Differential induction of enzyme in soybean cell cultures by elicitor or osmotic stress.
Identifieur interne : 002D83 ( Main/Exploration ); précédent : 002D82; suivant : 002D84Differential induction of enzyme in soybean cell cultures by elicitor or osmotic stress.
Auteurs : G. Kochs [Allemagne] ; R. Welle ; H. GrisebachSource :
- Planta [ 0032-0935 ] ; 1987.
Abstract
Soybean cell cultures were challenged either by glucan elicitor from Phytophthora megasperma f.sp. glycinea or by osmotic stress (0.4 M glucose). Osmotic stress induced production of a microsomal NADPH-dependent flavone synthase (flavone synthase II) which catalyses conversion of (2S)-naringenin to apigenin. In one of our cell-lines this enzyme activity was not detected either in unchallenged cells or in cells treated with glucan elicitor. Inducibility of flavone synthase II by 0.4 M glucose was highest at the end of the linear growth phase. Changes in the activities of a number of other enzymes were determined after treatment of the cells with elicitor or 0.4 M glucose. The activities of phenylalanine ammonialyase, cinnamate 4-hydroxylase, chalcone synthase and dihydroxypterocarpan 6a-hydroxylase all increased with elicitor and with osmoticum, albeit to a different degree. The rise in enzyme activity occurred later with osmoticum than with elicitor. The prenyltransferase involved in glyceollin synthesis was induced strongly by elicitor but only very weakly by osmoticum, whereas isoflavone synthase and NADPH: cytochrome-c reductase were only induced by elicitor. The activity of glucose-6-phosphate dehydrogenase did not change with elicitor or with osmoticum. Different product patterns were also obtained: whereas with elicitor, glyceollin I was the major product, intermediates of the glyceollin pathway (7,4'-dihydroxyflavanone, trihydroxypterocarpan) accumulated with osmoticum.
DOI: 10.1007/BF00392301
PubMed: 24225715
Affiliations:
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Kochs</name><affiliation wicri:level="3"><nlm:affiliation>Lehrstuhl für Biochemie der Pflanzen, Institut für Biologie II, Schänzlestrasse 1, D-7800, Freiburg, Federal Republic of Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Lehrstuhl für Biochemie der Pflanzen, Institut für Biologie II, Schänzlestrasse 1, D-7800, Freiburg</wicri:regionArea><placeName><region type="land" nuts="1">Bade-Wurtemberg</region><region type="district" nuts="2">District de Fribourg-en-Brisgau</region><settlement type="city">Fribourg-en-Brisgau</settlement></placeName></affiliation></author><author><name sortKey="Welle, R" sort="Welle, R" uniqKey="Welle R" first="R" last="Welle">R. Welle</name></author><author><name sortKey="Grisebach, H" sort="Grisebach, H" uniqKey="Grisebach H" first="H" last="Grisebach">H. Grisebach</name></author></analytic><series><title level="j">Planta</title><idno type="ISSN">0032-0935</idno><imprint><date when="1987" type="published">1987</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Soybean cell cultures were challenged either by glucan elicitor from Phytophthora megasperma f.sp. glycinea or by osmotic stress (0.4 M glucose). Osmotic stress induced production of a microsomal NADPH-dependent flavone synthase (flavone synthase II) which catalyses conversion of (2S)-naringenin to apigenin. In one of our cell-lines this enzyme activity was not detected either in unchallenged cells or in cells treated with glucan elicitor. Inducibility of flavone synthase II by 0.4 M glucose was highest at the end of the linear growth phase. Changes in the activities of a number of other enzymes were determined after treatment of the cells with elicitor or 0.4 M glucose. The activities of phenylalanine ammonialyase, cinnamate 4-hydroxylase, chalcone synthase and dihydroxypterocarpan 6a-hydroxylase all increased with elicitor and with osmoticum, albeit to a different degree. The rise in enzyme activity occurred later with osmoticum than with elicitor. The prenyltransferase involved in glyceollin synthesis was induced strongly by elicitor but only very weakly by osmoticum, whereas isoflavone synthase and NADPH: cytochrome-c reductase were only induced by elicitor. The activity of glucose-6-phosphate dehydrogenase did not change with elicitor or with osmoticum. Different product patterns were also obtained: whereas with elicitor, glyceollin I was the major product, intermediates of the glyceollin pathway (7,4'-dihydroxyflavanone, trihydroxypterocarpan) accumulated with osmoticum. </div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">24225715</PMID><DateCompleted><Year>2013</Year><Month>11</Month><Day>15</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0032-0935</ISSN><JournalIssue CitedMedium="Print"><Volume>171</Volume><Issue>4</Issue><PubDate><Year>1987</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Planta</Title><ISOAbbreviation>Planta</ISOAbbreviation></Journal><ArticleTitle>Differential induction of enzyme in soybean cell cultures by elicitor or osmotic stress.</ArticleTitle><Pagination><MedlinePgn>519-24</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/BF00392301</ELocationID><Abstract><AbstractText>Soybean cell cultures were challenged either by glucan elicitor from Phytophthora megasperma f.sp. glycinea or by osmotic stress (0.4 M glucose). Osmotic stress induced production of a microsomal NADPH-dependent flavone synthase (flavone synthase II) which catalyses conversion of (2S)-naringenin to apigenin. In one of our cell-lines this enzyme activity was not detected either in unchallenged cells or in cells treated with glucan elicitor. Inducibility of flavone synthase II by 0.4 M glucose was highest at the end of the linear growth phase. Changes in the activities of a number of other enzymes were determined after treatment of the cells with elicitor or 0.4 M glucose. The activities of phenylalanine ammonialyase, cinnamate 4-hydroxylase, chalcone synthase and dihydroxypterocarpan 6a-hydroxylase all increased with elicitor and with osmoticum, albeit to a different degree. The rise in enzyme activity occurred later with osmoticum than with elicitor. The prenyltransferase involved in glyceollin synthesis was induced strongly by elicitor but only very weakly by osmoticum, whereas isoflavone synthase and NADPH: cytochrome-c reductase were only induced by elicitor. The activity of glucose-6-phosphate dehydrogenase did not change with elicitor or with osmoticum. Different product patterns were also obtained: whereas with elicitor, glyceollin I was the major product, intermediates of the glyceollin pathway (7,4'-dihydroxyflavanone, trihydroxypterocarpan) accumulated with osmoticum. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kochs</LastName><ForeName>G</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Lehrstuhl für Biochemie der Pflanzen, Institut für Biologie II, Schänzlestrasse 1, D-7800, Freiburg, Federal Republic of Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Welle</LastName><ForeName>R</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Grisebach</LastName><ForeName>H</ForeName><Initials>H</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Planta</MedlineTA><NlmUniqueID>1250576</NlmUniqueID><ISSNLinking>0032-0935</ISSNLinking></MedlineJournalInfo></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>1986</Year><Month>11</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>1987</Year><Month>04</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>11</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>1987</Year><Month>8</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1987</Year><Month>8</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24225715</ArticleId><ArticleId IdType="doi">10.1007/BF00392301</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Eur J Biochem. 1986 Mar 3;155(2):311-8</Citation><ArticleIdList><ArticleId IdType="pubmed">3956488</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1976 May;57(5):760-5</Citation><ArticleIdList><ArticleId IdType="pubmed">16659566</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Biochem. 1976 Jan;70(1):241-50</Citation><ArticleIdList><ArticleId IdType="pubmed">1259145</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Biochem Biophys. 1984 Jul;232(1):240-8</Citation><ArticleIdList><ArticleId IdType="pubmed">6540068</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1972 Aug 25;247(16):5123-31</Citation><ArticleIdList><ArticleId IdType="pubmed">5057461</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Cell Rep. 1982 Apr;1(3):123-7</Citation><ArticleIdList><ArticleId IdType="pubmed">24259025</ArticleId></ArticleIdList></Reference><Reference><Citation>Methods Enzymol. 1985;110:130-44</Citation><ArticleIdList><ArticleId IdType="pubmed">2991702</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1965 Sep;40(5):779-84</Citation><ArticleIdList><ArticleId IdType="pubmed">16656157</ArticleId></ArticleIdList></Reference><Reference><Citation>J Cell Biol. 1967 Feb;32(2):415-38</Citation><ArticleIdList><ArticleId IdType="pubmed">10976232</ArticleId></ArticleIdList></Reference><Reference><Citation>Eur J Biochem. 1984 Jul 2;142(1):127-31</Citation><ArticleIdList><ArticleId IdType="pubmed">6540173</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country><region><li>Bade-Wurtemberg</li><li>District de Fribourg-en-Brisgau</li></region><settlement><li>Fribourg-en-Brisgau</li></settlement></list><tree><noCountry><name sortKey="Grisebach, H" sort="Grisebach, H" uniqKey="Grisebach H" first="H" last="Grisebach">H. Grisebach</name><name sortKey="Welle, R" sort="Welle, R" uniqKey="Welle R" first="R" last="Welle">R. Welle</name></noCountry><country name="Allemagne"><region name="Bade-Wurtemberg"><name sortKey="Kochs, G" sort="Kochs, G" uniqKey="Kochs G" first="G" last="Kochs">G. Kochs</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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