Induction of an endogenous tumor necrosis factor in mice by murine recombinant interferon-? combined with a lipid A subunit analog (GLA-60) of low toxicity

1989 ◽  
Vol 29 (2) ◽  
Author(s):  
Ikuo Saiki ◽  
Hiroaki Maeda ◽  
Takuma Sakurai ◽  
Jun Murata ◽  
Joji Iida ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Lipid A ◽  
Recombinant Interferon ◽  
A Subunit ◽  
Low Toxicity ◽  
Necrosis Factor

MONOPHOSPHORYL LIPID A PROTECTS AGAINST GRAM-POSITIVE SEPSIS AND TUMOR NECROSIS FACTOR

Shock ◽  
1994 ◽  
Vol 2 (4) ◽  
pp. 271-274 ◽  
Author(s):  
Mark E. Astiz ◽  
Angel Galera ◽  
Dhanonjoy C. Saha ◽  
Charles Carpati ◽  
Eric C. Rackow
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Lipid A ◽  
Gram Positive ◽  
Monophosphoryl Lipid A ◽  
Monophosphoryl Lipid ◽  
Necrosis Factor

Intratumoral Production of Tumor Necrosis Factor Augmented by Endogenous Interferons Results in Potent Antitumor Effects of DT-5461, a Synthetic Lipid A Analog

1995 ◽  
Vol 17 (2) ◽  
pp. 141-150 ◽  
Author(s):  
Eiji Kumazawa ◽  
Toshihiko Akimoto ◽  
Yasuo Kita ◽  
Takeshi Jimbo ◽  
Noriko Joto ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Lipid A ◽  
Antitumor Effects ◽  
Necrosis Factor

scholarly journals Regulation of neutrophil migration and superoxide production by recombinant tumor necrosis factors-alpha and -beta: comparison to recombinant interferon-gamma and interleukin-1 alpha

Blood ◽  
1987 ◽  
Vol 70 (4) ◽  
pp. 979-984 ◽  
Author(s):  
IS Figari ◽  
NA Mori ◽  
MA Jr Palladino
Keyword(s):  
Tumor Necrosis Factor ◽  
Interferon Gamma ◽  
Tumor Necrosis ◽  
Interleukin 1 ◽  
Neutrophil Migration ◽  
Human Tumor ◽  
Superoxide Production ◽  
Polymorphonuclear Neutrophil ◽  
Recombinant Interferon ◽  
Necrosis Factor

Abstract We compared the ability of recombinant human tumor necrosis factor- alpha (rHuTNF-alpha) and tumor necrosis factor-beta (rHuTNF-beta) to stimulate polymorphonuclear neutrophil (PMN) migration and superoxide production. Significant PMN migration occurred across polycarbonate filters after stimulation with rHuTNF-alpha at concentrations ranging from 10(-7) to 10(-10) mol/L and at 10(-7) to 10(-8) mol/L for rHuTNF- beta and N-formylmethionyl-leucyl phenylalanine (FMLP), whereas recombinant human interferon-gamma was only minimally active at 10(-7) mol/L and recombinant human interleukin-1 alpha was inactive at the doses tested. In addition, antibodies to rHuTNF-alpha completely inhibited rHuTNF-alpha but not rHuTNF-beta or FMLP-induced PMN migration. Combinations of rHuTNF-alpha and rHuTNF-beta (at similar molar concentrations) stimulated PMN migration levels comparable to that obtained with rHuTNF-alpha alone. Checkerboard analyses performed by placing different concentrations of rHuTNF-alpha and rHuTNF-beta above and below polycarbonate filters of microchemotaxis chambers demonstrated that rHuTNF-alpha and rHuTNF-beta stimulated both chemotactic and chemokinetic responses by PMN. Additional studies demonstrated that 1 X 10(-8) mol/L rHuTNF-alpha and 3 X 10(-9) mol/L rHuTNF-beta (which represents 10(4) U/mL of each cytokine) were similar in their ability to induce superoxide production by PMNs; however, at ten- to 100-fold lower molar concentrations (10(3) and 10(2) units), rHuTNF-alpha was significantly more active than rHuTNF-beta. At the doses tested, both cytokines were less active than phorbol myristate acetate at stimulating O2- release. The results demonstrate that rHuTNF- alpha and rHuTNF-beta differ quantitatively but not qualitatively in their effects on PMN functions in vitro and suggest that rHuTNF-beta may be less toxic than rHuTNF-alpha in vivo.

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