Arachidonic Acid Metabolism

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Ayman O S Elkadi - One of the best experts on this subject based on the ideXlab platform.

  • acute doxorubicin toxicity differentially alters cytochrome p450 expression and Arachidonic Acid Metabolism in rat kidney and liver
    Drug Metabolism and Disposition, 2011
    Co-Authors: Beshay N M Zordoky, Anwar Anwarmohamed, Mona E Aboutabl, Ayman O S Elkadi
    Abstract:

    The use of doxorubicin (DOX) is limited by significant cardiotoxicity, nephrotoxicity, and hepatotoxicity. We have previously shown that DOX cardiotoxicity induces several cardiac cytochrome P450 (P450) enzymes with subsequent alteration in P450-mediated Arachidonic Acid Metabolism. Therefore, in the current study, we investigated the effect of acute DOX toxicity on P450 expression and Arachidonic Acid Metabolism in the kidney and liver of male Sprague-Dawley rats. Acute DOX toxicity was induced by a single intraperitoneal injection (15 mg/kg) of the drug. After 6 and 24 h, the kidneys and livers were harvested, and several P450 gene and protein expressions were determined by real-time polymerase chain reaction and Western blot analyses, respectively. Kidney and liver microsomal protein from control or DOX-treated rats was incubated with Arachidonic Acid, and its metabolites were determined by liquid chromatography-electron spray ionization-mass spectrometry. Our results showed that acute DOX toxicity caused an induction of CYP1B1 and CYP4A enzymes and an inhibition of CYP2B1 and CYP2C11 in both the kidney and liver. CYP2E1 was induced and soluble epoxide hydrolase (sEH) was inhibited in the kidney only. In addition, DOX toxicity caused a significant increase in epoxyeicosatrienoic Acids formation in the kidney and a significant increase in 20-hydroxyeicosatetraenoic Acid formation in both the kidney and the liver. In conclusion, acute DOX toxicity alters the expression of several P450 and sEH enzymes in an organ-specific manner. These changes can be attributed to DOX-induced inflammation and resulted in altered P450-mediated Arachidonic Acid Metabolism.

Beshay N M Zordoky - One of the best experts on this subject based on the ideXlab platform.

  • acute doxorubicin toxicity differentially alters cytochrome p450 expression and Arachidonic Acid Metabolism in rat kidney and liver
    Drug Metabolism and Disposition, 2011
    Co-Authors: Beshay N M Zordoky, Anwar Anwarmohamed, Mona E Aboutabl, Ayman O S Elkadi
    Abstract:

    The use of doxorubicin (DOX) is limited by significant cardiotoxicity, nephrotoxicity, and hepatotoxicity. We have previously shown that DOX cardiotoxicity induces several cardiac cytochrome P450 (P450) enzymes with subsequent alteration in P450-mediated Arachidonic Acid Metabolism. Therefore, in the current study, we investigated the effect of acute DOX toxicity on P450 expression and Arachidonic Acid Metabolism in the kidney and liver of male Sprague-Dawley rats. Acute DOX toxicity was induced by a single intraperitoneal injection (15 mg/kg) of the drug. After 6 and 24 h, the kidneys and livers were harvested, and several P450 gene and protein expressions were determined by real-time polymerase chain reaction and Western blot analyses, respectively. Kidney and liver microsomal protein from control or DOX-treated rats was incubated with Arachidonic Acid, and its metabolites were determined by liquid chromatography-electron spray ionization-mass spectrometry. Our results showed that acute DOX toxicity caused an induction of CYP1B1 and CYP4A enzymes and an inhibition of CYP2B1 and CYP2C11 in both the kidney and liver. CYP2E1 was induced and soluble epoxide hydrolase (sEH) was inhibited in the kidney only. In addition, DOX toxicity caused a significant increase in epoxyeicosatrienoic Acids formation in the kidney and a significant increase in 20-hydroxyeicosatetraenoic Acid formation in both the kidney and the liver. In conclusion, acute DOX toxicity alters the expression of several P450 and sEH enzymes in an organ-specific manner. These changes can be attributed to DOX-induced inflammation and resulted in altered P450-mediated Arachidonic Acid Metabolism.

  • Acute Doxorubicin Toxicity Differentially Alters Cytochrome P450 Expression and Arachidonic Acid Metabolism in Rat Kidney and Liver
    Drug Metabolism and Disposition, 2011
    Co-Authors: Beshay N M Zordoky, Mona E Aboutabl, Anwar Anwar-mohamed, Ayman O.s. El-kadi
    Abstract:

    The use of doxorubicin (DOX) is limited by significant cardiotoxicity, nephrotoxicity, and hepatotoxicity. We have previously shown that DOX cardiotoxicity induces several cardiac cytochrome P450 (P450) enzymes with subsequent alteration in P450-mediated Arachidonic Acid Metabolism. Therefore, in the current study, we investigated the effect of acute DOX toxicity on P450 expression and Arachidonic Acid Metabolism in the kidney and liver of male Sprague Dawley rats. Acute DOX toxicity was induced by a single intraperitoneal injection of 15 mg/kg of the drug. After 6 and 24 h, the kidneys and livers were harvested and the expression of several P450 gene and protein expressions were determined by real time-PCR and Western blot analyses, respectively. Kidney and liver microsomal protein from control or DOX treated rats was incubated with Arachidonic Acid, and its metabolites were determined by liquid chromatography-electron spray ionization-mass spectrometry. Our results showed that acute DOX toxicity caused an induction of CYP1B1 and CYP4A enzymes and an inhibition of CYP2B1 and CYP2C11 in both the kidney and liver. CYP2E1 was induced and soluble epoxide hydrolase (sEH) was inhibited in the kidney only. In addition, DOX toxicity caused a significant increase in the epoxyeicosatrienoic Acids formation in the kidney and a significant increase in 20-hydroxyeicosatetraenoic Acid formation in both the kidney and the liver. In conclusion, acute DOX toxicity alters the expression of several P450 and sEH enzymes in an organ-specific manner. These changes can be attributed to DOX-induced inflammation and resulted in altered P450-mediated Arachidonic Acid Metabolism.

Mona E Aboutabl - One of the best experts on this subject based on the ideXlab platform.

  • acute doxorubicin toxicity differentially alters cytochrome p450 expression and Arachidonic Acid Metabolism in rat kidney and liver
    Drug Metabolism and Disposition, 2011
    Co-Authors: Beshay N M Zordoky, Anwar Anwarmohamed, Mona E Aboutabl, Ayman O S Elkadi
    Abstract:

    The use of doxorubicin (DOX) is limited by significant cardiotoxicity, nephrotoxicity, and hepatotoxicity. We have previously shown that DOX cardiotoxicity induces several cardiac cytochrome P450 (P450) enzymes with subsequent alteration in P450-mediated Arachidonic Acid Metabolism. Therefore, in the current study, we investigated the effect of acute DOX toxicity on P450 expression and Arachidonic Acid Metabolism in the kidney and liver of male Sprague-Dawley rats. Acute DOX toxicity was induced by a single intraperitoneal injection (15 mg/kg) of the drug. After 6 and 24 h, the kidneys and livers were harvested, and several P450 gene and protein expressions were determined by real-time polymerase chain reaction and Western blot analyses, respectively. Kidney and liver microsomal protein from control or DOX-treated rats was incubated with Arachidonic Acid, and its metabolites were determined by liquid chromatography-electron spray ionization-mass spectrometry. Our results showed that acute DOX toxicity caused an induction of CYP1B1 and CYP4A enzymes and an inhibition of CYP2B1 and CYP2C11 in both the kidney and liver. CYP2E1 was induced and soluble epoxide hydrolase (sEH) was inhibited in the kidney only. In addition, DOX toxicity caused a significant increase in epoxyeicosatrienoic Acids formation in the kidney and a significant increase in 20-hydroxyeicosatetraenoic Acid formation in both the kidney and the liver. In conclusion, acute DOX toxicity alters the expression of several P450 and sEH enzymes in an organ-specific manner. These changes can be attributed to DOX-induced inflammation and resulted in altered P450-mediated Arachidonic Acid Metabolism.

  • Acute Doxorubicin Toxicity Differentially Alters Cytochrome P450 Expression and Arachidonic Acid Metabolism in Rat Kidney and Liver
    Drug Metabolism and Disposition, 2011
    Co-Authors: Beshay N M Zordoky, Mona E Aboutabl, Anwar Anwar-mohamed, Ayman O.s. El-kadi
    Abstract:

    The use of doxorubicin (DOX) is limited by significant cardiotoxicity, nephrotoxicity, and hepatotoxicity. We have previously shown that DOX cardiotoxicity induces several cardiac cytochrome P450 (P450) enzymes with subsequent alteration in P450-mediated Arachidonic Acid Metabolism. Therefore, in the current study, we investigated the effect of acute DOX toxicity on P450 expression and Arachidonic Acid Metabolism in the kidney and liver of male Sprague Dawley rats. Acute DOX toxicity was induced by a single intraperitoneal injection of 15 mg/kg of the drug. After 6 and 24 h, the kidneys and livers were harvested and the expression of several P450 gene and protein expressions were determined by real time-PCR and Western blot analyses, respectively. Kidney and liver microsomal protein from control or DOX treated rats was incubated with Arachidonic Acid, and its metabolites were determined by liquid chromatography-electron spray ionization-mass spectrometry. Our results showed that acute DOX toxicity caused an induction of CYP1B1 and CYP4A enzymes and an inhibition of CYP2B1 and CYP2C11 in both the kidney and liver. CYP2E1 was induced and soluble epoxide hydrolase (sEH) was inhibited in the kidney only. In addition, DOX toxicity caused a significant increase in the epoxyeicosatrienoic Acids formation in the kidney and a significant increase in 20-hydroxyeicosatetraenoic Acid formation in both the kidney and the liver. In conclusion, acute DOX toxicity alters the expression of several P450 and sEH enzymes in an organ-specific manner. These changes can be attributed to DOX-induced inflammation and resulted in altered P450-mediated Arachidonic Acid Metabolism.

Anwar Anwarmohamed - One of the best experts on this subject based on the ideXlab platform.

  • acute doxorubicin toxicity differentially alters cytochrome p450 expression and Arachidonic Acid Metabolism in rat kidney and liver
    Drug Metabolism and Disposition, 2011
    Co-Authors: Beshay N M Zordoky, Anwar Anwarmohamed, Mona E Aboutabl, Ayman O S Elkadi
    Abstract:

    The use of doxorubicin (DOX) is limited by significant cardiotoxicity, nephrotoxicity, and hepatotoxicity. We have previously shown that DOX cardiotoxicity induces several cardiac cytochrome P450 (P450) enzymes with subsequent alteration in P450-mediated Arachidonic Acid Metabolism. Therefore, in the current study, we investigated the effect of acute DOX toxicity on P450 expression and Arachidonic Acid Metabolism in the kidney and liver of male Sprague-Dawley rats. Acute DOX toxicity was induced by a single intraperitoneal injection (15 mg/kg) of the drug. After 6 and 24 h, the kidneys and livers were harvested, and several P450 gene and protein expressions were determined by real-time polymerase chain reaction and Western blot analyses, respectively. Kidney and liver microsomal protein from control or DOX-treated rats was incubated with Arachidonic Acid, and its metabolites were determined by liquid chromatography-electron spray ionization-mass spectrometry. Our results showed that acute DOX toxicity caused an induction of CYP1B1 and CYP4A enzymes and an inhibition of CYP2B1 and CYP2C11 in both the kidney and liver. CYP2E1 was induced and soluble epoxide hydrolase (sEH) was inhibited in the kidney only. In addition, DOX toxicity caused a significant increase in epoxyeicosatrienoic Acids formation in the kidney and a significant increase in 20-hydroxyeicosatetraenoic Acid formation in both the kidney and the liver. In conclusion, acute DOX toxicity alters the expression of several P450 and sEH enzymes in an organ-specific manner. These changes can be attributed to DOX-induced inflammation and resulted in altered P450-mediated Arachidonic Acid Metabolism.

Kazuo Ohuchi - One of the best experts on this subject based on the ideXlab platform.

  • Stimulation of Arachidonic Acid Metabolism by a streptococcal preparation (OK-432) in rat peritoneal macrophages
    Biochimica et Biophysica Acta, 1992
    Co-Authors: Masako Watanabe, Hirota Fujiki, Noriyasu Hirasawa, Yoshiyuki Shishido, Kazuo Ohuchi
    Abstract:

    Abstract A streptococcal preparation OK-432 is reported to be an immunopotentiator and a potent antitumor agent. In order to elucidate the mechanism of biologic action, effects of OK-432 on Arachidonic Acid Metabolism in rat peritoneal macrophages were investigated. Prostaglandin E2 production and release of radioactivity from [3H]Arachidonic Acid-labeled macrophages were found to be stimulated by OK-432 in a concentration-dependent manner (5 to 80 μg/ml). Heat-treatment of OK-432 further stimulated its effects. These stimulative effects on Arachidonic Acid Metabolism by OK-432 were not observed in MDCK cells that have no phagocytic activity. Furthermore, cytochalasin B treatment completely suppressed the stimulative effects induced by OK-432 in macrophages. These results strongly indicate that the stimulative effects by OK-432 on Arachidonic Acid Metabolism are dependent on phagocytosis of OK-432 particles. Significance of stimulation of Arachidonic Acid Metabolism in macrophages by OK-432 for its bioligical effects is discussed.

  • Dual effects of staurosporine on Arachidonic Acid Metabolism in rat peritoneal macrophages
    Biochimica et Biophysica Acta, 1990
    Co-Authors: Masako Watanabe, Hirota Fujiki, Noriyasu Hirasawa, Tsuneo Ozeki, Susumu Tsurufuji, Toshiya Tamura, Mariko Ohashi, Kazuo Ohuchi
    Abstract:

    Abstract Staurosporine is a microbial anti-fungal alkaloid having a most potent inhibitory activity on protein kinase C and is recently found as a non-12-O-tetradecanoylphorbol-13-acetate (non-TPA)-type tumor promoter of mouse skin, although tumor promotion induced by a TPA-type tumor promoter teleocidin is suppressed by staurosporine. When rat peritoneal macrophages were incubated in the medium containing various concentrations of staurosporine, prostaglandin E2 production and release of radioactivity from [3H]Arachidonic Acid-labeled macrophages were stimulated at concentrations of 1 and 10 ng/ml. But higher concentrations of staurosporine such as 100 and 1000 ng/ml showed no stimulative effect on prostaglandin E2 production although cytoplasmic free calcium levels were increased in a dose-dependent manner. Staurosporine-induced stimulation of prostaglandin E2 production was inhibited by treatment with cycloheximide, suggesting that a certain protein synthesis is prerequisite for the stimulation of arahcidonic Acid Metabolism. At higher concentrations (100 and 1000 ng/ml), staurosporine inhibited TPA-type tumor promoter (TPA, teleocidin and aplysiatoxin)-induced stimulation of Arachidonic Acid Metabolism probably due to the inhibition of protein kinases. Tumor promotion activity and anti-tumor promotion activity of staurosporine might be explained by the fact that the lower concentrations of staurosporine stimulate Arachidonic Acid Metabolism and the higher concentrations of staurosporine inhibit the tumor promoter-induced Arachidonic Acid Metabolism, respectively.