Differential expression of prostaglandin (PG) synthesis enzymes in conceptus during peri-implantation period and endometrial expression of carbonyl reductase/PG 9-ketoreductase in the pig.
Prostaglandins (PGs) play a pivotal role in luteolysis, maternal recognition of pregnancy, and implantation. In many species, including pigs, both conceptus (embryo and associated membranes) and endometrium synthesize PGE(2), which may antagonize PGF(2alpha) by playing a luteotropic/antiluteolytic role. Previously, we have reported expression profiles of PG G/H synthases (PGHS-1 and PGHS-2), PGE synthase (mPGES-1), and PGF synthase (PGFS) in the endometrium of cyclic and pregnant pigs. In the present study, expression of above-mentioned PG synthesis enzymes and PG 9-ketoreductase (CBR1), which converts PGE(2) into PGF(2alpha), and the PGE(2)/PGF(2alpha) ratios were investigated in porcine peri- and post-implantation conceptuses. Furthermore, expression of CBR1 was examined in the endometrium. PGHS-2 and mPGES-1 were upregulated, and PGHS-1, PGFS, and CBR1 were downregulated in conceptuses during trophoblastic elongation. A second increase of mPGES-1 mRNA occurred after days 20-21 of pregnancy. After initiation of implantation, expression of PGHS-1, PGFS, and CBR1 in conceptuses increased and remained higher until days 24-25 of pregnancy. Comparison of the endometrial CBR1 protein expression in cyclic and pregnant gilts revealed upregulation on days 16-17 of the cycle and downregulation on days 10-11 of pregnancy. In conclusion, reciprocal expression of PGHS-2, mPGES-1, PGFS, and CBR1 in day 10-13 conceptuses and decrease of endometrial CBR1 may be important in increasing the PGE(2)/PGF(2alpha) ratio during maternal recognition of pregnancy. This study indicates that PGE(2) produced via PGHS-2 and mPGES-1 in conceptus may be involved in corpus luteum control. Moreover, high expression of conceptus PGHS-1, mPGES-1, PGFS, and CBR1 after initiation of implantation suggests their significant role in placentation.
Waclawik
Agnieszka
A
Institute of Animal Reproduction and Food Research of Polish Academy of Sciences, Tuwima 10, 10-747 Olsztyn, Poland.
Ziecik
Adam J
AJ
D000429:Alcohol Oxidoreductases / Q000032:analysis* / Q000235:genetics; D000449:Aldehyde Reductase; D000074408:Aldo-Keto Reductases; D000818:Animals; D015153:Blotting, Western / Q000379:methods; D015237:Dinoprost / Q000031:analogs & derivatives / Q000032:analysis; D015232:Dinoprostone / Q000032:analysis; D010064:Embryo Implantation / Q000502:physiology; D004628:Embryonic Structures / Q000737:chemistry; D004717:Endometrium / Q000737:chemistry / Q000201:enzymology*; D030762:Estrous Cycle; D005260:Female; D005865:Gestational Age; D006911:Hydroxyprostaglandin Dehydrogenases / Q000032:analysis* / Q000235:genetics; D019746:Intramolecular Oxidoreductases / Q000032:analysis* / Q000235:genetics; D011247:Pregnancy; D011270:Pregnancy, Animal / Q000378:metabolism*; D000071876:Prostaglandin-E Synthases; D011451:Prostaglandin-Endoperoxide Synthases / Q000032:analysis* / Q000235:genetics; D012333:RNA, Messenger / Q000032:analysis; D020133:Reverse Transcriptase Polymerase Chain Reaction; D013552:Swine / Q000378:metabolism
D012333:RNA, Messenger; C008228:15-keto-13,14-dihydroprostaglandin F2alpha; D015237:Dinoprost; D000429:Alcohol Oxidoreductases; D000074408:Aldo-Keto Reductases; D006911:Hydroxyprostaglandin Dehydrogenases; C031051:prostaglandin-F synthase; D000449:Aldehyde Reductase; D011451:Prostaglandin-Endoperoxide Synthases; D019746:Intramolecular Oxidoreductases; D000071876:Prostaglandin-E Synthases; D015232:Dinoprostone