PPARδ functions as a prostacyclin receptor in blastocyst implantation

Trends in Endocrinology and Metabolism

Volumn 11, Issue 4, 2000, Pages 137-142

  Lim, Hyunjung ^a   Dey, Sudhansu K ^b  

^a BRIGHAM AND WOMEN S HOSPITAL   (United States)

^b UNIVERSITY OF KANSAS MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOOXYGENASE 1; CYCLOOXYGENASE 2; ESTROGEN; HEPARIN BINDING EPIDERMAL GROWTH FACTOR; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR; PROGESTERONE; PROSTACYCLIN RECEPTOR; PROSTAGLANDIN;

DECIDUALIZATION; ENDOMETRIUM; HORMONAL REGULATION; NIDATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; RECEPTOR INTRINSIC ACTIVITY; REVIEW;

ANIMALS; BLASTOCYST; EMBRYO IMPLANTATION; PROSTAGLANDINS; RECEPTORS, CELL SURFACE; RECEPTORS, CYTOPLASMIC AND NUCLEAR; RECEPTORS, EPOPROSTENOL; RECEPTORS, PROSTAGLANDIN; SIGNAL TRANSDUCTION; TRANSCRIPTION FACTORS;

EID: 0034094324     PISSN: 10432760     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1043-2760(00)00243-5     Document Type: Review

References (47)

1. Paria B.C.et al. Blastocyst's state of activity determines the 'window' of implantation in the mouse receptive uterus. Proc. Natl. Acad. Sci. U. S. A. 90:1993;10159-10162.
2. Dey S.K. Implantation. Adashi E.Y. Reproductive Endocrinology, Surgery and Technology. 1996;421-434 Lippincott-Raven.
3. Das S.K.et al. Heparin-binding EGF-like growth factor gene is induced in the mouse uterus temporally by the blastocyst solely at the site of its apposition. a possible ligand for interaction with blastocysts EGF-receptor in implantation Development. 120:1994;1071-1083.
4. Chakraborty I.et al. Developmental expression of the cyclo-oxygenase genes in the peri-implantation mouse uterus and their differential regulation by the blastocyst and ovarian steroids. J. Mol. Endocrinol. 16:1996;107-122.
5. Das S.K.et al. Expression of betacellulin and epiregulin genes in the mouse uterus temporally by the blastocyst solely at the site of its apposition is coincident with the 'window' of implantation. Dev. Biol. 190:1997;178-190.
6. Rankin J.C.et al. Early involvement of cyclic nucleotides in the artificially stimulated decidual cell reaction in the mouse uterus. Biol. Reprod. 17:1977;549-554.
7. Lim H.et al. Multiple reproductive failures in cyclooxygenase 2-deficient mice. Cell. 91:1997;197-208.
8. Smith W.L., DeWitt D.L. Prostaglandin endoperoxide H synthase-1 and-2. Adv. Immunol. 62:1996;167-215.
9. Dinchuk J.E.et al. Renal abnormalities and an altered inflammatory response in mice lacking cyclooxygenase II. Nature. 378:1995;406-409.
10. Langenbach R.et al. Prostaglandin synthase 1 gene disruption in mice reduces arachidonic acid-induced inflammation and indomethacin-induced gastric ulceration. Cell. 83:1995;483-492.
11. Morham S.G.et al. Prostaglandin synthase 2 gene disruption causes severe renal pathology in the mouse. Cell. 83:1995;473-482.
12. Negishi M.et al. Molecular mechanism of diverse actions of prostanoid receptors. Biochim. Biophys. Acta. 1259:1995;109-120.
13. Yang Z.M.et al. Potential sites of prostaglandin actions in the periimplantation mouse uterus. differential expression and regulation of prostaglandin receptor genes Biol. Reprod. 56:1997;368-379.
14. Ushibuki F.et al. Impaired febrile response in mice lacking the prostaglandin E receptor subtype EP3. Nature. 395:1998;281-284.
15. Hizaki H.et al. Abortive expansion of the cumulus and impaired fertility in mice lacking the prostaglandin E receptor subtype EP2. Proc. Natl. Acad. Sci. U. S. A. 96:1999;10501-10506.
16. Kennedy C.R.J.et al. Salt-sensitive hypertension and reduced fertility in mice lacking the prostaglandin EP2 receptor. Nat. Med. 5:1999;217-220.
17. Tilley S.L.et al. Reproductive failure and reduced blood pressure in mice lacking the EP2 prostaglandin E2 receptor. J. Clin. Invest. 103:1999;1539-1545.
18. Mangelsdorf D.J., Evans R.M. The RXR heterodimers and orphan receptors. Cell. 83:1995;841-850.
19. Kliewer S.A.et al. Differential expression and activation of a family of murine peroxisome proliferator-activated receptors. Proc. Natl. Acad. Sci. U. S. A. 91:1994;7355-7359.
20. Desvergne B., Wahli W. Peroxisome proliferator-activated receptors. nuclear control of metabolism Endocr. Rev. 20:1999;649-688.
21. Kliewer S.A.et al. Convergence of 9-cis retinoic acid and peroxisome proliferator signaling pathways through heterodimer formation of their receptors. Nature. 358:1992;771-774.
22. Direnzo J.et al. Peroxisome proliferator-activated receptors and retinoic acid receptors differentially control the interactions of retinoid X receptor heterodimers with ligands, coactivators, and corepressors. Mol. Cell. Biol. 17:1997;2166-2176.
23. Zhou G.R.et al. Nuclear receptors have distinct affinities for coactivators. characterization by fluorescence resonance energy transfer Mol. Endocrinol. 12:1998;1594-1604.
24. Isseman I., Green S. Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators. Nature. 347:1990;645-650.
25. Schoonjans K.J.et al. The peroxisome proliferator activated receptors (PPARs) and their effects on lipid metabolism and adipocyte differentiation. Biochim. Biophys. Acta. 1302:1996;93-109.
26. Jiang C.et al. PPARγ agonists inhibit production of monocyte inflammatory cytokines. Nature. 391:1998;82-86.
27. Mueller E.et al. Terminal differentiation of human breast cancer through PPARγ Mol. Cell. 1:1998;465-470.
28. Ricote M.et al. The peroxisome proliferator-activated receptor-γ is a negative regulator of macrophage activation. Nature. 391:1998;79-81.
29. Staels B.et al. Activation of human aortic smooth-muscle cells is inhibited by PPARα but not by PPARγ activators. Nature. 393:1998;790-793.
30. Tontonoz P.et al. PPARγ promotes monocyte-macrophage differentiation and uptake of oxidized LDL. Cell. 93:1998;241-252.
31. Lee S.S.et al. Targeted disruption of the α isoform of the peroxisome proliferator-activated receptor gene in mice results in abolishment of the pleiotropic effects of peroxisome proliferators. Mol. Cell. Biol. 15:1995;3012-3022.
32. Barak Y.et al. PPARγ is required for placental, cardiac, and adipose tissue development. Mol. Cell. 4:1999;585-595.
33. Kubota N.et al. PPARγ mediates high fat diet-induced adipocyte hypertrophy and insulin resistance. Mol. Cell. 4:1999;597-609.
34. Braissant O., Wahli W. Differential expression of peroxisome proliferator-activated receptors-α,-β, and -γ during rat embryonic development. Endocrinology. 139:1998;2748-2754.
35. Lim H.et al. Cyclo-oxygenase-2-derived prostacyclin mediates embryo implantation in the mouse via PPARδ Genes Dev. 13:1999;1561-1574.
36. McAdam B.F.et al. Systemic biosynthesis of prostacyclin by cyclooxygenase (COX)-2. the human pharmacology of a selective inhibitor of COX-2 Proc. Natl. Acad. Sci. U. S. A. 96:1999;272-277.
37. Brock T.G.et al. Arachidonic acid is preferentially metabolized by cyclooxygenase-2 to prostacyclin and prostaglandin E2. J. Biol. Chem. 274:1999;11660-11666.
38. Murata T.F.et al. Altered pain perception and inflammatory response in mice lacking prostacyclin receptor. Nature. 388:1997;678-682.
39. Forman B.M.et al. Hypolipidemic drugs, polyunsaturated fatty acids, and eicosanoids are ligands for peroxisome proliferator-activated receptors α and δ Proc. Natl. Acad. Sci. U. S. A. 94:1997;4312-4317.
40. Berger J.et al. Novel PPARγ and PPARδ ligands produce distinct biological effects. J. Biol. Chem. 274:1999;6718-6725.
41. Meade E.A.et al. Peroxisome proliferators enhance cyclooxygenase-2 expression in epithelial cells. J. Biol. Chem. 274:1999;8328-8334.
42. He T.C.et al. PPARδ is an APC-regulated target of nonsteroidal anti-inflammatory drugs. Cell. 99:1999;335-345.
43. 2. Nature. 390:1997;622-625.
44. 2 in allergic response and parturition. Nature. 390:1997;618-622.
45. Nguyen M.T.et al. The prostaglandin receptor EP4 triggers remodelling of the cardiovascular system at birth. Nature. 390:1997;78-81.
46. Sugimoto Y.et al. Failure of parturition in mice lacking prostaglandin F receptor. Science. 277:1997;681-683.
47. 2. J. Clin. Invest. 103:1998;1994-2001.