Modulation of platelet-activating factor (PAF) synthesis and release from human polymorphonuclear leukocytes (PMN): Role of extracellular albumin
Human neutrophilic polymorphonuclear leukocytes (PMN) stimulated with N′-formyl-methionyl-leucyl-phenylalanine (FMLP) in the presence of cytochalasin B but in the absence of human serum albumin (HSA) synthesized only small amounts of platelet-activating factor (PAF) that attained maximum levels with...
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Veröffentlicht in: | Archives of biochemistry and biophysics 1985-09, Vol.241 (2), p.337-347 |
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creator | Ludwig, Janet C. Hoppens, Carol L. McManus, Linda M. Mott, Glen E. Pinckard, R.Neal |
description | Human neutrophilic polymorphonuclear leukocytes (PMN) stimulated with
N′-formyl-methionyl-leucyl-phenylalanine (FMLP) in the presence of cytochalasin B but in the absence of human serum albumin (HSA) synthesized only small amounts of platelet-activating factor (PAF) that attained maximum levels within 60–120 s after stimulation; in addition, no release of PAF occurred. However, in the presence of 2.5 mg HSA/ml, there was a threefold increase in PAF synthesis, 30–40% of which was released within 5 min after FMLP stimulation. In the presence of 50 mg HSA/ml there was at least a fourfold increase in PAF synthesis and release, with maximal synthesis occurring 10–20 min after stimulation. Thus, the presence of HSA during PMN stimulation not only induced an albumin dose-dependent increase in PAF release but significantly augmented the synthesis of PAF. In contrast to PAF synthesis and release, the presence or absence of HSA had no effect upon lysosomal enzyme secretion from FMLP-stimulated PMN, which was maximal within 30–60 s after stimulation. These results demonstrate that HSA plays an essential role
in vitro in the synthesis and release of PAF from human PMN, and support the hypothesis that there is a cyclic PAF synthesis-release coupling mechanism in the stimulated human PMN. |
doi_str_mv | 10.1016/0003-9861(85)90555-7 |
format | Article |
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N′-formyl-methionyl-leucyl-phenylalanine (FMLP) in the presence of cytochalasin B but in the absence of human serum albumin (HSA) synthesized only small amounts of platelet-activating factor (PAF) that attained maximum levels within 60–120 s after stimulation; in addition, no release of PAF occurred. However, in the presence of 2.5 mg HSA/ml, there was a threefold increase in PAF synthesis, 30–40% of which was released within 5 min after FMLP stimulation. In the presence of 50 mg HSA/ml there was at least a fourfold increase in PAF synthesis and release, with maximal synthesis occurring 10–20 min after stimulation. Thus, the presence of HSA during PMN stimulation not only induced an albumin dose-dependent increase in PAF release but significantly augmented the synthesis of PAF. In contrast to PAF synthesis and release, the presence or absence of HSA had no effect upon lysosomal enzyme secretion from FMLP-stimulated PMN, which was maximal within 30–60 s after stimulation. These results demonstrate that HSA plays an essential role
in vitro in the synthesis and release of PAF from human PMN, and support the hypothesis that there is a cyclic PAF synthesis-release coupling mechanism in the stimulated human PMN.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(85)90555-7</identifier><identifier>PMID: 4037794</identifier><identifier>CODEN: ABBIA4</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Applied sciences ; Calcium - pharmacology ; Dose-Response Relationship, Drug ; Exact sciences and technology ; Humans ; In Vitro Techniques ; Kinetics ; N-Formylmethionine Leucyl-Phenylalanine - pharmacology ; Neutrophils - metabolism ; Other techniques and industries ; Platelet Activating Factor - biosynthesis ; Platelet Activating Factor - isolation & purification ; Serum Albumin - pharmacology ; Tritium</subject><ispartof>Archives of biochemistry and biophysics, 1985-09, Vol.241 (2), p.337-347</ispartof><rights>1985</rights><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c452t-8efa06038ad426375bbd14a0d4c913232282edd9610137e87712b7e1e8396f1a3</citedby><cites>FETCH-LOGICAL-c452t-8efa06038ad426375bbd14a0d4c913232282edd9610137e87712b7e1e8396f1a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0003986185905557$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8841555$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4037794$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ludwig, Janet C.</creatorcontrib><creatorcontrib>Hoppens, Carol L.</creatorcontrib><creatorcontrib>McManus, Linda M.</creatorcontrib><creatorcontrib>Mott, Glen E.</creatorcontrib><creatorcontrib>Pinckard, R.Neal</creatorcontrib><title>Modulation of platelet-activating factor (PAF) synthesis and release from human polymorphonuclear leukocytes (PMN): Role of extracellular albumin</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>Human neutrophilic polymorphonuclear leukocytes (PMN) stimulated with
N′-formyl-methionyl-leucyl-phenylalanine (FMLP) in the presence of cytochalasin B but in the absence of human serum albumin (HSA) synthesized only small amounts of platelet-activating factor (PAF) that attained maximum levels within 60–120 s after stimulation; in addition, no release of PAF occurred. However, in the presence of 2.5 mg HSA/ml, there was a threefold increase in PAF synthesis, 30–40% of which was released within 5 min after FMLP stimulation. In the presence of 50 mg HSA/ml there was at least a fourfold increase in PAF synthesis and release, with maximal synthesis occurring 10–20 min after stimulation. Thus, the presence of HSA during PMN stimulation not only induced an albumin dose-dependent increase in PAF release but significantly augmented the synthesis of PAF. In contrast to PAF synthesis and release, the presence or absence of HSA had no effect upon lysosomal enzyme secretion from FMLP-stimulated PMN, which was maximal within 30–60 s after stimulation. These results demonstrate that HSA plays an essential role
in vitro in the synthesis and release of PAF from human PMN, and support the hypothesis that there is a cyclic PAF synthesis-release coupling mechanism in the stimulated human PMN.</description><subject>Applied sciences</subject><subject>Calcium - pharmacology</subject><subject>Dose-Response Relationship, Drug</subject><subject>Exact sciences and technology</subject><subject>Humans</subject><subject>In Vitro Techniques</subject><subject>Kinetics</subject><subject>N-Formylmethionine Leucyl-Phenylalanine - pharmacology</subject><subject>Neutrophils - metabolism</subject><subject>Other techniques and industries</subject><subject>Platelet Activating Factor - biosynthesis</subject><subject>Platelet Activating Factor - isolation & purification</subject><subject>Serum Albumin - pharmacology</subject><subject>Tritium</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kdGO1CAUhhujWcfVN9CEC2N2LqpQKFAvTDYbV0121Ri9JhROHZRChXbjPIZvLHUmc-kVJ_zf-Tn8p6qeEvySYMJfYYxp3UlOLmS77XDbtrW4V20I7niNqWT3q80JeVg9yvkHxoQw3pxVZwxTITq2qf7cRrt4PbsYUBzQVErwMNfazO6uXIfvaCh1TOji8-X1FuV9mHeQXUY6WJQKqzOgIcUR7ZZRBzRFvx9jmnYxLKaoCXlYfkaznyEXj9uP29foS_Swvga_56QNeF8mSEj7fhldeFw9GLTP8OR4nlffrt9-vXpf33x69-Hq8qY2rG3mWsKgMS__1JY1nIq27y1hGltmOkIb2jSyAWs7XrKiAqQQpOkFEJC04wPR9Lx6cfCdUvy1QJ7V6PI6jA4Ql6wEp7xpJSkgO4AmxZwTDGpKbtRprwhW6ybUGrNaY1ayVf82oURpe3b0X_oR7KnpGH3Rnx91nY32Q9LBuHzCpGSkGBXszQGDksWdg6SycRAMWJfAzMpG9_85_gJRB6YE</recordid><startdate>198509</startdate><enddate>198509</enddate><creator>Ludwig, Janet C.</creator><creator>Hoppens, Carol L.</creator><creator>McManus, Linda M.</creator><creator>Mott, Glen E.</creator><creator>Pinckard, R.Neal</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>7X8</scope></search><sort><creationdate>198509</creationdate><title>Modulation of platelet-activating factor (PAF) synthesis and release from human polymorphonuclear leukocytes (PMN): Role of extracellular albumin</title><author>Ludwig, Janet C. ; Hoppens, Carol L. ; McManus, Linda M. ; Mott, Glen E. ; Pinckard, R.Neal</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c452t-8efa06038ad426375bbd14a0d4c913232282edd9610137e87712b7e1e8396f1a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Applied sciences</topic><topic>Calcium - pharmacology</topic><topic>Dose-Response Relationship, Drug</topic><topic>Exact sciences and technology</topic><topic>Humans</topic><topic>In Vitro Techniques</topic><topic>Kinetics</topic><topic>N-Formylmethionine Leucyl-Phenylalanine - pharmacology</topic><topic>Neutrophils - metabolism</topic><topic>Other techniques and industries</topic><topic>Platelet Activating Factor - biosynthesis</topic><topic>Platelet Activating Factor - isolation & purification</topic><topic>Serum Albumin - pharmacology</topic><topic>Tritium</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ludwig, Janet C.</creatorcontrib><creatorcontrib>Hoppens, Carol L.</creatorcontrib><creatorcontrib>McManus, Linda M.</creatorcontrib><creatorcontrib>Mott, Glen E.</creatorcontrib><creatorcontrib>Pinckard, R.Neal</creatorcontrib><collection>Pascal-Francis</collection><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>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ludwig, Janet C.</au><au>Hoppens, Carol L.</au><au>McManus, Linda M.</au><au>Mott, Glen E.</au><au>Pinckard, R.Neal</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Modulation of platelet-activating factor (PAF) synthesis and release from human polymorphonuclear leukocytes (PMN): Role of extracellular albumin</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1985-09</date><risdate>1985</risdate><volume>241</volume><issue>2</issue><spage>337</spage><epage>347</epage><pages>337-347</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><coden>ABBIA4</coden><abstract>Human neutrophilic polymorphonuclear leukocytes (PMN) stimulated with
N′-formyl-methionyl-leucyl-phenylalanine (FMLP) in the presence of cytochalasin B but in the absence of human serum albumin (HSA) synthesized only small amounts of platelet-activating factor (PAF) that attained maximum levels within 60–120 s after stimulation; in addition, no release of PAF occurred. However, in the presence of 2.5 mg HSA/ml, there was a threefold increase in PAF synthesis, 30–40% of which was released within 5 min after FMLP stimulation. In the presence of 50 mg HSA/ml there was at least a fourfold increase in PAF synthesis and release, with maximal synthesis occurring 10–20 min after stimulation. Thus, the presence of HSA during PMN stimulation not only induced an albumin dose-dependent increase in PAF release but significantly augmented the synthesis of PAF. In contrast to PAF synthesis and release, the presence or absence of HSA had no effect upon lysosomal enzyme secretion from FMLP-stimulated PMN, which was maximal within 30–60 s after stimulation. These results demonstrate that HSA plays an essential role
in vitro in the synthesis and release of PAF from human PMN, and support the hypothesis that there is a cyclic PAF synthesis-release coupling mechanism in the stimulated human PMN.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>4037794</pmid><doi>10.1016/0003-9861(85)90555-7</doi><tpages>11</tpages></addata></record> |
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subjects | Applied sciences Calcium - pharmacology Dose-Response Relationship, Drug Exact sciences and technology Humans In Vitro Techniques Kinetics N-Formylmethionine Leucyl-Phenylalanine - pharmacology Neutrophils - metabolism Other techniques and industries Platelet Activating Factor - biosynthesis Platelet Activating Factor - isolation & purification Serum Albumin - pharmacology Tritium |
title | Modulation of platelet-activating factor (PAF) synthesis and release from human polymorphonuclear leukocytes (PMN): Role of extracellular albumin |
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