| Selective deacylation of arachidonate-containing ethanolamine-linked phosphoglycerides in stimulated human neutrophils. | |
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MedLine Citation:
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PMID: 2250009 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The involvement of the ethanolamine-linked phosphoglyceride fraction (PE) in neutrophil signal transduction is suggested by the stimulus-induced release of arachidonic acid from PE (Chilton, F. H., and Connell, T. R. (1988) J. Biol. Chem. 263, 5260-5265) and by the synthesis of acetylated PE species, predominantly 1-O-alk-1'-enyl-2-acetyl-sn-glycero-3-phosphoethanolamine (alkenylacetyl-GPE; Tessner, T. G., and Wykle, R. L. (1987) J. Biol. Chem. 262, 12660-12664) in stimulated cells. In the studies reported here, we investigated the relationship between arachidonic acid release from PE and generation of the lysophospholipid precursor required in the biosynthesis of alkenylacetyl-GPE. In order to follow these reactions, we prelabeled neutrophils with 1-O-[3H]alk-1'-enyl-2-arachidonoyl-sn-glycero-3-phosphoethanolamine (alkenyl-acyl-GPE). We also followed the hydrolysis of endogenous PE by analysis as the dinitrophenyl derivative using a high pressure liquid chromatography method we developed. Our results coupled with those of Chilton et al. (Chilton, F. H., Ellis, J. M., Olson, S. C., and Wykle, R. L. (1984) J. Biol. Chem. 259, 12014-12019) indicate that in human neutrophils the metabolism of alkenylacyl-GPE and alkylacyl-sn-glycero-3-phosphocholine (GPC) are strikingly similar with regard to arachidonate metabolism. When added to neutrophils, both 1-O-[3H]alkenyl-2-lyso-GPE and 1-O-[3H]alkyl-2-lyso-GPC are acylated predominantly with arachidonic acid, and the resulting arachidonoyl-containing phospholipids are extensively deacylated upon stimulation. However, hydrolysis of PE in the neutrophil differs from hydrolysis of choline-containing phosphoglycerides in that stimulation leads to a greater accumulation of the ethanolamine-linked lysophospholipid. A comparison of the molecular species of endogenous PE (based on molar concentrations measured as the dinitrophenyl derivative) from resting and stimulated neutrophils indicated that only those species which contain arachidonate are significantly hydrolyzed. |
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Authors:
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T G Tessner; D G Greene; R L Wykle |
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Publication Detail:
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Type: In Vitro; Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 265 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 1990 Dec |
Date Detail:
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Created Date: 1991-01-17 Completed Date: 1991-01-17 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 21032-8 Citation Subset: IM |
Affiliation:
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Department of Biochemistry, Wake Forest University Medical Center, Winston-Salem, North Carolina 27103. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Arachidonic Acids
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blood* Calcimycin / pharmacology Chromatography, High Pressure Liquid Humans Kinetics Neutrophils / drug effects, physiology* Phospholipids / blood*, isolation & purification Plasmalogens / blood* Signal Transduction Time Factors Tritium |
| Grant Support | |
ID/Acronym/Agency:
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AI-17287/AI/NIAID NIH HHS; CA43297/CA/NCI NIH HHS; HL-26818/HL/NHLBI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Arachidonic Acids; 0/Phospholipids; 0/Plasmalogens; 0/phosphatidal ethanolamines; 10028-17-8/Tritium; 52665-69-7/Calcimycin |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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