Release of Lysosomal Phospholipase A1 and A2 into Cytosol and Rapid Turnover of Newly-Formed Lysophosphatidylcholine in FL Cells during Fusion-from-within Induced by Measles Virus
Identifieur interne : 001510 ( Istex/Corpus ); précédent : 001509; suivant : 001511Release of Lysosomal Phospholipase A1 and A2 into Cytosol and Rapid Turnover of Newly-Formed Lysophosphatidylcholine in FL Cells during Fusion-from-within Induced by Measles Virus
Auteurs : Yasuo Suzuki ; Makoto MatsumotoSource :
- The Journal of Biochemistry [ 0021-924X ] ; 1982-10.
Abstract
The subcellular distribution of the phospholipase activities and metabolism of lysophosphatidylcholine in cultured human cell line (FL cells) during “fusion-from-within” induced by measles virus were studied. During cell fusion, fairly high activities of phospholipase A1 and A2, the optimal pHs of which were acidic, appeared in the cytosol. These phospholipases were confirmed to be of lysosomal origin by the following facts: (1) the properties of these phospholipases were the same as those of lysosomal phospholipase A1 and A2; (2) a decrease in the total activity of phospholipases A1, A2 and acid phosphatase in the lysosomal fraction of the infected cells coincided with an increase in their activity in the cytosol. The release of lysosomal phospholipase A1 and A2, into the cytosol of the infected cells appeared to be related to the extent of cell fusion-from-within. Phospholipase A1 and A2 released to the cytosol hydrolyzed the cell membrane-bound phospholipids to form lysophospholipids. 1-[1–14C]Palmitoyl-GPC, incorporated into the cells from the culture medium, was rapidly converted into phosphatidylcholine, triacylglycerol and phosphatidylethanolamine in the cells during fusion-from-within, but the radioactive lysophosphatidylcholine and fatty acids were hardly detectable, indicating a rapid turnover of cellular lysophosphatidylcholine during cell fusion. The subcellular lysophospholipid acyl-hydrolase activities of the infected cells were higher than those of normal cells. Possible relation between the membrane fusion induced by measles virus and the phospholipid metabolism in the infected cells were discussed.
Url:
DOI: 10.1093/oxfordjournals.jbchem.a134098
Links to Exploration step
ISTEX:A85F4FBD23343F5495405726CFB73E3EF2B022FALe document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>Release of Lysosomal Phospholipase A1 and A2 into Cytosol and Rapid Turnover of Newly-Formed Lysophosphatidylcholine in FL Cells during Fusion-from-within Induced by Measles Virus</title><author><name sortKey="Suzuki, Yasuo" sort="Suzuki, Yasuo" uniqKey="Suzuki Y" first="Yasuo" last="Suzuki">Yasuo Suzuki</name><affiliation><mods:affiliation>Department of Biochemistry, Shizuoka College of Pharmacy, Shizuoka, Shizuoka 422</mods:affiliation></affiliation></author><author><name sortKey="Matsumoto, Makoto" sort="Matsumoto, Makoto" uniqKey="Matsumoto M" first="Makoto" last="Matsumoto">Makoto Matsumoto</name><affiliation><mods:affiliation>Department of Biochemistry, Shizuoka College of Pharmacy, Shizuoka, Shizuoka 422</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:A85F4FBD23343F5495405726CFB73E3EF2B022FA</idno><date when="1982" year="1982">1982</date><idno type="doi">10.1093/oxfordjournals.jbchem.a134098</idno><idno type="url">https://api.istex.fr/document/A85F4FBD23343F5495405726CFB73E3EF2B022FA/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">001510</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Release of Lysosomal Phospholipase A1 and A2 into Cytosol and Rapid Turnover of Newly-Formed Lysophosphatidylcholine in FL Cells during Fusion-from-within Induced by Measles Virus</title><author><name sortKey="Suzuki, Yasuo" sort="Suzuki, Yasuo" uniqKey="Suzuki Y" first="Yasuo" last="Suzuki">Yasuo Suzuki</name><affiliation><mods:affiliation>Department of Biochemistry, Shizuoka College of Pharmacy, Shizuoka, Shizuoka 422</mods:affiliation></affiliation></author><author><name sortKey="Matsumoto, Makoto" sort="Matsumoto, Makoto" uniqKey="Matsumoto M" first="Makoto" last="Matsumoto">Makoto Matsumoto</name><affiliation><mods:affiliation>Department of Biochemistry, Shizuoka College of Pharmacy, Shizuoka, Shizuoka 422</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">The Journal of Biochemistry</title><idno type="ISSN">0021-924X</idno><idno type="eISSN">-</idno><imprint><publisher>Oxford University Press</publisher><date type="published" when="1982-10">1982-10</date><biblScope unit="volume">92</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="1683">1683</biblScope><biblScope unit="page" to="1692">1692</biblScope></imprint><idno type="ISSN">0021-924X</idno></series><idno type="istex">A85F4FBD23343F5495405726CFB73E3EF2B022FA</idno><idno type="DOI">10.1093/oxfordjournals.jbchem.a134098</idno><idno type="ArticleID">92.6.1683</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0021-924X</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract">The subcellular distribution of the phospholipase activities and metabolism of lysophosphatidylcholine in cultured human cell line (FL cells) during “fusion-from-within” induced by measles virus were studied. During cell fusion, fairly high activities of phospholipase A1 and A2, the optimal pHs of which were acidic, appeared in the cytosol. These phospholipases were confirmed to be of lysosomal origin by the following facts: (1) the properties of these phospholipases were the same as those of lysosomal phospholipase A1 and A2; (2) a decrease in the total activity of phospholipases A1, A2 and acid phosphatase in the lysosomal fraction of the infected cells coincided with an increase in their activity in the cytosol. The release of lysosomal phospholipase A1 and A2, into the cytosol of the infected cells appeared to be related to the extent of cell fusion-from-within. Phospholipase A1 and A2 released to the cytosol hydrolyzed the cell membrane-bound phospholipids to form lysophospholipids. 1-[1–14C]Palmitoyl-GPC, incorporated into the cells from the culture medium, was rapidly converted into phosphatidylcholine, triacylglycerol and phosphatidylethanolamine in the cells during fusion-from-within, but the radioactive lysophosphatidylcholine and fatty acids were hardly detectable, indicating a rapid turnover of cellular lysophosphatidylcholine during cell fusion. The subcellular lysophospholipid acyl-hydrolase activities of the infected cells were higher than those of normal cells. Possible relation between the membrane fusion induced by measles virus and the phospholipid metabolism in the infected cells were discussed.</div></front></TEI><istex><corpusName>oup</corpusName><author><json:item><name>Yasuo SUZUKI</name><affiliations><json:string>Department of Biochemistry, Shizuoka College of Pharmacy, Shizuoka, Shizuoka 422</json:string></affiliations></json:item><json:item><name>Makoto MATSUMOTO</name><affiliations><json:string>Department of Biochemistry, Shizuoka College of Pharmacy, Shizuoka, Shizuoka 422</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Articles</value></json:item></subject><articleId><json:string>92.6.1683</json:string></articleId><language><json:string>eng</json:string></language><abstract>The subcellular distribution of the phospholipase activities and metabolism of lysophosphatidylcholine in cultured human cell line (FL cells) during “fusion-from-within” induced by measles virus were studied. During cell fusion, fairly high activities of phospholipase A1 and A2, the optimal pHs of which were acidic, appeared in the cytosol. These phospholipases were confirmed to be of lysosomal origin by the following facts: (1) the properties of these phospholipases were the same as those of lysosomal phospholipase A1 and A2; (2) a decrease in the total activity of phospholipases A1, A2 and acid phosphatase in the lysosomal fraction of the infected cells coincided with an increase in their activity in the cytosol. The release of lysosomal phospholipase A1 and A2, into the cytosol of the infected cells appeared to be related to the extent of cell fusion-from-within. Phospholipase A1 and A2 released to the cytosol hydrolyzed the cell membrane-bound phospholipids to form lysophospholipids. 1-[1–14C]Palmitoyl-GPC, incorporated into the cells from the culture medium, was rapidly converted into phosphatidylcholine, triacylglycerol and phosphatidylethanolamine in the cells during fusion-from-within, but the radioactive lysophosphatidylcholine and fatty acids were hardly detectable, indicating a rapid turnover of cellular lysophosphatidylcholine during cell fusion. The subcellular lysophospholipid acyl-hydrolase activities of the infected cells were higher than those of normal cells. Possible relation between the membrane fusion induced by measles virus and the phospholipid metabolism in the infected cells were discussed.</abstract><qualityIndicators><score>7.446</score><pdfVersion>1.2</pdfVersion><pdfPageSize>489 x 724 pts</pdfPageSize><refBibsNative>false</refBibsNative><keywordCount>1</keywordCount><abstractCharCount>1642</abstractCharCount><pdfWordCount>4698</pdfWordCount><pdfCharCount>30380</pdfCharCount><pdfPageCount>10</pdfPageCount><abstractWordCount>229</abstractWordCount></qualityIndicators><title>Release of Lysosomal Phospholipase A1 and A2 into Cytosol and Rapid Turnover of Newly-Formed Lysophosphatidylcholine in FL Cells during Fusion-from-within Induced by Measles Virus</title><genre.original><json:string>research-article</json:string></genre.original><genre><json:string>research-article</json:string></genre><host><volume>92</volume><publisherId><json:string>jbchem</json:string></publisherId><pages><last>1692</last><first>1683</first></pages><issn><json:string>0021-924X</json:string></issn><issue>6</issue><genre><json:string>Journal</json:string></genre><language><json:string>unknown</json:string></language><eissn><json:string>-</json:string></eissn><title>The Journal of Biochemistry</title></host><categories><wos><json:string>BIOCHEMISTRY & MOLECULAR BIOLOGY</json:string></wos></categories><publicationDate>1982</publicationDate><copyrightDate>1982</copyrightDate><doi><json:string>10.1093/oxfordjournals.jbchem.a134098</json:string></doi><id>A85F4FBD23343F5495405726CFB73E3EF2B022FA</id><fulltext><json:item><original>true</original><mimetype>application/pdf</mimetype><extension>pdf</extension><uri>https://api.istex.fr/document/A85F4FBD23343F5495405726CFB73E3EF2B022FA/fulltext/pdf</uri></json:item><json:item><original>false</original><mimetype>application/zip</mimetype><extension>zip</extension><uri>https://api.istex.fr/document/A85F4FBD23343F5495405726CFB73E3EF2B022FA/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/A85F4FBD23343F5495405726CFB73E3EF2B022FA/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a">Release of Lysosomal Phospholipase A1 and A2 into Cytosol and Rapid Turnover of Newly-Formed Lysophosphatidylcholine in FL Cells during Fusion-from-within Induced by Measles Virus</title><respStmt xml:id="ISTEX-API" resp="Références bibliographiques récupérées via GROBID" name="ISTEX-API (INIST-CNRS)"></respStmt><respStmt xml:id="ISTEX-API" resp="Références bibliographiques récupérées via GROBID" name="ISTEX-API (INIST-CNRS)"></respStmt></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>Oxford University Press</publisher><availability><p>OUP</p></availability><date>1982</date></publicationStmt><notesStmt><note>1This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.</note><note>2To whom correspondence should be addressed.</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a">Release of Lysosomal Phospholipase A1 and A2 into Cytosol and Rapid Turnover of Newly-Formed Lysophosphatidylcholine in FL Cells during Fusion-from-within Induced by Measles Virus</title><author><persName><forename type="first">Yasuo</forename><surname>SUZUKI</surname></persName><affiliation>Department of Biochemistry, Shizuoka College of Pharmacy, Shizuoka, Shizuoka 422</affiliation></author><author><persName><forename type="first">Makoto</forename><surname>MATSUMOTO</surname></persName><affiliation>Department of Biochemistry, Shizuoka College of Pharmacy, Shizuoka, Shizuoka 422</affiliation></author></analytic><monogr><title level="j">The Journal of Biochemistry</title><idno type="pISSN">0021-924X</idno><idno type="eISSN">-</idno><imprint><publisher>Oxford University Press</publisher><date type="published" when="1982-10"></date><biblScope unit="volume">92</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="1683">1683</biblScope><biblScope unit="page" to="1692">1692</biblScope></imprint></monogr><idno type="istex">A85F4FBD23343F5495405726CFB73E3EF2B022FA</idno><idno type="DOI">10.1093/oxfordjournals.jbchem.a134098</idno><idno type="ArticleID">92.6.1683</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1982</date></creation><langUsage><language ident="en">en</language></langUsage><abstract><p>The subcellular distribution of the phospholipase activities and metabolism of lysophosphatidylcholine in cultured human cell line (FL cells) during “fusion-from-within” induced by measles virus were studied. During cell fusion, fairly high activities of phospholipase A1 and A2, the optimal pHs of which were acidic, appeared in the cytosol. These phospholipases were confirmed to be of lysosomal origin by the following facts: (1) the properties of these phospholipases were the same as those of lysosomal phospholipase A1 and A2; (2) a decrease in the total activity of phospholipases A1, A2 and acid phosphatase in the lysosomal fraction of the infected cells coincided with an increase in their activity in the cytosol. The release of lysosomal phospholipase A1 and A2, into the cytosol of the infected cells appeared to be related to the extent of cell fusion-from-within. Phospholipase A1 and A2 released to the cytosol hydrolyzed the cell membrane-bound phospholipids to form lysophospholipids. 1-[1–14C]Palmitoyl-GPC, incorporated into the cells from the culture medium, was rapidly converted into phosphatidylcholine, triacylglycerol and phosphatidylethanolamine in the cells during fusion-from-within, but the radioactive lysophosphatidylcholine and fatty acids were hardly detectable, indicating a rapid turnover of cellular lysophosphatidylcholine during cell fusion. The subcellular lysophospholipid acyl-hydrolase activities of the infected cells were higher than those of normal cells. Possible relation between the membrane fusion induced by measles virus and the phospholipid metabolism in the infected cells were discussed.</p></abstract><textClass><keywords scheme="keyword"><list><item><term>Articles</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1982-10">Published</change><change xml:id="refBibs-istex" who="#ISTEX-API" when="2016-3-14">References added</change><change xml:id="refBibs-istex" who="#ISTEX-API" when="2016-3-22">References added</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><original>false</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/A85F4FBD23343F5495405726CFB73E3EF2B022FA/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="corpus oup" wicri:toSee="no header"><istex:docType PUBLIC="-//NLM//DTD Journal Publishing DTD v2.3 20070202//EN" URI="journalpublishing.dtd" name="istex:docType"></istex:docType><istex:document><article article-type="research-article"><front><journal-meta><journal-id journal-id-type="hwp">jbiochem</journal-id><journal-id journal-id-type="publisher-id">jbchem</journal-id><journal-id journal-id-type="pmc">jbiochem</journal-id><journal-title>The Journal of Biochemistry</journal-title><issn pub-type="epub">-</issn><issn pub-type="ppub">0021-924X</issn><publisher><publisher-name>Oxford University Press</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="publisher-id">92.6.1683</article-id><article-id pub-id-type="doi">10.1093/oxfordjournals.jbchem.a134098</article-id><article-categories><subj-group><subject>Articles</subject></subj-group></article-categories><title-group><article-title>Release of Lysosomal Phospholipase A<sub>1</sub> and A<sub>2</sub> into Cytosol and Rapid Turnover of Newly-Formed Lysophosphatidylcholine in FL Cells during Fusion-from-within Induced by Measles Virus<xref ref-type="fn" rid="fn1"><sup>1</sup></xref></article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>SUZUKI</surname><given-names>Yasuo</given-names></name></contrib><contrib contrib-type="author"><name><surname>MATSUMOTO</surname><given-names>Makoto</given-names></name><xref ref-type="corresp" rid="cor1"><sup>2</sup></xref></contrib><aff><institution>Department of Biochemistry, Shizuoka College of Pharmacy</institution> <addr-line>Shizuoka, Shizuoka 422</addr-line></aff></contrib-group><author-notes><corresp id="cor1"><sup>2</sup>To whom correspondence should be addressed.</corresp><fn id="fn1"><p><sup>1</sup>This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.</p></fn></author-notes><pub-date pub-type="ppub"><month>10</month><year>1982</year></pub-date><volume>92</volume><issue>6</issue><fpage>1683</fpage><lpage>1692</lpage><history><date date-type="received"><day>08</day><month>7</month><year>1982</year></date></history><copyright-statement>© 1982, by the Japanese Biochemical Society</copyright-statement><copyright-year>1982</copyright-year><abstract><p>The subcellular distribution of the phospholipase activities and metabolism of lysophosphatidylcholine in cultured human cell line (FL cells) during “fusion-from-within” induced by measles virus were studied.</p><p>During cell fusion, fairly high activities of phospholipase A<sub>1</sub> and A<sub>2</sub>, the optimal pHs of which were acidic, appeared in the cytosol. These phospholipases were confirmed to be of lysosomal origin by the following facts: (1) the properties of these phospholipases were the same as those of lysosomal phospholipase A<sub>1</sub> and A<sub>2</sub>; (2) a decrease in the total activity of phospholipases A<sub>1</sub>, A<sub>2</sub> and acid phosphatase in the lysosomal fraction of the infected cells coincided with an increase in their activity in the cytosol. The release of lysosomal phospholipase A<sub>1</sub> and A<sub>2</sub>, into the cytosol of the infected cells appeared to be related to the extent of cell fusion-from-within. Phospholipase A<sub>1</sub> and A<sub>2</sub> released to the cytosol hydrolyzed the cell membrane-bound phospholipids to form lysophospholipids.</p><p>1-[1–<sup>14</sup>C]Palmitoyl-GPC, incorporated into the cells from the culture medium, was rapidly converted into phosphatidylcholine, triacylglycerol and phosphatidylethanolamine in the cells during fusion-from-within, but the radioactive lysophosphatidylcholine and fatty acids were hardly detectable, indicating a rapid turnover of cellular lysophosphatidylcholine during cell fusion. The subcellular lysophospholipid acyl-hydrolase activities of the infected cells were higher than those of normal cells.</p><p>Possible relation between the membrane fusion induced by measles virus and the phospholipid metabolism in the infected cells were discussed.</p></abstract></article-meta></front></article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Release of Lysosomal Phospholipase A1 and A2 into Cytosol and Rapid Turnover of Newly-Formed Lysophosphatidylcholine in FL Cells during Fusion-from-within Induced by Measles Virus</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Release of Lysosomal Phospholipase A1 and A2 into Cytosol and Rapid Turnover of Newly-Formed Lysophosphatidylcholine in FL Cells during Fusion-from-within Induced by Measles Virus1</title></titleInfo><name type="personal"><namePart type="given">Yasuo</namePart><namePart type="family">SUZUKI</namePart><affiliation>Department of Biochemistry, Shizuoka College of Pharmacy, Shizuoka, Shizuoka 422</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Makoto</namePart><namePart type="family">MATSUMOTO</namePart><affiliation>Department of Biochemistry, Shizuoka College of Pharmacy, Shizuoka, Shizuoka 422</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="research-article"></genre><subject><topic>Articles</topic></subject><originInfo><publisher>Oxford University Press</publisher><dateIssued encoding="w3cdtf">1982-10</dateIssued><copyrightDate encoding="w3cdtf">1982</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract>The subcellular distribution of the phospholipase activities and metabolism of lysophosphatidylcholine in cultured human cell line (FL cells) during “fusion-from-within” induced by measles virus were studied. During cell fusion, fairly high activities of phospholipase A1 and A2, the optimal pHs of which were acidic, appeared in the cytosol. These phospholipases were confirmed to be of lysosomal origin by the following facts: (1) the properties of these phospholipases were the same as those of lysosomal phospholipase A1 and A2; (2) a decrease in the total activity of phospholipases A1, A2 and acid phosphatase in the lysosomal fraction of the infected cells coincided with an increase in their activity in the cytosol. The release of lysosomal phospholipase A1 and A2, into the cytosol of the infected cells appeared to be related to the extent of cell fusion-from-within. Phospholipase A1 and A2 released to the cytosol hydrolyzed the cell membrane-bound phospholipids to form lysophospholipids. 1-[1–14C]Palmitoyl-GPC, incorporated into the cells from the culture medium, was rapidly converted into phosphatidylcholine, triacylglycerol and phosphatidylethanolamine in the cells during fusion-from-within, but the radioactive lysophosphatidylcholine and fatty acids were hardly detectable, indicating a rapid turnover of cellular lysophosphatidylcholine during cell fusion. The subcellular lysophospholipid acyl-hydrolase activities of the infected cells were higher than those of normal cells. Possible relation between the membrane fusion induced by measles virus and the phospholipid metabolism in the infected cells were discussed.</abstract><note type="footnotes">1This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.</note><note type="author-notes">2To whom correspondence should be addressed.</note><relatedItem type="host"><titleInfo><title>The Journal of Biochemistry</title></titleInfo><genre type="Journal">journal</genre><identifier type="ISSN">0021-924X</identifier><identifier type="eISSN">-</identifier><identifier type="PublisherID">jbchem</identifier><identifier type="PublisherID-hwp">jbiochem</identifier><part><date>1982</date><detail type="volume"><caption>vol.</caption><number>92</number></detail><detail type="issue"><caption>no.</caption><number>6</number></detail><extent unit="pages"><start>1683</start><end>1692</end></extent></part></relatedItem><identifier type="istex">A85F4FBD23343F5495405726CFB73E3EF2B022FA</identifier><identifier type="DOI">10.1093/oxfordjournals.jbchem.a134098</identifier><identifier type="ArticleID">92.6.1683</identifier><accessCondition type="use and reproduction" contentType="copyright">© 1982, by the Japanese Biochemical Society</accessCondition><recordInfo><recordContentSource>OUP</recordContentSource></recordInfo></mods></metadata><annexes><json:item><original>true</original><mimetype>application/pdf</mimetype><extension>pdf</extension><uri>https://api.istex.fr/document/A85F4FBD23343F5495405726CFB73E3EF2B022FA/annexes/pdf</uri></json:item></annexes><enrichments><istex:catWosTEI uri="https://api.istex.fr/document/A85F4FBD23343F5495405726CFB73E3EF2B022FA/enrichments/catWos"><teiHeader><profileDesc><textClass><classCode scheme="WOS">BIOCHEMISTRY & MOLECULAR BIOLOGY</classCode></textClass></profileDesc></teiHeader></istex:catWosTEI></enrichments><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Informatique/explor/ScrumV1/Data/Istex/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001510 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Istex/Corpus/biblio.hfd -nk 001510 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Informatique
|area= ScrumV1
|flux= Istex
|étape= Corpus
|type= RBID
|clé= ISTEX:A85F4FBD23343F5495405726CFB73E3EF2B022FA
|texte= Release of Lysosomal Phospholipase A1 and A2 into Cytosol and Rapid Turnover of Newly-Formed Lysophosphatidylcholine in FL Cells during Fusion-from-within Induced by Measles Virus
}}
| This area was generated with Dilib version V0.6.39. |  |