Effect of defensin HNP-1 of human neutrophils on production of tumor necrosis factor α by human blood monocytes in vitro

1992 ◽  
Vol 113 (5) ◽  
pp. 709-712
Author(s):  
N. I. Misuno ◽  
T. S. Kolesnikova ◽  
R. I. Lehrer ◽  
T. Ganz ◽  
N. N. Voitenok
Keyword(s):  
Tumor Necrosis Factor ◽  
Human Blood ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Human Neutrophils ◽  
Blood Monocytes ◽  
Factor Α ◽  
Necrosis Factor

Substance P C-terminal octapeptide analogues augment tumor necrosis factor-α release by human blood monocytes and macrophages

1998 ◽  
Vol 82 (2) ◽  
pp. 126-132 ◽  
Author(s):  
Wen-Zhe Ho ◽  
George Stavropoulos ◽  
Jian-Ping Lai ◽  
Bao-Feng Hu ◽  
Vassilike Magafa ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Substance P ◽  
Human Blood ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Blood Monocytes ◽  
Monocytes And Macrophages ◽  
Factor Α ◽  
Necrosis Factor

scholarly journals Regulation of Neutrophil Apoptosis by Tumor Necrosis Factor-α: Requirement for TNFR55 and TNFR75 for Induction of Apoptosis In Vitro

Blood ◽  
1997 ◽  
Vol 90 (7) ◽  
pp. 2772-2783 ◽  
Author(s):  
Joanna Murray ◽  
Jeffrey A.J. Barbara ◽  
Sarah A. Dunkley ◽  
Angel F. Lopez ◽  
Xaveer Van Ostade ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Human Neutrophils ◽  
Receptor Subtypes ◽  
Neutrophil Apoptosis ◽  
Tnf Α ◽  
Factor Α ◽  
Necrosis Factor

Abstract Granulocyte apoptosis is an important mechanism underlying the removal of redundant neutrophils from an inflammatory focus. The ability of many proinflammatory agents to impede this event suggests that such agents act not only in a priming or secretagogue capacity but also increase neutrophil longevity by delaying apoptosis. We have examined whether this hypothesis holds true for all neutrophil priming agents, in particular tumor necrosis factor-α (TNF-α), which has been variably reported to either induce, delay, or have no effect on neutrophil apoptosis. After 20 hours coincubation TNF-α inhibited neutrophil apoptosis; however, more detailed analysis demonstrated its ability to promote apoptosis in a subpopulation of cells at earlier (2 to 8 hours) times. Formyl-Met-Leu-Phe, platelet-activating factor, inositol hexakisphosphate, lipopolysaccharide, leukotriene B4 , and granulocyte-macrophage colony-stimulating factor all inhibited apoptosis at 6 and 20 hours. The early proapoptotic effect of TNF-α was concentration-dependent (EC50 2.8 ng/mL), abolished by TNF-α neutralizing antibody, and was not associated with any change in cell viability or recovery. Of relevance to the inflamed site, the ability of TNF-α to accelerate apoptosis was lost if neutrophils were primed with 1 μmol/L PAF or aged for 6 hours before TNF-α addition. The TNFR55-selective TNF-α mutants (E146K, R32W-S86T) induced neutrophil apoptosis but with a potency 14-fold lower than wild-type TNF-α. Although the TNFR75-selective mutant (D143F ) did not induce apoptosis, blocking antibodies to both receptor subtypes abolished TNF-α–stimulated apoptosis. Hence, TNF-α has the unique ability to induce apoptosis in human neutrophils via a mechanism where TNFR75 facilitates the dominant TNFR55 death effect. This may be an important mechanism controlling neutrophil longevity and clearance in vivo.

scholarly journals Regulation of Neutrophil Apoptosis by Tumor Necrosis Factor-α: Requirement for TNFR55 and TNFR75 for Induction of Apoptosis In Vitro

Blood ◽  
1997 ◽  
Vol 90 (7) ◽  
pp. 2772-2783 ◽  
Author(s):  
Joanna Murray ◽  
Jeffrey A.J. Barbara ◽  
Sarah A. Dunkley ◽  
Angel F. Lopez ◽  
Xaveer Van Ostade ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Human Neutrophils ◽  
Receptor Subtypes ◽  
Neutrophil Apoptosis ◽  
Tnf Α ◽  
Factor Α ◽  
Necrosis Factor

Granulocyte apoptosis is an important mechanism underlying the removal of redundant neutrophils from an inflammatory focus. The ability of many proinflammatory agents to impede this event suggests that such agents act not only in a priming or secretagogue capacity but also increase neutrophil longevity by delaying apoptosis. We have examined whether this hypothesis holds true for all neutrophil priming agents, in particular tumor necrosis factor-α (TNF-α), which has been variably reported to either induce, delay, or have no effect on neutrophil apoptosis. After 20 hours coincubation TNF-α inhibited neutrophil apoptosis; however, more detailed analysis demonstrated its ability to promote apoptosis in a subpopulation of cells at earlier (2 to 8 hours) times. Formyl-Met-Leu-Phe, platelet-activating factor, inositol hexakisphosphate, lipopolysaccharide, leukotriene B4 , and granulocyte-macrophage colony-stimulating factor all inhibited apoptosis at 6 and 20 hours. The early proapoptotic effect of TNF-α was concentration-dependent (EC50 2.8 ng/mL), abolished by TNF-α neutralizing antibody, and was not associated with any change in cell viability or recovery. Of relevance to the inflamed site, the ability of TNF-α to accelerate apoptosis was lost if neutrophils were primed with 1 μmol/L PAF or aged for 6 hours before TNF-α addition. The TNFR55-selective TNF-α mutants (E146K, R32W-S86T) induced neutrophil apoptosis but with a potency 14-fold lower than wild-type TNF-α. Although the TNFR75-selective mutant (D143F ) did not induce apoptosis, blocking antibodies to both receptor subtypes abolished TNF-α–stimulated apoptosis. Hence, TNF-α has the unique ability to induce apoptosis in human neutrophils via a mechanism where TNFR75 facilitates the dominant TNFR55 death effect. This may be an important mechanism controlling neutrophil longevity and clearance in vivo.

scholarly journals Alterations in Gene Expression of Interferon and Tumor Necrosis Factor‐α in Human Blood Macrophage-Like Monocytes Induced by Clinical and Standard Salmonella typhi Strains in vitro

2021 ◽  
Vol 15 (6) ◽  
pp. 658-675
Author(s):  
Mehdi Ghanbari Sardari ◽  
Ramak Yahya Raeyat ◽  
Mohammadreza Mehrabi ◽  
Taghi Zahraiee Salehi ◽  
Jalil Mehrzad Salakojani ◽  
...  
Keyword(s):  
Gene Expression ◽  
Tumor Necrosis Factor ◽  
Human Blood ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Salmonella Typhi ◽  
Factor Α ◽  
Necrosis Factor

scholarly journals In Vivo and in Vitro Evidence for the Involvement of Tumor Necrosis Factor-α in the Induction of Leptin by Lipopolysaccharide*

Endocrinology ◽  
1998 ◽  
Vol 139 (5) ◽  
pp. 2278-2283 ◽  
Author(s):  
Brian N. Finck ◽  
Keith W. Kelley ◽  
Robert Dantzer ◽  
Rodney W. Johnson
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Factor Α ◽  
Necrosis Factor

scholarly journals Ectopic HOXB4 overcomes the inhibitory effect of tumor necrosis factor-α on Fanconi anemia hematopoietic stem and progenitor cells

Blood ◽  
2009 ◽  
Vol 113 (21) ◽  
pp. 5111-5120 ◽  
Author(s):  
Michael D. Milsom ◽  
Bernhard Schiedlmeier ◽  
Jeff Bailey ◽  
Mi-Ok Kim ◽  
Dandan Li ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Fanconi Anemia ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Ectopic Expression ◽  
Hematopoietic Stem ◽  
Tnf Α ◽  
Factor Α ◽  
Necrosis Factor

AbstractEctopic delivery of HOXB4 elicits the expansion of engrafting hematopoietic stem cells (HSCs). We hypothesized that inhibition of tumor necrosis factor-α (TNF-α) signaling may be central to the self-renewal signature of HOXB4. Because HSCs derived from Fanconi anemia (FA) knockout mice are hypersensitive to TNF-α, we studied Fancc−/− HSCs to determine the physiologic effects of HOXB4 on TNF-α sensitivity and the relationship of these effects to the engraftment defect of FA HSCs. Overexpression of HOXB4 reversed the in vitro hypersensitivity to TNF-α of Fancc−/− HSCs and progenitors (P) and partially rescued the engraftment defect of these cells. Coexpression of HOXB4 and the correcting FA-C protein resulted in full correction compared with wild-type (WT) HSCs. Ectopic expression of HOXB4 resulted in a reduction in both apoptosis and reactive oxygen species in Fancc−/− but not WT HSC/P. HOXB4 overexpression was also associated with a significant reduction in surface expression of TNF-α receptors on Fancc−/− HSC/P. Finally, enhanced engraftment was seen even when HOXB4 was expressed in a time-limited fashion during in vivo reconstitution. Thus, the HOXB4 engraftment signature may be related to its effects on TNF-α signaling, and this pathway may be a molecular target for timed pharmacologic manipulation of HSC during reconstitution.

Sign in / Sign up

Export Citation Format

Share Document