Activation of nadph oxidase of human neutrophils. Potentiation of chemotactic peptide by a diacylglycerol
Formyl-methionyl-leucyl-phenylalanine (fMLP) and 1-oleoyl-2-acetyl-glycerol (OAG) are synergistic stimuli of the respiratory burst of neutrophils. Simultaneous exposure to both agents greatly enhanced superoxide production, both in rate and extent. OAG potentiated the response to fMLP also in Ca ++-...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1984-11, Vol.125 (1), p.367-373 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Dewald, Beatrice Payne, Trevor G. Baggiolini, Marco |
| description | Formyl-methionyl-leucyl-phenylalanine (fMLP) and 1-oleoyl-2-acetyl-glycerol (OAG) are synergistic stimuli of the respiratory burst of neutrophils. Simultaneous exposure to both agents greatly enhanced superoxide production, both in rate and extent. OAG potentiated the response to fMLP also in Ca
++-free medium. Pretreatment of the neutrophils with fMLP drastically shortened the lag of superoxide production in response to OAG. Our findings lead to the following conclusions: (i) Protein kinase C is likely to be involved in the activation of the NADPH oxidase by fMLP; (ii) OAG appears to be utilized as an intermediate in the activation process; (iii) prestimulation of the cells with fMLP facilitates the response to OAG. |
| doi_str_mv | 10.1016/S0006-291X(84)80377-0 |
| format | Article |
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++-free medium. Pretreatment of the neutrophils with fMLP drastically shortened the lag of superoxide production in response to OAG. Our findings lead to the following conclusions: (i) Protein kinase C is likely to be involved in the activation of the NADPH oxidase by fMLP; (ii) OAG appears to be utilized as an intermediate in the activation process; (iii) prestimulation of the cells with fMLP facilitates the response to OAG.</description><subject>Applied sciences</subject><subject>Cytochrome c Group - blood</subject><subject>Diglycerides - pharmacology</subject><subject>Drug Synergism</subject><subject>Enzyme Activation</subject><subject>Exact sciences and technology</subject><subject>Glycerides - pharmacology</subject><subject>Humans</subject><subject>N-Formylmethionine Leucyl-Phenylalanine - pharmacology</subject><subject>NADH, NADPH Oxidoreductases - blood</subject><subject>NADPH Oxidases</subject><subject>Neutrophils - enzymology</subject><subject>Other techniques and industries</subject><subject>Protein Kinase C</subject><subject>Protein Kinases - blood</subject><subject>Superoxides - blood</subject><subject>Time Factors</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkFGL1DAQx4Mo53r6EQ7yIOI99G6Spmn7JMfhqXDggQq-hXQydSNtU5P0cL-93dtlX30amPn9Z4YfYxcCrgQIff0NAHQhW_HzfaMuGyjruoBnbCOghUIKUM_Z5oS8ZK9S-g0ghNLtGTvT0FaNKjfM32D2jzb7MPHQ88m6ecvDX-9son1ju4x24hMtOYZ564d0xR9Cpin7Uwa3NIZs1z3IZ5qzd8S7HbfceYu74dewQ4pheM1e9HZI9OZYz9mPu4_fbz8X918_fbm9uS9QSciFAilV3aGr-xaU7ivsVVfWSFL32K0NYStXlxWWTdNB1SnqKk1KSqqpE1qW5-zdYe8cw5-FUjajT0jDYCcKSzJCQVsLrVewOoAYQ0qRejNHP9q4MwLMXrF5Umz2_kyjzJNiA2vu4nhg6UZyp9TR6Tp_e5zbhHboo53QpxPWNGWpZLtiHw4YrTIePUWT0NOE5HwkzMYF_59H_gFEFJn7</recordid><startdate>19841130</startdate><enddate>19841130</enddate><creator>Dewald, Beatrice</creator><creator>Payne, Trevor G.</creator><creator>Baggiolini, Marco</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</scope><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>7QR</scope><scope>7T5</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope></search><sort><creationdate>19841130</creationdate><title>Activation of nadph oxidase of human neutrophils. 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++-free medium. Pretreatment of the neutrophils with fMLP drastically shortened the lag of superoxide production in response to OAG. Our findings lead to the following conclusions: (i) Protein kinase C is likely to be involved in the activation of the NADPH oxidase by fMLP; (ii) OAG appears to be utilized as an intermediate in the activation process; (iii) prestimulation of the cells with fMLP facilitates the response to OAG.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>6095843</pmid><doi>10.1016/S0006-291X(84)80377-0</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Biochemical and biophysical research communications, 1984-11, Vol.125 (1), p.367-373 |
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| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Applied sciences Cytochrome c Group - blood Diglycerides - pharmacology Drug Synergism Enzyme Activation Exact sciences and technology Glycerides - pharmacology Humans N-Formylmethionine Leucyl-Phenylalanine - pharmacology NADH, NADPH Oxidoreductases - blood NADPH Oxidases Neutrophils - enzymology Other techniques and industries Protein Kinase C Protein Kinases - blood Superoxides - blood Time Factors |
| title | Activation of nadph oxidase of human neutrophils. Potentiation of chemotactic peptide by a diacylglycerol |
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