The Selenoenzyme Phospholipid Hydroperoxide Glutathione Peroxidase Controls the Activity of the 15-Lipoxygenase with Complex Substrates and Preserves the Specificity of the Oxygenation Products
Mammalian 15-lipoxygenases have been suggested to be involved in cell differentiation and atherogenesis because of their capability of oxygenating polyenoic fatty acids esterified to biomembranes and lipoproteins. We investigated the interaction of the lipid-peroxidizing 15-lipoxygenase and the hydr...
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| Veröffentlicht in: | The Journal of biological chemistry 1996-03, Vol.271 (9), p.4653-4658 |
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| creator | Schnurr, Kerstin Belkner, Jutta Ursini, Fulvio Schewe, Tankred Kühn, Hartmut |
| description | Mammalian 15-lipoxygenases have been suggested to be involved in cell differentiation and atherogenesis because of their capability
of oxygenating polyenoic fatty acids esterified to biomembranes and lipoproteins. We investigated the interaction of the lipid-peroxidizing
15-lipoxygenase and the hydroperoxy lipid-reducing phospholipid hydroperoxide glutathione peroxidase during their reaction
with biomembranes and lipoproteins and obtained the following results. 1) Lipoxygenase treatment of submitochondrial membranes
led to the formation of hydroperoxyphosphatidylethanolamine and hydroperoxyphosphatidylcholine as indicated by high performance
liquid chromatography with chemiluminescence detection. In 15-lipoxygenase-treated low density lipoprotein cholesteryl hydroperoxylinoleate
was the major oxygenation product. 2) Phospholipid hydroperoxide glutathione peroxidase was capable of reducing the hydroperoxy
lipids formed by the 15-lipoxygenase to their corresponding alcohols. 3) Preincubation of low density lipoprotein and submitochondrial
membranes with the phospholipid hydroperoxide glutathione peroxidase completely prevented the lipoxygenase reaction. However,
addition of exogenous hydroperoxy lipids restored the oxygenase activity. 4) Short-term incubations of the complex substrates
with the 15-lipoxygenase led to a specific pattern of oxidation products which was rendered more unspecific at long-term incubation
or at high substrate concentrations. If the phosholipid hydroperoxide glutathione peroxidase was present during the reaction,
the specific product pattern was preserved.
These data indicate that the phospholipid hydroperoxide glutathione peroxidase is capable of reducing hydroperoxy ester lipids
formed by a 15-lipoxygenase, and that it may down-regulate the 15-lipoxygenase pathways in mammalian cells. The specificity
of 15-lipoxygenase-derived hydroperoxy lipids depends on their immediate reduction to the corresponding alcohols preventing
postcatalytic isomerization. |
| doi_str_mv | 10.1074/jbc.271.9.4653 |
| format | Article |
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of oxygenating polyenoic fatty acids esterified to biomembranes and lipoproteins. We investigated the interaction of the lipid-peroxidizing
15-lipoxygenase and the hydroperoxy lipid-reducing phospholipid hydroperoxide glutathione peroxidase during their reaction
with biomembranes and lipoproteins and obtained the following results. 1) Lipoxygenase treatment of submitochondrial membranes
led to the formation of hydroperoxyphosphatidylethanolamine and hydroperoxyphosphatidylcholine as indicated by high performance
liquid chromatography with chemiluminescence detection. In 15-lipoxygenase-treated low density lipoprotein cholesteryl hydroperoxylinoleate
was the major oxygenation product. 2) Phospholipid hydroperoxide glutathione peroxidase was capable of reducing the hydroperoxy
lipids formed by the 15-lipoxygenase to their corresponding alcohols. 3) Preincubation of low density lipoprotein and submitochondrial
membranes with the phospholipid hydroperoxide glutathione peroxidase completely prevented the lipoxygenase reaction. However,
addition of exogenous hydroperoxy lipids restored the oxygenase activity. 4) Short-term incubations of the complex substrates
with the 15-lipoxygenase led to a specific pattern of oxidation products which was rendered more unspecific at long-term incubation
or at high substrate concentrations. If the phosholipid hydroperoxide glutathione peroxidase was present during the reaction,
the specific product pattern was preserved.
These data indicate that the phospholipid hydroperoxide glutathione peroxidase is capable of reducing hydroperoxy ester lipids
formed by a 15-lipoxygenase, and that it may down-regulate the 15-lipoxygenase pathways in mammalian cells. The specificity
of 15-lipoxygenase-derived hydroperoxy lipids depends on their immediate reduction to the corresponding alcohols preventing
postcatalytic isomerization.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.271.9.4653</identifier><identifier>PMID: 8617728</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Alcohols - analysis ; Alcohols - metabolism ; Animals ; Arachidonate 15-Lipoxygenase - metabolism ; Cattle ; Glutathione Peroxidase - metabolism ; Humans ; Intracellular Membranes - enzymology ; Kinetics ; Lipid Peroxides - isolation & purification ; Lipid Peroxides - metabolism ; Lipoproteins, LDL - blood ; Lipoproteins, LDL - isolation & purification ; Mammals ; Mitochondria, Heart - enzymology ; Oxidation-Reduction ; Phospholipid Hydroperoxide Glutathione Peroxidase ; Rabbits ; Reticulocytes - enzymology ; Submitochondrial Particles - enzymology ; Substrate Specificity ; Time Factors</subject><ispartof>The Journal of biological chemistry, 1996-03, Vol.271 (9), p.4653-4658</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-d4d8166c20ca96ae6818979a4253bfbb23359aaa19d23e07d79ad30e9634c7c93</citedby><cites>FETCH-LOGICAL-c357t-d4d8166c20ca96ae6818979a4253bfbb23359aaa19d23e07d79ad30e9634c7c93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8617728$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schnurr, Kerstin</creatorcontrib><creatorcontrib>Belkner, Jutta</creatorcontrib><creatorcontrib>Ursini, Fulvio</creatorcontrib><creatorcontrib>Schewe, Tankred</creatorcontrib><creatorcontrib>Kühn, Hartmut</creatorcontrib><title>The Selenoenzyme Phospholipid Hydroperoxide Glutathione Peroxidase Controls the Activity of the 15-Lipoxygenase with Complex Substrates and Preserves the Specificity of the Oxygenation Products</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Mammalian 15-lipoxygenases have been suggested to be involved in cell differentiation and atherogenesis because of their capability
of oxygenating polyenoic fatty acids esterified to biomembranes and lipoproteins. We investigated the interaction of the lipid-peroxidizing
15-lipoxygenase and the hydroperoxy lipid-reducing phospholipid hydroperoxide glutathione peroxidase during their reaction
with biomembranes and lipoproteins and obtained the following results. 1) Lipoxygenase treatment of submitochondrial membranes
led to the formation of hydroperoxyphosphatidylethanolamine and hydroperoxyphosphatidylcholine as indicated by high performance
liquid chromatography with chemiluminescence detection. In 15-lipoxygenase-treated low density lipoprotein cholesteryl hydroperoxylinoleate
was the major oxygenation product. 2) Phospholipid hydroperoxide glutathione peroxidase was capable of reducing the hydroperoxy
lipids formed by the 15-lipoxygenase to their corresponding alcohols. 3) Preincubation of low density lipoprotein and submitochondrial
membranes with the phospholipid hydroperoxide glutathione peroxidase completely prevented the lipoxygenase reaction. However,
addition of exogenous hydroperoxy lipids restored the oxygenase activity. 4) Short-term incubations of the complex substrates
with the 15-lipoxygenase led to a specific pattern of oxidation products which was rendered more unspecific at long-term incubation
or at high substrate concentrations. If the phosholipid hydroperoxide glutathione peroxidase was present during the reaction,
the specific product pattern was preserved.
These data indicate that the phospholipid hydroperoxide glutathione peroxidase is capable of reducing hydroperoxy ester lipids
formed by a 15-lipoxygenase, and that it may down-regulate the 15-lipoxygenase pathways in mammalian cells. The specificity
of 15-lipoxygenase-derived hydroperoxy lipids depends on their immediate reduction to the corresponding alcohols preventing
postcatalytic isomerization.</description><subject>Alcohols - analysis</subject><subject>Alcohols - metabolism</subject><subject>Animals</subject><subject>Arachidonate 15-Lipoxygenase - metabolism</subject><subject>Cattle</subject><subject>Glutathione Peroxidase - metabolism</subject><subject>Humans</subject><subject>Intracellular Membranes - enzymology</subject><subject>Kinetics</subject><subject>Lipid Peroxides - isolation & purification</subject><subject>Lipid Peroxides - metabolism</subject><subject>Lipoproteins, LDL - blood</subject><subject>Lipoproteins, LDL - isolation & purification</subject><subject>Mammals</subject><subject>Mitochondria, Heart - enzymology</subject><subject>Oxidation-Reduction</subject><subject>Phospholipid Hydroperoxide Glutathione Peroxidase</subject><subject>Rabbits</subject><subject>Reticulocytes - enzymology</subject><subject>Submitochondrial Particles - enzymology</subject><subject>Substrate Specificity</subject><subject>Time Factors</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkc1q3DAURkVpSadpt90VRBfd2ZEs_2kZhjQpDCQwKXQnZOk6VrAtV5KTcd-ub1ZNPYRoI6Tv3MOFD6HPlKSUVPnFY6PSrKIpT_OyYG_QhpKaJaygv96iDSEZTXhW1O_RB-8fSTw5p2forC5pVWX1Bv297wDvoYfRwvhnGQDfddZPne3NZDS-WbSzEzh7MBrwdT8HGTpjx4itn9ID3toxONt7HKLrUgXzZMKCbfv_TYtkZyZ7WB5gPMLPJnRxYph6OOD93PjgZACP5ajxnQMP7glW034CZVqjXsluV02IG0TY6lkF_xG9a2Xv4dPpPkc_v1_db2-S3e31j-3lLlGsqEKic13TslQZUZKXEsqa1rziMs8K1rRNkzFWcCkl5TpjQCodM80I8JLlqlKcnaNvq3dy9vcMPojBeAV9L0ewsxdVTYqsLvIIpiuonPXeQSsmZwbpFkGJOHYmYmcidia4OHYWB76czHMzgH7BTyXF_Ouad-ahezYORGOs6mB4LfkHZcejdw</recordid><startdate>19960301</startdate><enddate>19960301</enddate><creator>Schnurr, Kerstin</creator><creator>Belkner, Jutta</creator><creator>Ursini, Fulvio</creator><creator>Schewe, Tankred</creator><creator>Kühn, Hartmut</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19960301</creationdate><title>The Selenoenzyme Phospholipid Hydroperoxide Glutathione Peroxidase Controls the Activity of the 15-Lipoxygenase with Complex Substrates and Preserves the Specificity of the Oxygenation Products</title><author>Schnurr, Kerstin ; Belkner, Jutta ; Ursini, Fulvio ; Schewe, Tankred ; Kühn, Hartmut</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-d4d8166c20ca96ae6818979a4253bfbb23359aaa19d23e07d79ad30e9634c7c93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Alcohols - analysis</topic><topic>Alcohols - metabolism</topic><topic>Animals</topic><topic>Arachidonate 15-Lipoxygenase - metabolism</topic><topic>Cattle</topic><topic>Glutathione Peroxidase - metabolism</topic><topic>Humans</topic><topic>Intracellular Membranes - enzymology</topic><topic>Kinetics</topic><topic>Lipid Peroxides - isolation & purification</topic><topic>Lipid Peroxides - metabolism</topic><topic>Lipoproteins, LDL - blood</topic><topic>Lipoproteins, LDL - isolation & purification</topic><topic>Mammals</topic><topic>Mitochondria, Heart - enzymology</topic><topic>Oxidation-Reduction</topic><topic>Phospholipid Hydroperoxide Glutathione Peroxidase</topic><topic>Rabbits</topic><topic>Reticulocytes - enzymology</topic><topic>Submitochondrial Particles - enzymology</topic><topic>Substrate Specificity</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schnurr, Kerstin</creatorcontrib><creatorcontrib>Belkner, Jutta</creatorcontrib><creatorcontrib>Ursini, Fulvio</creatorcontrib><creatorcontrib>Schewe, Tankred</creatorcontrib><creatorcontrib>Kühn, Hartmut</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schnurr, Kerstin</au><au>Belkner, Jutta</au><au>Ursini, Fulvio</au><au>Schewe, Tankred</au><au>Kühn, Hartmut</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Selenoenzyme Phospholipid Hydroperoxide Glutathione Peroxidase Controls the Activity of the 15-Lipoxygenase with Complex Substrates and Preserves the Specificity of the Oxygenation Products</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1996-03-01</date><risdate>1996</risdate><volume>271</volume><issue>9</issue><spage>4653</spage><epage>4658</epage><pages>4653-4658</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Mammalian 15-lipoxygenases have been suggested to be involved in cell differentiation and atherogenesis because of their capability
of oxygenating polyenoic fatty acids esterified to biomembranes and lipoproteins. We investigated the interaction of the lipid-peroxidizing
15-lipoxygenase and the hydroperoxy lipid-reducing phospholipid hydroperoxide glutathione peroxidase during their reaction
with biomembranes and lipoproteins and obtained the following results. 1) Lipoxygenase treatment of submitochondrial membranes
led to the formation of hydroperoxyphosphatidylethanolamine and hydroperoxyphosphatidylcholine as indicated by high performance
liquid chromatography with chemiluminescence detection. In 15-lipoxygenase-treated low density lipoprotein cholesteryl hydroperoxylinoleate
was the major oxygenation product. 2) Phospholipid hydroperoxide glutathione peroxidase was capable of reducing the hydroperoxy
lipids formed by the 15-lipoxygenase to their corresponding alcohols. 3) Preincubation of low density lipoprotein and submitochondrial
membranes with the phospholipid hydroperoxide glutathione peroxidase completely prevented the lipoxygenase reaction. However,
addition of exogenous hydroperoxy lipids restored the oxygenase activity. 4) Short-term incubations of the complex substrates
with the 15-lipoxygenase led to a specific pattern of oxidation products which was rendered more unspecific at long-term incubation
or at high substrate concentrations. If the phosholipid hydroperoxide glutathione peroxidase was present during the reaction,
the specific product pattern was preserved.
These data indicate that the phospholipid hydroperoxide glutathione peroxidase is capable of reducing hydroperoxy ester lipids
formed by a 15-lipoxygenase, and that it may down-regulate the 15-lipoxygenase pathways in mammalian cells. The specificity
of 15-lipoxygenase-derived hydroperoxy lipids depends on their immediate reduction to the corresponding alcohols preventing
postcatalytic isomerization.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8617728</pmid><doi>10.1074/jbc.271.9.4653</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1996-03, Vol.271 (9), p.4653-4658 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78052854 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Alcohols - analysis Alcohols - metabolism Animals Arachidonate 15-Lipoxygenase - metabolism Cattle Glutathione Peroxidase - metabolism Humans Intracellular Membranes - enzymology Kinetics Lipid Peroxides - isolation & purification Lipid Peroxides - metabolism Lipoproteins, LDL - blood Lipoproteins, LDL - isolation & purification Mammals Mitochondria, Heart - enzymology Oxidation-Reduction Phospholipid Hydroperoxide Glutathione Peroxidase Rabbits Reticulocytes - enzymology Submitochondrial Particles - enzymology Substrate Specificity Time Factors |
| title | The Selenoenzyme Phospholipid Hydroperoxide Glutathione Peroxidase Controls the Activity of the 15-Lipoxygenase with Complex Substrates and Preserves the Specificity of the Oxygenation Products |
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