Involvement of tyrosine kinase in the induction of cyclo‐oxygenase and nitric oxide synthase by endotoxin in cultured cells
1 Cyclo‐oxygenase (COX) and nitric oxide synthase (NOS) are two enzymes which have distinct cytokine‐inducible isoforms (COX‐2 and iNOS). Many cytokine receptors have an intracellular tyrosine kinase domain. Here we have used the tyrosine kinase inhibitors, erbstatin and genistein, to investigate th...
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| Published in: | British journal of pharmacology Vol. 113; no. 4; pp. 1522 - 1528 |
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| Main Authors: | , , , , |
| Format: | Journal Article |
| Language: | English |
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Oxford, UK
Blackwell Publishing Ltd
01-12-1994
Nature Publishing |
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| Abstract | 1
Cyclo‐oxygenase (COX) and nitric oxide synthase (NOS) are two enzymes which have distinct cytokine‐inducible isoforms (COX‐2 and iNOS). Many cytokine receptors have an intracellular tyrosine kinase domain. Here we have used the tyrosine kinase inhibitors, erbstatin and genistein, to investigate the potential role of tyrosine kinase activation in the induction on COX‐2 and iNOS caused by endotoxin (lipopolysaccharide; LPS) in bovine aortic endothelial cells (BAEC) and J774.2 macrophages.
2
The main COX metabolites, 6‐oxo‐prostaglandin F1α (6‐oxo‐PGF1α) (for BAEC) and PGF2α (for 774.2 macrophages) were measured by radioimmunossay: (i) accumulation of COX metabolites from endogenous arachidonic acid was measured at 24 h after addition of LPS (1 μg ml−1); (ii) in experiments designed to measure ‘COX activity’, COX metabolites generated by BAEC or J774.2 macrophages activated with LPS were assayed (at 12 h after LPS administration) after incubation of the washed cells with exogenous arachidonic acid (30 μg for 15min). Western blot analysis with a specific antibody to COX‐2 was used to determine the expression of COX‐2 protein caused by LPS in cell extracts. Accumulation of nitrite (measured by the Griess reaction) was used as an indicator of NO formation and, hence, iNOS activity.
3
Erbstatin (0.05 to 5 μg ml−1) or genistein (0.5 to 50 μg ml−1) caused a dose‐dependent inhibition of the accumulation of COX metabolites in the supernatant of BAEC or J774.2 macrophages activated with LPS. Erbstatin or genistein also caused a dose‐dependent inhibition of ‘COX activity’ in both cell types. Western blot analysis showed that erbstatin (5 μg ml−1) or genistein (50μg ml−1) inhibited the expression of COX‐2 protein in BAEC and J774.2 macrophages activated with LPS (1 μg ml−1 for 24 h).
4
Erbstatin or genistein also caused a dose‐dependent inhibition of nitrite accumulation in J774.2 macrophages activated with LPS (1 μg ml−1 for 24 h). In contrast to J774.2 macrophages, BAEC stimulated with LPS (1 μg ml−1 for 24 h) did not produce detectable amounts (> 1μm) of nitrite.
5
These results suggest that tyrosine phosphorylation is part of the signal transduction mechanism that mediates (i) the induction of COX‐2 and iNOS elicited by LPS in J774.2 macrophages, and (ii) the induction of COX‐2 by LPS in BAEC. |
|---|---|
| AbstractList | Cyclo‐oxygenase (COX) and nitric oxide synthase (NOS) are two enzymes which have distinct cytokine‐inducible isoforms (COX‐2 and iNOS). Many cytokine receptors have an intracellular tyrosine kinase domain. Here we have used the tyrosine kinase inhibitors, erbstatin and genistein, to investigate the potential role of tyrosine kinase activation in the induction on COX‐2 and iNOS caused by endotoxin (lipopolysaccharide; LPS) in bovine aortic endothelial cells (BAEC) and J774.2 macrophages.
The main COX metabolites, 6‐oxo‐prostaglandin F
1α
(6‐oxo‐PGF
1α
) (for BAEC) and PGF
2α
(for 774.2 macrophages) were measured by radioimmunossay: (i) accumulation of COX metabolites from endogenous arachidonic acid was measured at 24 h after addition of LPS (1 μg ml
−1
); (ii) in experiments designed to measure ‘COX activity’, COX metabolites generated by BAEC or J774.2 macrophages activated with LPS were assayed (at 12 h after LPS administration) after incubation of the washed cells with exogenous arachidonic acid (30 μg for 15min). Western blot analysis with a specific antibody to COX‐2 was used to determine the expression of COX‐2 protein caused by LPS in cell extracts. Accumulation of nitrite (measured by the Griess reaction) was used as an indicator of NO formation and, hence, iNOS activity.
Erbstatin (0.05 to 5 μg ml
−1
) or genistein (0.5 to 50 μg ml
−1
) caused a dose‐dependent inhibition of the accumulation of COX metabolites in the supernatant of BAEC or J774.2 macrophages activated with LPS. Erbstatin or genistein also caused a dose‐dependent inhibition of ‘COX activity’ in both cell types. Western blot analysis showed that erbstatin (5 μg ml
−1
) or genistein (50μg ml
−1
) inhibited the expression of COX‐2 protein in BAEC and J774.2 macrophages activated with LPS (1 μg ml
−1
for 24 h).
Erbstatin or genistein also caused a dose‐dependent inhibition of nitrite accumulation in J774.2 macrophages activated with LPS (1 μg ml
−1
for 24 h). In contrast to J774.2 macrophages, BAEC stimulated with LPS (1 μg ml
−1
for 24 h) did not produce detectable amounts (> 1μ
m
) of nitrite.
These results suggest that tyrosine phosphorylation is part of the signal transduction mechanism that mediates (i) the induction of COX‐2 and iNOS elicited by LPS in J774.2 macrophages, and (ii) the induction of COX‐2 by LPS in BAEC. 1. Cyclo-oxygenase (COX) and nitric oxide synthase (NOS) are two enzymes which have distinct cytokine-inducible isoforms (COX-2 and iNOS). Many cytokine receptors have an intracellular tyrosine kinase domain. Here we have used the tyrosine kinase inhibitors, erbstatin and genistein, to investigate the potential role of tyrosine kinase activation in the induction on COX-2 and iNOS caused by endotoxin (lipopolysaccharide; LPS) in bovine aortic endothelial cells (BAEC) and J774.2 macrophages. 2. The main COX metabolites, 6-oxo-prostaglandin F1 alpha (6-oxo-PGF1 alpha) (for BAEC) and PGF2 alpha (for 774.2 macrophages) were measured by radioimmunossay: (i) accumulation of COX metabolites from endogenous arachidonic acid was measured at 24 h after addition of LPS (1 microgram ml-1); (ii) in experiments designed to measure 'COX activity', COX metabolites generated by BAEC or J774.2 macrophages activated with LPS were assayed (at 12 h after LPS administration) after incubation of the washed cells with exogenous arachidonic acid (30 microM for 15 min). Western blot analysis with a specific antibody to COX-2 was used to determine the expression of COX-2 protein caused by LPS in cell extracts. Accumulation of nitrite (measured by the Griess reaction) was used as an indicator of NO formation and, hence, iNOS activity. 3. Erbstatin (0.05 to 5 micrograms ml-1) or genistein (0.5 to 50 micrograms ml-1) caused a dose-dependent inhibition of the accumulation of COX metabolites in the supernatant of BAEC or J774.2 macrophages activated with LPS. Erbstatin or genistein also caused a dose-dependent inhibition of 'COX activity' in both cell types. Western blot analysis showed that erbstatin (5 ig ml1') or genistein (50gg ml-') inhibited the expression of COX-2 protein in BAEC and J774.2 macrophages activated with LPS (lLgml-' for 24 h).4. Erbstatin or genistein also caused a dose-dependent inhibition of nitrite accumulation in J774.2 macrophages activated with LPS (1 sg ml-' for 24 h). In contrast to J774.2 macrophages, BAECstimulated with LPS (1 pg ml-' for 24 h) did not produce detectable amounts (<1PiM) of nitrite.5. These results suggest that tyrosine phosphorylation is part of the signal transduction mechanism that mediates (i) the induction of COX-2 and iNOS elicited by LPS in J774.2 macrophages, and (ii) the induction of COX-2 by LPS in BAEC. 1. Cyclo-oxygenase (COX) and nitric oxide synthase (NOS) are two enzymes which have distinct cytokine-inducible isoforms (COX-2 and iNOS). Many cytokine receptors have an intracellular tyrosine kinase domain. Here we have used the tyrosine kinase inhibitors, erbstatin and genistein, to investigate the potential role of tyrosine kinase activation in the induction on COX-2 and iNOS caused by endotoxin (lipopolysaccharide; LPS) in bovine aortic endothelial cells (BAEC) and J774.2 macrophages. 2. The main COX metabolites, 6-oxo-prostaglandin F1 alpha (6-oxo-PGF1 alpha) (for BAEC) and PGF2 alpha (for 774.2 macrophages) were measured by radioimmunossay: (i) accumulation of COX metabolites from endogenous arachidonic acid was measured at 24 h after addition of LPS (1 microgram ml-1); (ii) in experiments designed to measure 'COX activity', COX metabolites generated by BAEC or J774.2 macrophages activated with LPS were assayed (at 12 h after LPS administration) after incubation of the washed cells with exogenous arachidonic acid (30 microM for 15 min). Western blot analysis with a specific antibody to COX-2 was used to determine the expression of COX-2 protein caused by LPS in cell extracts. Accumulation of nitrite (measured by the Griess reaction) was used as an indicator of NO formation and, hence, iNOS activity. 3. Erbstatin (0.05 to 5 micrograms ml-1) or genistein (0.5 to 50 micrograms ml-1) caused a dose-dependent inhibition of the accumulation of COX metabolites in the supernatant of BAEC or J774.2 macrophages activated with LPS. Erbstatin or genistein also caused a dose-dependent inhibition of 'COX activity' in both cell types. Western blot analysis showed that erbstatin (5 ig ml1') or genistein (50gg ml-') inhibited the expression of COX-2 protein in BAEC and J774.2 macrophages activated with LPS (lLgml-' for 24 h).4. Erbstatin or genistein also caused a dose-dependent inhibition of nitrite accumulation in J774.2 macrophages activated with LPS (1 sg ml-' for 24 h). In contrast to J774.2 macrophages, BAECstimulated with LPS (1 pg ml-' for 24 h) did not produce detectable amounts (<1PiM) of nitrite.5. These results suggest that tyrosine phosphorylation is part of the signal transduction mechanism that mediates (i) the induction of COX-2 and iNOS elicited by LPS in J774.2 macrophages, and (ii) the induction of COX-2 by LPS in BAEC. 1. Cyclo-oxygenase (COX) and nitric oxide synthase (NOS) are two enzymes which have distinct cytokine-inducible isoforms (COX-2 and iNOS). Many cytokine receptors have an intracellular tyrosine kinase domain. Here we have used the tyrosine kinase inhibitors, erbstatin and genistein, to investigate the potential role of tyrosine kinase activation in the induction on COX-2 and iNOS caused by endotoxin (lipopolysaccharide; LPS) in bovine aortic endothelial cells (BAEC) and J774.2 macrophages. 2. The main COX metabolites, 6-oxo-prostaglandin F1 alpha (6-oxo-PGF1 alpha) (for BAEC) and PGF2 alpha (for 774.2 macrophages) were measured by radioimmunossay: (i) accumulation of COX metabolites from endogenous arachidonic acid was measured at 24 h after addition of LPS (1 microgram ml-1); (ii) in experiments designed to measure 'COX activity', COX metabolites generated by BAEC or J774.2 macrophages activated with LPS were assayed (at 12 h after LPS administration) after incubation of the washed cells with exogenous arachidonic acid (30 microM for 15 min). Western blot analysis with a specific antibody to COX-2 was used to determine the expression of COX-2 protein caused by LPS in cell extracts. Accumulation of nitrite (measured by the Griess reaction) was used as an indicator of NO formation and, hence, iNOS activity. 3. Erbstatin (0.05 to 5 micrograms ml-1) or genistein (0.5 to 50 micrograms ml-1) caused a dose-dependent inhibition of the accumulation of COX metabolites in the supernatant of BAEC or J774.2 macrophages activated with LPS. Erbstatin or genistein also caused a dose-dependent inhibition of 'COX activity' in both cell types. 1 Cyclo‐oxygenase (COX) and nitric oxide synthase (NOS) are two enzymes which have distinct cytokine‐inducible isoforms (COX‐2 and iNOS). Many cytokine receptors have an intracellular tyrosine kinase domain. Here we have used the tyrosine kinase inhibitors, erbstatin and genistein, to investigate the potential role of tyrosine kinase activation in the induction on COX‐2 and iNOS caused by endotoxin (lipopolysaccharide; LPS) in bovine aortic endothelial cells (BAEC) and J774.2 macrophages. 2 The main COX metabolites, 6‐oxo‐prostaglandin F1α (6‐oxo‐PGF1α) (for BAEC) and PGF2α (for 774.2 macrophages) were measured by radioimmunossay: (i) accumulation of COX metabolites from endogenous arachidonic acid was measured at 24 h after addition of LPS (1 μg ml−1); (ii) in experiments designed to measure ‘COX activity’, COX metabolites generated by BAEC or J774.2 macrophages activated with LPS were assayed (at 12 h after LPS administration) after incubation of the washed cells with exogenous arachidonic acid (30 μg for 15min). Western blot analysis with a specific antibody to COX‐2 was used to determine the expression of COX‐2 protein caused by LPS in cell extracts. Accumulation of nitrite (measured by the Griess reaction) was used as an indicator of NO formation and, hence, iNOS activity. 3 Erbstatin (0.05 to 5 μg ml−1) or genistein (0.5 to 50 μg ml−1) caused a dose‐dependent inhibition of the accumulation of COX metabolites in the supernatant of BAEC or J774.2 macrophages activated with LPS. Erbstatin or genistein also caused a dose‐dependent inhibition of ‘COX activity’ in both cell types. Western blot analysis showed that erbstatin (5 μg ml−1) or genistein (50μg ml−1) inhibited the expression of COX‐2 protein in BAEC and J774.2 macrophages activated with LPS (1 μg ml−1 for 24 h). 4 Erbstatin or genistein also caused a dose‐dependent inhibition of nitrite accumulation in J774.2 macrophages activated with LPS (1 μg ml−1 for 24 h). In contrast to J774.2 macrophages, BAEC stimulated with LPS (1 μg ml−1 for 24 h) did not produce detectable amounts (> 1μm) of nitrite. 5 These results suggest that tyrosine phosphorylation is part of the signal transduction mechanism that mediates (i) the induction of COX‐2 and iNOS elicited by LPS in J774.2 macrophages, and (ii) the induction of COX‐2 by LPS in BAEC. |
| Author | Akarasereenont, P. Thiemermann, C. Appleton, I. Vane, J.R. Mitchell, J.A. |
| AuthorAffiliation | William Harvey Research Institute, St. Bartholomew's Hospital Medical College, London |
| AuthorAffiliation_xml | – name: William Harvey Research Institute, St. Bartholomew's Hospital Medical College, London |
| Author_xml | – sequence: 1 givenname: P. surname: Akarasereenont fullname: Akarasereenont, P. – sequence: 2 givenname: J.A. surname: Mitchell fullname: Mitchell, J.A. – sequence: 3 givenname: I. surname: Appleton fullname: Appleton, I. – sequence: 4 givenname: C. surname: Thiemermann fullname: Thiemermann, C. – sequence: 5 givenname: J.R. surname: Vane fullname: Vane, J.R. |
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| ContentType | Journal Article |
| Copyright | 1994 British Pharmacological Society 1995 INIST-CNRS |
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| Keywords | Cell culture Prostaglandin-endoperoxide synthase Enzyme Transferases Rodentia Enzyme inhibitor Endotoxin In vitro Nitric-oxide synthase Vertebrata Mammalia Mouse Animal Oxidoreductases Protein-tyrosine kinase Macrophage |
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| PublicationTitle | British journal of pharmacology |
| PublicationTitleAlternate | Br J Pharmacol |
| PublicationYear | 1994 |
| Publisher | Blackwell Publishing Ltd Nature Publishing |
| Publisher_xml | – name: Blackwell Publishing Ltd – name: Nature Publishing |
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Cyclo‐oxygenase (COX) and nitric oxide synthase (NOS) are two enzymes which have distinct cytokine‐inducible isoforms (COX‐2 and iNOS). Many cytokine... 1. Cyclo-oxygenase (COX) and nitric oxide synthase (NOS) are two enzymes which have distinct cytokine-inducible isoforms (COX-2 and iNOS). Many cytokine... Cyclo‐oxygenase (COX) and nitric oxide synthase (NOS) are two enzymes which have distinct cytokine‐inducible isoforms (COX‐2 and iNOS). Many cytokine receptors... |
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| SubjectTerms | Amino Acid Oxidoreductases - biosynthesis Animals Aorta, Thoracic - cytology Aorta, Thoracic - enzymology Arachidonic Acid - pharmacology Biological and medical sciences Cattle Cell Survival - drug effects Cells, Cultured cytokines Enzyme Induction - drug effects Enzyme Induction - physiology General and cellular metabolism. Vitamins Genistein Hydroquinones - pharmacology Isoflavones - pharmacology lipopolysaccharide Lipopolysaccharides - pharmacology Macrophages - drug effects Macrophages - enzymology Medical sciences Mice nitric oxide Nitric Oxide Synthase Pharmacology. Drug treatments Prostaglandin-Endoperoxide Synthases - biosynthesis prostaglandins Protein-Tyrosine Kinases - antagonists & inhibitors Protein-Tyrosine Kinases - physiology tyrosine kinase receptor |
| Title | Involvement of tyrosine kinase in the induction of cyclo‐oxygenase and nitric oxide synthase by endotoxin in cultured cells |
| URI | https://onlinelibrary.wiley.com/doi/abs/10.1111%2Fj.1476-5381.1994.tb17169.x https://www.ncbi.nlm.nih.gov/pubmed/7534189 https://search.proquest.com/docview/77774382 https://pubmed.ncbi.nlm.nih.gov/PMC1510522 |
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