecular Biology 372, no. 3 (September 2007): 660–71. http://dx.doi.org/10.1016/j.jmb.2007.06.082.

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26

Meekins, J. W. "Interleukin-6, tumour necrosis factor and soluble tumour necrosis factor receptors in women with pre-eclampsia." BJOG: An International Journal of Obstetrics and Gynaecology 102, no. 10 (October 1995): 842–43. http://dx.doi.org/10.1111/j.1471-0528.1995.tb10859.x.

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27

Abdalla, Sayed Abdalla, Hiroyuki Horiuchi, Shuichi Furusawa, and Haruo Matsuda. "Molecular study on chicken tumor necrosis factor receptor-II and tumor necrosis factor receptor-associated factor-5." Veterinary Immunology and Immunopathology 98, no. 1-2 (March 2004): 31–41. http://dx.doi.org/10.1016/j.vetimm.2003.10.004.

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28

Keane, Helen M., Nick Sheron, John Goka, Robin D. Hughes, and Roger Williams. "Plasma Inhibitory Activity against Tumour Necrosis Factor in Fulminant Hepatic Failure." Clinical Science 90, no. 1 (January 1, 1996): 77–80. http://dx.doi.org/10.1042/cs0900077.

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1. Soluble tumour necrosis factor receptors released into the circulation inhibit the effects of excess tumour necrosis factor-α and represent an important protective response. 2. In this study we have measured the levels of tumour necrosis factor and soluble tumour necrosis factor receptors p55 and p75 in the plasma of 10 patients with fulminant hepatic failure and 10 healthy control subjects. The capacity of the plasmas at varying dilutions to inhibit the biological activity of 1000 pg/ml of recombinant tumour necrosis factor in a tumour necrosis factor cytotoxicity assay in vitro was also determined. 3. The mean plasma levels of tumour necrosis factor in patients with fulminant hepatic failure (48.4 ± 10.9 pg/ml) were significantly increased compared with normal control subjects (6.1 ± 1.04 pg/ml, P < 0.01). Plasma soluble tumour necrosis factor receptors p55 and p75 were also significantly elevated in patients with fulminant hepatic failure (18.16 ± 9.94 ng/ml and 16.06 ± 9.93 ng/ml respectively) when compared with normal control subjects (1.28 ± 0.24 ng/ml and 1.62 ± 0.91 ng/ml, P < 0.001). 4. Fulminant hepatic failure plasma had a much lower capacity to inhibit tumour necrosis factor bioactivity in vitro, with a statistically significant difference between the inhibitory capacity of the fulminant hepatic failure and normal plasma seen at plasma dilutions of 1:5 and 1:20 (P < 0.05). 5. The reduced tumour necrosis factor neutralization capacity observed in fulminant hepatic failure, despite the increased levels of soluble tumour necrosis factor receptors, suggests enhanced susceptibility to the potential deleterious effects of tumour necrosis factor in fulminant hepatic failure.

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29

Van Rijen, Miranda M. L., Herold J. Metselaar, Martijn Hommes, Jan N. M. Ijzermans, Hugo W. Tilanus, and Jaap Kwekkeboom. "Mycophenolic acid is a potent inhibitor of the expression of tumour necrosis factor- and tumour necrosis factor-receptor superfamily costimulatory molecules." Immunology 109, no. 1 (May 2003): 109–16. http://dx.doi.org/10.1046/j.1365-2567.2003.01635.x.

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30

Kaji, Keisuke, Rei Katogi, Yoshiaki Azuma, Asuka Naito, Jun-Ichiro Inoue, and Akira Kudo. "Tumor Necrosis Factor α-Induced Osteoclastogenesis Requires Tumor Necrosis Factor Receptor-Associated Factor 6." Journal of Bone and Mineral Research 16, no. 9 (September 1, 2001): 1593–99. http://dx.doi.org/10.1359/jbmr.2001.16.9.1593.

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31

Rubin, B. Y., S. L. Anderson, S. A. Sullivan, B. D. Williamson, E. A. Carswell, and L. J. Old. "Nonhematopoietic cells selected for resistance to tumor necrosis factor produce tumor necrosis factor." Journal of Experimental Medicine 164, no. 4 (October 1, 1986): 1350–55. http://dx.doi.org/10.1084/jem.164.4.1350.

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TNF-resistant lines of L cells can be derived from TNF-sensitive populations by repeated exposure to TNF, and these resistant L cells, in contrast to sensitive L cells and other types of cells, lack demonstrable cell surface receptors for TNF. We have now found that TNF-resistant L cells produce a factor that is cytotoxic for L cells and has the following distinguishing characteristics of mouse TNF: it is a protein of 43 kD, composed of 16 kD subunits, that competes with TNF for receptor binding, induces hemorrhagic necrosis of the TNF-sensitive mouse sarcoma Meth A, has synergistic cytotoxic action with interferon, and its activity is neutralized by antibody to TNF. The two conclusions of this study are that cells selected for TNF resistance spontaneously produce a molecule resembling macrophage TNF, and that cells of nonhematopoietic origin are capable of producing TNF.

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32

Naudé, Petrus J. W., Johan A. den Boer, Paul G. M. Luiten, and Ulrich L. M. Eisel. "Tumor necrosis factor receptor cross-talk." FEBS Journal 278, no. 6 (February 8, 2011): 888–98. http://dx.doi.org/10.1111/j.1742-4658.2011.08017.x.

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33

Tchorzewski, H., K. Zeman, J. Kantorski, E. Paleolog, M. Kahan, M. Feldmann, M. Kwinkowski, et al. "The effect of tumour necrosis factor-α (TNF-α) muteins on human neutrophilsin vitro." Mediators of Inflammation 2, no. 1 (1993): 41–48. http://dx.doi.org/10.1155/s0962935193000055.

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Tumour necrosis factor-α (TNF-α) has been implicated as an important inflammatory mediator.In vitro, TNF-α is reported to activate human polymorphonuclear neutrophils (PMN), inducing responses such as phagocytic activity, degranulation and oxidative metabolism. Biological responses to TNF-α are initiated by its binding to specific cell surface receptors, and various studies have shown that the major TNF receptor species on PMN is the 75 kDa receptor. To verify the suggestion that the receptor binding domain includes the region close to the N-terminus of the TNF-α molecule, four TNF-α derivatives termed muteins were constructed, using a synthetic cDNA fragment substituting the N-terminal 3–7 selected hydrophilic or hydrophobic amino acids in the original TNF-α genomic DNA. Binding of muteins to PMN was assessed using monoclonal antibodies recognizing either the 55 kDa (p55) or the 75 kDa (p75) TNF receptor subtypes. Blocking by muteins of anti-p75 antibody binding to PMN was as expected from their N-terminal amino acid composition and hydrophilic properties. Hydrophilic muteins competed well with anti-TNF receptor antibodies for binding to the p75 receptor. In contrast, hydrophobic muteins were unable to block anti-p75 binding. Similarly, degranulation, chemiluminescence or enhancement of the PMN response to specific stimuli by the muteins correlated with the hydrophilic properties of the muteins. The significance of these observations in relation to the molecular structure of TNF-α is discussed.

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34

Niessen, Natalie M., Peter G. Gibson, Jodie L. Simpson, Hayley A. Scott, Katherine J. Baines, and Michael Fricker. "Airway monocyte modulation relates to tumour necrosis factor dysregulation in neutrophilic asthma." ERJ Open Research 7, no. 3 (June 11, 2021): 00131–2021. http://dx.doi.org/10.1183/23120541.00131-2021.

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BackgroundDysregulation of tumour necrosis factor-α (TNF-α) signalling is implicated in neutrophilic asthma. TNF-α signalling involves membrane-bound and soluble ligand (TNF-α) and receptors (TNFRs); however, little is known about how these proteins are altered in asthma. We hypothesised that intercompartment-, immune cell- and/or asthma inflammatory phenotype-dependent regulation could relate to TNF dysregulation in neutrophilic asthma.MethodsMeasurements were made in 45 adults with asthma (36 non-neutrophilic, 9 neutrophilic) and 8 non-asthma controls. Soluble TNF-α, TNF receptor 1 (TNFR1) and TNFR2 were quantified in plasma and sputum supernatant by ELISA, and membrane-bound TNF-α/TNFR1/TNFR2 measured on eosinophils, neutrophils, monocytes, and macrophages in blood and sputum by flow cytometry. Marker expression was compared between inflammatory phenotypes and compartments, and relationship of membrane-bound and soluble TNF markers and immune cell numbers tested by correlation.ResultsSoluble sputum TNFR1 and TNFR2 were increased in neutrophilic versus non-neutrophilic asthma (p=0.010 and p=0.029). Membrane-bound TNF-α expression was upregulated on sputum versus blood monocytes, while TNFR1 and TNFR2 levels were reduced on airway versus blood monocytes and neutrophils. Soluble TNFR1 and TNFR2 in sputum significantly correlated with the number of airway monocytes (p=0.016, r=0.358 and p=0.029, r=0.327).ConclusionOur results imply that increased sputum soluble TNF receptor levels observed in neutrophilic asthma relate to the increased recruitment of monocytes and neutrophils into the airways and their subsequent receptor shedding. Monocytes also increase TNF-α ligand expression in the airways. These results suggest an important contribution of airway monocytes to the altered inflammatory milieu in neutrophilic asthma.

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Dandekar, P., J. Gregson, R. Campbell, and F. Bianic. "Living with Tumour necrosis factor receptor-associated periodic fever syndrome (TRAPS)." Pediatric Rheumatology 13, Suppl 1 (2015): P23. http://dx.doi.org/10.1186/1546-0096-13-s1-p23.

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Miceli-Richard, C., P. Dieude, E. Hachulla, X. Puechal, F. Cornelis, and X. Mariette. "Tumour necrosis factor receptor 2 (TNFRSF1B) association study in Sjogren's syndrome." Annals of the Rheumatic Diseases 66, no. 12 (December 1, 2007): 1684–85. http://dx.doi.org/10.1136/ard.2007.071167.

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Newbery, HJ, N. Fisher, M. Pirmohamed, NR Kitteringham, IT Gilmore, D. Adams, and BK Park. "Investigation of Tumour Necrosis Factor Receptor Polymorphisms in Alcoholic Liver Disease." Clinical Science 97, s41 (July 1, 1999): 8P—9P. http://dx.doi.org/10.1042/cs097008pc.

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Gallagher, Grant, Joyce Eskdale, Debbie Lynch, and Paul Horgan. "Tumour necrosis factor receptor alleles predict metastatic behaviour in colorectal cancer." Gastroenterology 118, no. 4 (April 2000): A766. http://dx.doi.org/10.1016/s0016-5085(00)85202-6.

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Aurich, S., J. C. Simon, and R. Treudler. "Tumour necrosis factor receptor-associated periodic syndrome mimicking chronic spontaneous urticaria." Journal of the European Academy of Dermatology and Venereology 31, no. 11 (June 7, 2017): e487-e488. http://dx.doi.org/10.1111/jdv.14327.

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Scallon, Bernard J., Han Trinh, Mark Nedelman, Fionula M. Brennan, Marc Feldmann, and John Ghrayeb. "Functional comparisons of different tumour necrosis factor receptor/IgG fusion proteins." Cytokine 7, no. 8 (November 1995): 759–70. http://dx.doi.org/10.1006/cyto.1995.0091.

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Bongioanni, P., Maria Rosaria Romano, Roberto Sposito, Maura Castagna, Barbara Boccardi, and Monica Borgna. "T-cell tumour necrosis factor-α receptor binding in demented patients." Journal of Neurology 244, no. 7 (July 23, 1997): 418–25. http://dx.doi.org/10.1007/s004150050115.

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Wu, Shanshan, Kai Dong, Jiajia Wang, and Yaxin Bi. "Tumor necrosis factor alpha improves glucose homeostasis in diabetic mice independent with tumor necrosis factor receptor 1 and tumor necrosis factor receptor 2." Endocrine Journal 65, no. 6 (2018): 601–9. http://dx.doi.org/10.1507/endocrj.ej17-0539.

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Yang, Ya-Chien, Tsuey-Ying Hsu, Jen-Yang Chen, Czau-Siung Yang, and Rong-Hwa Lin. "Tumour necrosis factor-α-induced apoptosis in cord blood T lymphocytes: involvement of both tumour necrosis factor receptor types 1 and 2." British Journal of Haematology 115, no. 2 (November 2001): 435–41. http://dx.doi.org/10.1046/j.1365-2141.2001.03090.x.

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Arntzen, K. J., K. Egeberg, S. Rahimipoor, L. Vatten, and R. Austgulen. "LPS mediated production of IL-1, PGE2 and PGF2α from term decidua involves tumour necrosis factor and tumour necrosis factor receptor p55." Journal of Reproductive Immunology 45, no. 2 (December 2000): 113–25. http://dx.doi.org/10.1016/s0165-0378(99)00045-5.

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Reibnegger, Gilbert, Antonio Diez-Ruiz, Dietmar Fuchs, and Helmut Wachter. "Soluble tumour necrosis factor receptors as prognostic factors in cancer." Lancet 344, no. 8923 (September 1994): 681–82. http://dx.doi.org/10.1016/s0140-6736(94)92115-6.

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Dinarello, Charles A. "Interleukin-1, Tumour Necrosis Factor and Treatment of the Septic Shock Syndrome." Canadian Journal of Infectious Diseases 3, suppl b (1992): 11–19. http://dx.doi.org/10.1155/1992/652727.

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Treating the septic shock syndrome with antibodies that block only endotoxin has its limitations. Other targets for treating septic shock include neutralizing antibodies to the complement fragment C5a, platelet activating factor antagonists and blockade of endothelial cell leukocyte adhesion molecules. Specific blockade of the pro-inflammatory cytokines interleukin-1 (IL-1) or tumour necrosis factor (TNF) reduces the morbidity and mortality associated with septic shock. Moreover, blocking IL-1 and TNF likely has uses in treating diseases other than septic shock. Use of neutralizing antibodies to TNF or IL-1 receptors has reduced the consequences of infection and inflammation, including lethal outcomes in animal models. The IL-1 receptor antagonist, a naturally occurring cytokine, blocks shock and death due to Escherichia coli as well as ameliorates a variety of inflammatory diseases. Soluble TNF and IL-1 surface receptors, which bind their respective cytokines. also ameliorate disease processes. Clinical trials are presently evaluating the safety and efficacy of anticytokine therapies either alone or in combination.

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Antunes, Ricardo F., Juan Carlos Kaski, and Ingrid E. Dumitriu. "The Role of Costimulatory Receptors of the Tumour Necrosis Factor Receptor Family in Atherosclerosis." Journal of Biomedicine and Biotechnology 2012 (2012): 1–16. http://dx.doi.org/10.1155/2012/464532.

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Atherosclerosis is a chronic inflammatory disease that is mediated by both the innate and adaptive immune responses. T lymphocytes, that together with B cells are the cellular effectors of the adaptive immune system, are currently endowed with crucial roles in the development and progression of atherosclerosis. Costimulatory receptors are a class of molecules expressed by T lymphocytes that regulate the activation of T cells and the generation of effector T-cell responses. In this review we present the roles of costimulatory receptors of the tumour necrosis factor receptor (TNFR) superfamily in atherosclerosis and discuss the implications for future therapies that could be used to specifically modulate the immune response of pathogenic T cells in this disease.

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So, Takanori, Seung-Woo Lee, and Michael Croft. "Tumor Necrosis Factor/Tumor Necrosis Factor Receptor Family Members That Positively Regulate Immunity." International Journal of Hematology 83, no. 1 (January 1, 2006): 1–11. http://dx.doi.org/10.1532/ijh97.05120.

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McLeish, K. R., J. B. Klein, T. Schepers, and G. Sonnenfeld. "Modulation of transmembrane signalling in HL-60 granulocytes by tumour necrosis factor-α." Biochemical Journal 279, no. 2 (October 15, 1991): 455–60. http://dx.doi.org/10.1042/bj2790455.

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Differentiated HL-60 granulocytes were used to study the mechanism by which tumour necrosis factor-alpha (TNF) enhances responses to N-formyl-methionyl-leucylphenylalanine (FMLP). Cultivation of differentiated HL-60 cells with 100 units of TNF/ml for 24 h resulted in a 3-fold increase in superoxide release and 4-fold increase in prostaglandin E2 production on stimulation with 1 microM-FMLP. On the other hand, cultivation with TNF failed to increase phorbol diester stimulation of superoxide release. Formyl-peptide-receptor expression determined on isolated membranes from cells cultivated with TNF (TNF-M) was increased by 50% compared with membranes from control cells (NM). Similarly, FMLP binding to intact HL-60 cells was increased by cultivation with TNF. Guanine-nucleotide-binding proteins (G-protein) levels were not different between TNF-M and NM, as determined by pertussis-toxin-catalysed ADP-ribosylation and by immunoblotting with antisera recognizing alpha i2 subunit. Binding of guanosine 5′-[gamma-thio]triphosphate and GTP hydrolysis stimulated by FMLP were enhanced by about 50% in TNF-M. The efficiency of G-protein activation by formyl-peptide receptors did not differ between TNF-M and NM. TNF regulates expression of formyl-peptide receptors independently of G-protein levels. The regulation of receptor expression is one mechanism by which TNF enhances cell responses to formylated peptides.

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Steinshamn, Sigurd, Ole-Lars Brekke, and Anders Waage. "Soluble tumour necrosis factor receptors, tumour necrosis factor and interleukin-6 in serum in granulocytopenic patients with fever." British Journal of Haematology 89, no. 4 (March 12, 2008): 719–24. http://dx.doi.org/10.1111/j.1365-2141.1995.tb08407.x.

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