title: Differential expression of type II, IV and cytosolic PLA2 messenger RNA in human intrauterine tissues at term.
abstract: The involvement of phospholipase A2 (PLA2) enzymes in the formation of biologically-active phospholipid metabolites by human gestational tissues has principally been characterized by the use of enzyme activity assays. While such assays have established the presence of functional PLA2 activity, there is a paucity of information concerning the tissue distribution and relative contribution to net activity made by specific PLA2 isozymes. In particular, both secretory and cytosolic isozymes may be involved in gestational tissue phospholipid metabolism. Thus, the aim of this study was to test the hypothesis that phospholipase A2 mRNA transcripts encoding Type II, Type IV and cytosolic PLA2 are tissue-specifically expressed in human amnion, choriodecidua and placenta obtained at term. The relative expression of polyA+ mRNA encoding these PLA2 isozymes was determined by Northern blot analysis and laser densitometry. The data obtained confirm the tissue-specific expression of PLA2 mRNA in human intrauterine tissues. Cytosolic PLA2 mRNA was most abundantly expressed in amnion when compared to either choriodecidua (which was 5-fold less than amnion; P < 0.001) or placenta (72-fold less than amnion; P < 0.001). In contrast, the secretory PLA2 mRNA transcripts (i.e. Type II and Type IV) were most abundantly expressed in placenta. Type II PLA2 mRNA expression in choriodecidua and amnion was 30-fold less than that observed in placenta (both P < 0.001). Type IV PLA2 mRNA expression was 37-fold (P < 0.001) and 73-fold (P < 0.001) less in choriodecidua and amnion respectively. These data support the conclusion that cytosolic PLA2 is the principal PLA2 isozyme mediating phospholipid metabolism and the liberation of fatty acid substrate (i.e. arachidonic acid) in term amnion, while secretory PLA2 isozymes, and in particular, Type II PLA2 play a major role in phospholipid metabolism in term placenta.
authors.affiliation: Department of Perinatal Medicine, Royal Women's Hospital, Carlton, Victoria, Australia.
authors.forename: K A
authors.initials: KA
authors.lastname: Freed
authors.forename: E K
authors.initials: EK
authors.lastname: Moses
authors.forename: S P
authors.initials: SP
authors.lastname: Brennecke
authors.forename: G E
authors.initials: GE
authors.lastname: Rice
mesh_terms: D000650:Amnion / Q000378:metabolism; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern / Q000379:methods / Q000592:standards; D002823:Chorion / Q000378:metabolism; D003600:Cytosol / Q000378:metabolism; D015342:DNA Probes / Q000235:genetics; D003656:Decidua / Q000378:metabolism; D005260:Female; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000235:genetics; D006801:Humans; D007527:Isoenzymes / Q000235:genetics*; D010741:Phospholipases A / Q000235:genetics*; D054467:Phospholipases A2; D010920:Placenta / Q000378:metabolism; D011247:Pregnancy / Q000235:genetics* / Q000378:metabolism*; D012333:RNA, Messenger / Q000235:genetics* / Q000378:metabolism*; D012337:RNA, Ribosomal, 18S / Q000235:genetics; D051381:Rats; D014018:Tissue Distribution; D014599:Uterus / Q000378:metabolism*
chemical_list: D015342:DNA Probes; D007527:Isoenzymes; D012333:RNA, Messenger; D012337:RNA, Ribosomal, 18S; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D010741:Phospholipases A; D054467:Phospholipases A2