Evidence for Two Distinct Forms of Fatty Acid Cyclooxygenase in Brain
Abstract: The enzymatic metabolism of [14C]arachidonic acid (AA) was studied with microsomes prepared from rabbit medulla. Prostaglandin E2 (PGE2) levels, measured either by radiochemistry or radioimmunoassay, rose rapidly and abruptly plateaued within 5 min, while prostaglandin F2a (PGF2a) levels c...
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| Autor*in: |
Lysz, Thomas W. [verfasserIn] Needleman, Philip [verfasserIn] |
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E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1982 |
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Online-Ressource |
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2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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In: Journal of neurochemistry - Oxford : Wiley-Blackwell, 1956, 38(1982), 4, Seite 0 |
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volume:38 ; year:1982 ; number:4 ; pages:0 |
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10.1111/j.1471-4159.1982.tb05355.x |
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| 520 | |a Abstract: The enzymatic metabolism of [14C]arachidonic acid (AA) was studied with microsomes prepared from rabbit medulla. Prostaglandin E2 (PGE2) levels, measured either by radiochemistry or radioimmunoassay, rose rapidly and abruptly plateaued within 5 min, while prostaglandin F2a (PGF2a) levels continued to rise for 30 min. The rapid termination of PGE2 biosynthesis was not the result of limited cofactor, substrate, or product feedback inhibition, nor was it due to PGE2-9-ketoreductase activity. Inhibition of the PGH2→ PGE2 isomerase by arachidonic acid or its metabolites could not explain the abrupt halt in PGE2 biosynthesis. Proof for two separate cyclooxygenases comes from our observation that a preincubation of the brain microsomes with unlabeled AA eliminated PGE2 biosynthesis while PGF2o production continued. Further evidence to suggest two cyclooxygenases in brain is derived from the observation that indomethacin inhibited PGE2 production at concentrations that did not affect PGF2a biosynthesis. These results suggest that one fatty acid cyclooxygenase is closely associated with PGH2→ PGE2 isomerase and readily undergoes autodestruction and the second cyclooxygenase is associated with a PGH2→ PGF2a reductase and is somewhat resistant to arachidonate-induced destruction and to nonsteroidal antiinflammatory agents. | ||
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10.1111/j.1471-4159.1982.tb05355.x doi (DE-627)NLEJ240316800 DE-627 ger DE-627 rakwb Lysz, Thomas W. verfasserin aut Evidence for Two Distinct Forms of Fatty Acid Cyclooxygenase in Brain Oxford, UK Blackwell Publishing Ltd 1982 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The enzymatic metabolism of [14C]arachidonic acid (AA) was studied with microsomes prepared from rabbit medulla. Prostaglandin E2 (PGE2) levels, measured either by radiochemistry or radioimmunoassay, rose rapidly and abruptly plateaued within 5 min, while prostaglandin F2a (PGF2a) levels continued to rise for 30 min. The rapid termination of PGE2 biosynthesis was not the result of limited cofactor, substrate, or product feedback inhibition, nor was it due to PGE2-9-ketoreductase activity. Inhibition of the PGH2→ PGE2 isomerase by arachidonic acid or its metabolites could not explain the abrupt halt in PGE2 biosynthesis. Proof for two separate cyclooxygenases comes from our observation that a preincubation of the brain microsomes with unlabeled AA eliminated PGE2 biosynthesis while PGF2o production continued. Further evidence to suggest two cyclooxygenases in brain is derived from the observation that indomethacin inhibited PGE2 production at concentrations that did not affect PGF2a biosynthesis. These results suggest that one fatty acid cyclooxygenase is closely associated with PGH2→ PGE2 isomerase and readily undergoes autodestruction and the second cyclooxygenase is associated with a PGH2→ PGF2a reductase and is somewhat resistant to arachidonate-induced destruction and to nonsteroidal antiinflammatory agents. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Cyclooxygenase Needleman, Philip verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 38(1982), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:38 year:1982 number:4 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1982.tb05355.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 38 1982 4 0 |
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10.1111/j.1471-4159.1982.tb05355.x doi (DE-627)NLEJ240316800 DE-627 ger DE-627 rakwb Lysz, Thomas W. verfasserin aut Evidence for Two Distinct Forms of Fatty Acid Cyclooxygenase in Brain Oxford, UK Blackwell Publishing Ltd 1982 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The enzymatic metabolism of [14C]arachidonic acid (AA) was studied with microsomes prepared from rabbit medulla. Prostaglandin E2 (PGE2) levels, measured either by radiochemistry or radioimmunoassay, rose rapidly and abruptly plateaued within 5 min, while prostaglandin F2a (PGF2a) levels continued to rise for 30 min. The rapid termination of PGE2 biosynthesis was not the result of limited cofactor, substrate, or product feedback inhibition, nor was it due to PGE2-9-ketoreductase activity. Inhibition of the PGH2→ PGE2 isomerase by arachidonic acid or its metabolites could not explain the abrupt halt in PGE2 biosynthesis. Proof for two separate cyclooxygenases comes from our observation that a preincubation of the brain microsomes with unlabeled AA eliminated PGE2 biosynthesis while PGF2o production continued. Further evidence to suggest two cyclooxygenases in brain is derived from the observation that indomethacin inhibited PGE2 production at concentrations that did not affect PGF2a biosynthesis. These results suggest that one fatty acid cyclooxygenase is closely associated with PGH2→ PGE2 isomerase and readily undergoes autodestruction and the second cyclooxygenase is associated with a PGH2→ PGF2a reductase and is somewhat resistant to arachidonate-induced destruction and to nonsteroidal antiinflammatory agents. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Cyclooxygenase Needleman, Philip verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 38(1982), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:38 year:1982 number:4 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1982.tb05355.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 38 1982 4 0 |
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10.1111/j.1471-4159.1982.tb05355.x doi (DE-627)NLEJ240316800 DE-627 ger DE-627 rakwb Lysz, Thomas W. verfasserin aut Evidence for Two Distinct Forms of Fatty Acid Cyclooxygenase in Brain Oxford, UK Blackwell Publishing Ltd 1982 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The enzymatic metabolism of [14C]arachidonic acid (AA) was studied with microsomes prepared from rabbit medulla. Prostaglandin E2 (PGE2) levels, measured either by radiochemistry or radioimmunoassay, rose rapidly and abruptly plateaued within 5 min, while prostaglandin F2a (PGF2a) levels continued to rise for 30 min. The rapid termination of PGE2 biosynthesis was not the result of limited cofactor, substrate, or product feedback inhibition, nor was it due to PGE2-9-ketoreductase activity. Inhibition of the PGH2→ PGE2 isomerase by arachidonic acid or its metabolites could not explain the abrupt halt in PGE2 biosynthesis. Proof for two separate cyclooxygenases comes from our observation that a preincubation of the brain microsomes with unlabeled AA eliminated PGE2 biosynthesis while PGF2o production continued. Further evidence to suggest two cyclooxygenases in brain is derived from the observation that indomethacin inhibited PGE2 production at concentrations that did not affect PGF2a biosynthesis. These results suggest that one fatty acid cyclooxygenase is closely associated with PGH2→ PGE2 isomerase and readily undergoes autodestruction and the second cyclooxygenase is associated with a PGH2→ PGF2a reductase and is somewhat resistant to arachidonate-induced destruction and to nonsteroidal antiinflammatory agents. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Cyclooxygenase Needleman, Philip verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 38(1982), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:38 year:1982 number:4 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1982.tb05355.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 38 1982 4 0 |
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10.1111/j.1471-4159.1982.tb05355.x doi (DE-627)NLEJ240316800 DE-627 ger DE-627 rakwb Lysz, Thomas W. verfasserin aut Evidence for Two Distinct Forms of Fatty Acid Cyclooxygenase in Brain Oxford, UK Blackwell Publishing Ltd 1982 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The enzymatic metabolism of [14C]arachidonic acid (AA) was studied with microsomes prepared from rabbit medulla. Prostaglandin E2 (PGE2) levels, measured either by radiochemistry or radioimmunoassay, rose rapidly and abruptly plateaued within 5 min, while prostaglandin F2a (PGF2a) levels continued to rise for 30 min. The rapid termination of PGE2 biosynthesis was not the result of limited cofactor, substrate, or product feedback inhibition, nor was it due to PGE2-9-ketoreductase activity. Inhibition of the PGH2→ PGE2 isomerase by arachidonic acid or its metabolites could not explain the abrupt halt in PGE2 biosynthesis. Proof for two separate cyclooxygenases comes from our observation that a preincubation of the brain microsomes with unlabeled AA eliminated PGE2 biosynthesis while PGF2o production continued. Further evidence to suggest two cyclooxygenases in brain is derived from the observation that indomethacin inhibited PGE2 production at concentrations that did not affect PGF2a biosynthesis. These results suggest that one fatty acid cyclooxygenase is closely associated with PGH2→ PGE2 isomerase and readily undergoes autodestruction and the second cyclooxygenase is associated with a PGH2→ PGF2a reductase and is somewhat resistant to arachidonate-induced destruction and to nonsteroidal antiinflammatory agents. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Cyclooxygenase Needleman, Philip verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 38(1982), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:38 year:1982 number:4 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1982.tb05355.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 38 1982 4 0 |
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10.1111/j.1471-4159.1982.tb05355.x doi (DE-627)NLEJ240316800 DE-627 ger DE-627 rakwb Lysz, Thomas W. verfasserin aut Evidence for Two Distinct Forms of Fatty Acid Cyclooxygenase in Brain Oxford, UK Blackwell Publishing Ltd 1982 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: The enzymatic metabolism of [14C]arachidonic acid (AA) was studied with microsomes prepared from rabbit medulla. Prostaglandin E2 (PGE2) levels, measured either by radiochemistry or radioimmunoassay, rose rapidly and abruptly plateaued within 5 min, while prostaglandin F2a (PGF2a) levels continued to rise for 30 min. The rapid termination of PGE2 biosynthesis was not the result of limited cofactor, substrate, or product feedback inhibition, nor was it due to PGE2-9-ketoreductase activity. Inhibition of the PGH2→ PGE2 isomerase by arachidonic acid or its metabolites could not explain the abrupt halt in PGE2 biosynthesis. Proof for two separate cyclooxygenases comes from our observation that a preincubation of the brain microsomes with unlabeled AA eliminated PGE2 biosynthesis while PGF2o production continued. Further evidence to suggest two cyclooxygenases in brain is derived from the observation that indomethacin inhibited PGE2 production at concentrations that did not affect PGF2a biosynthesis. These results suggest that one fatty acid cyclooxygenase is closely associated with PGH2→ PGE2 isomerase and readily undergoes autodestruction and the second cyclooxygenase is associated with a PGH2→ PGF2a reductase and is somewhat resistant to arachidonate-induced destruction and to nonsteroidal antiinflammatory agents. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Cyclooxygenase Needleman, Philip verfasserin aut In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 38(1982), 4, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:38 year:1982 number:4 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1982.tb05355.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 38 1982 4 0 |
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Evidence for Two Distinct Forms of Fatty Acid Cyclooxygenase in Brain |
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Abstract: The enzymatic metabolism of [14C]arachidonic acid (AA) was studied with microsomes prepared from rabbit medulla. Prostaglandin E2 (PGE2) levels, measured either by radiochemistry or radioimmunoassay, rose rapidly and abruptly plateaued within 5 min, while prostaglandin F2a (PGF2a) levels continued to rise for 30 min. The rapid termination of PGE2 biosynthesis was not the result of limited cofactor, substrate, or product feedback inhibition, nor was it due to PGE2-9-ketoreductase activity. Inhibition of the PGH2→ PGE2 isomerase by arachidonic acid or its metabolites could not explain the abrupt halt in PGE2 biosynthesis. Proof for two separate cyclooxygenases comes from our observation that a preincubation of the brain microsomes with unlabeled AA eliminated PGE2 biosynthesis while PGF2o production continued. Further evidence to suggest two cyclooxygenases in brain is derived from the observation that indomethacin inhibited PGE2 production at concentrations that did not affect PGF2a biosynthesis. These results suggest that one fatty acid cyclooxygenase is closely associated with PGH2→ PGE2 isomerase and readily undergoes autodestruction and the second cyclooxygenase is associated with a PGH2→ PGF2a reductase and is somewhat resistant to arachidonate-induced destruction and to nonsteroidal antiinflammatory agents. |
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Abstract: The enzymatic metabolism of [14C]arachidonic acid (AA) was studied with microsomes prepared from rabbit medulla. Prostaglandin E2 (PGE2) levels, measured either by radiochemistry or radioimmunoassay, rose rapidly and abruptly plateaued within 5 min, while prostaglandin F2a (PGF2a) levels continued to rise for 30 min. The rapid termination of PGE2 biosynthesis was not the result of limited cofactor, substrate, or product feedback inhibition, nor was it due to PGE2-9-ketoreductase activity. Inhibition of the PGH2→ PGE2 isomerase by arachidonic acid or its metabolites could not explain the abrupt halt in PGE2 biosynthesis. Proof for two separate cyclooxygenases comes from our observation that a preincubation of the brain microsomes with unlabeled AA eliminated PGE2 biosynthesis while PGF2o production continued. Further evidence to suggest two cyclooxygenases in brain is derived from the observation that indomethacin inhibited PGE2 production at concentrations that did not affect PGF2a biosynthesis. These results suggest that one fatty acid cyclooxygenase is closely associated with PGH2→ PGE2 isomerase and readily undergoes autodestruction and the second cyclooxygenase is associated with a PGH2→ PGF2a reductase and is somewhat resistant to arachidonate-induced destruction and to nonsteroidal antiinflammatory agents. |
| abstract_unstemmed |
Abstract: The enzymatic metabolism of [14C]arachidonic acid (AA) was studied with microsomes prepared from rabbit medulla. Prostaglandin E2 (PGE2) levels, measured either by radiochemistry or radioimmunoassay, rose rapidly and abruptly plateaued within 5 min, while prostaglandin F2a (PGF2a) levels continued to rise for 30 min. The rapid termination of PGE2 biosynthesis was not the result of limited cofactor, substrate, or product feedback inhibition, nor was it due to PGE2-9-ketoreductase activity. Inhibition of the PGH2→ PGE2 isomerase by arachidonic acid or its metabolites could not explain the abrupt halt in PGE2 biosynthesis. Proof for two separate cyclooxygenases comes from our observation that a preincubation of the brain microsomes with unlabeled AA eliminated PGE2 biosynthesis while PGF2o production continued. Further evidence to suggest two cyclooxygenases in brain is derived from the observation that indomethacin inhibited PGE2 production at concentrations that did not affect PGF2a biosynthesis. These results suggest that one fatty acid cyclooxygenase is closely associated with PGH2→ PGE2 isomerase and readily undergoes autodestruction and the second cyclooxygenase is associated with a PGH2→ PGF2a reductase and is somewhat resistant to arachidonate-induced destruction and to nonsteroidal antiinflammatory agents. |
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Evidence for Two Distinct Forms of Fatty Acid Cyclooxygenase in Brain |
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http://dx.doi.org/10.1111/j.1471-4159.1982.tb05355.x |
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Needleman, Philip |
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Needleman, Philip |
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| doi_str |
10.1111/j.1471-4159.1982.tb05355.x |
| up_date |
2024-07-06T09:41:13.005Z |
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Prostaglandin E2 (PGE2) levels, measured either by radiochemistry or radioimmunoassay, rose rapidly and abruptly plateaued within 5 min, while prostaglandin F2a (PGF2a) levels continued to rise for 30 min. The rapid termination of PGE2 biosynthesis was not the result of limited cofactor, substrate, or product feedback inhibition, nor was it due to PGE2-9-ketoreductase activity. Inhibition of the PGH2→ PGE2 isomerase by arachidonic acid or its metabolites could not explain the abrupt halt in PGE2 biosynthesis. Proof for two separate cyclooxygenases comes from our observation that a preincubation of the brain microsomes with unlabeled AA eliminated PGE2 biosynthesis while PGF2o production continued. Further evidence to suggest two cyclooxygenases in brain is derived from the observation that indomethacin inhibited PGE2 production at concentrations that did not affect PGF2a biosynthesis. These results suggest that one fatty acid cyclooxygenase is closely associated with PGH2→ PGE2 isomerase and readily undergoes autodestruction and the second cyclooxygenase is associated with a PGH2→ PGF2a reductase and is somewhat resistant to arachidonate-induced destruction and to nonsteroidal antiinflammatory agents.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2006</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2006||||||||||</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Cyclooxygenase</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Needleman, Philip</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">Journal of neurochemistry</subfield><subfield code="d">Oxford : Wiley-Blackwell, 1956</subfield><subfield code="g">38(1982), 4, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243927584</subfield><subfield code="w">(DE-600)2020528-4</subfield><subfield code="x">1471-4159</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:38</subfield><subfield code="g">year:1982</subfield><subfield code="g">number:4</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1111/j.1471-4159.1982.tb05355.x</subfield><subfield code="q">text/html</subfield><subfield code="x">Verlag</subfield><subfield code="z">Deutschlandweit zugänglich</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-DJB</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">38</subfield><subfield code="j">1982</subfield><subfield code="e">4</subfield><subfield code="h">0</subfield></datafield></record></collection>
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7.400983 |