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dc.contributor.authorFisher, Gary J.en_US
dc.contributor.authorHenderson, Patricia A.en_US
dc.contributor.authorVoorhees, John J.en_US
dc.contributor.authorBaldassare, Joseph J.en_US
dc.date.accessioned2007-04-06T18:04:08Z
dc.date.available2007-04-06T18:04:08Z
dc.date.issued1991-02en_US
dc.identifier.citationFisher, Gary J.; Henderson, Patricia A.; Voorhees, John J.; Baldassare, Joseph J. (1991)."Epidermal growth factor-induced hydrolysis of phosphatidylcholine by phospholipase D and phospholipase C in human dermal fibroblasts." Journal of Cellular Physiology 146(2): 309-317. <http://hdl.handle.net/2027.42/49879>en_US
dc.identifier.issn0021-9541en_US
dc.identifier.issn1097-4652en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/49879
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=1999479&dopt=citationen_US
dc.description.abstractThe enzymatic pathways for formation of 1,2-diradylglyceride in response to epidermal growth factor in human dermal fibroblasts have been investigated. 1,2-Diradylglyceride mass was elevated 2-fold within one minute of addition of EGF. Maximal accumulation (4-fold) occurred at 5 minutes. Since both diacyl and ether-linked diglyceride species occur naturally and may accumulate following agonist activation, we developed a novel method to determine separately the alterations in diacyl and ether-linked diglycerides following stimulation of fibroblasts with EGF. Utilizing this method, it was found that approximately 80% of the total cellular 1,2-diradylglyceride was diacyl, the remaining 20% being ether-linked. Addition of EGF caused accumulation of 1,2-diacylglyceride with out alteration in the level of ether-linked diglyceride. Thus, the observed induction of 1,2-diradylglyceride by EGF was due exclusively to increased formation of 1,2-diacylglyceride. In cells labelled with [ 3 H]choline, the water soluble phosphatidylcholine hydrolysis products, phosphorylcholine and choline, were increased 2-fold within 5 minutes of addition of EGF. No hydrolysis of phosphatidylethanolamine, phosphatidylserine, or phosphatidylinositol was observed. Quantitation by radiolabel and mass revealed equivalent elevations in phosphorylcholine and choline, suggesting stimulation of both phospholipase C and phospholipase D activities. To identify the presence of EGF-induced phospholipase D activity, cells were labelled with exogenous [ 3 H]1-0-hexadecyl, 2-acyl phosphatidylcholine and its conversion to phosphatidic acid in response to EGF determined. Radiolabelled phosphatidic acid was detectable in 15 seconds after addition of EGF and was maximal (3-fold) at 30 seconds. Consistent with the presence of EGF-induced phospholipase D activity, treatment of cells with EGF, in the presence of [ 14 C]ethanol, resulted in the rapid formation of [ 14 C]phosphatidylethanol, the product of phospholipase D-catalyzed transphosphatidylation. The formation of phosphatidylethanol, which competes for the formation of phosphatidic acid by phospholipase D, did not diminish the induction of 1,2-diglyceride by EGF. These data suggest that the phosphatidic acid formed by phospholipase D-catalyzed hydrolysis of phosphatidylcholine is not a major precursor of the observed increased 1,2-diglyceride. Thus, the induction of 1,2-diacylglycerol by EGF may occur primarily via phospholipase C-catalyzed hydrolysis of phosphatidylcholine.en_US
dc.format.extent1052060 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.publisherWiley Subscription Services, Inc., A Wiley Companyen_US
dc.subject.otherLife and Medical Sciencesen_US
dc.subject.otherCell & Developmental Biologyen_US
dc.titleEpidermal growth factor-induced hydrolysis of phosphatidylcholine by phospholipase D and phospholipase C in human dermal fibroblastsen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbsecondlevelKinesiology and Sportsen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Dermatology, University of Michigan Medical Center, Ann Arbor, Michigan ; Department of Dermatology, University of Michigan Medical Center, Ann Arbor, Michiganen_US
dc.contributor.affiliationumDepartment of Dermatology, University of Michigan Medical Center, Ann Arbor, Michiganen_US
dc.contributor.affiliationotherAmerican Red Cross, St. Louis, Missourien_US
dc.contributor.affiliationotherAmerican Red Cross, St. Louis, Missourien_US
dc.identifier.pmid1999479en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/49879/1/1041460216_ftp.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1002/jcp.1041460216en_US
dc.identifier.sourceJournal of Cellular Physiologyen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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