{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T09:02:30Z","timestamp":1791018150723,"version":"4.1.0"},"reference-count":61,"publisher":"American Physiological Society","issue":"1","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American Journal of Physiology-Cell Physiology"],"published-print":{"date-parts":[[2007,1]]},"abstract":"<jats:p>Sphingosine 1-phosphate (S1P), a bioactive sphingolipid involved in diverse biological processes, is generated by sphingosine kinase (SphK) and acts via intracellular and\/or extracellular mechanisms. We used biochemical, pharmacological, and physiological approaches to investigate in rat myometrium the contractile effect of exogenous S1P and the possible contribution of SphK in endothelin-1 (ET-1)-mediated contraction. S1P stimulated uterine contractility (EC<jats:sub>50<\/jats:sub>= 1 \u03bcM and maximal response = 5 \u03bcM) by a pertussis toxin-insensitive and a phospholipse C (PLC)-independent pathway. Phosphorylated FTY720, which interacts with all S1P receptors, except S1P<jats:sub>2<\/jats:sub>receptors, failed to mimic S1P contractile response, indicating that the effects of S1P involved S1P<jats:sub>2<\/jats:sub>receptors that are expressed in myometrium. Contraction mediated by S1P and ET-1 required extracellular calcium and Rho kinase activation. Inhibition of SphK reduced ET-1-mediated contraction. ET-1, via ET<jats:sub>A<\/jats:sub>receptors coupled to pertussis toxin-insensitive G proteins, stimulated SphK1 activity and induced its translocation to the membranes. Myometrial contraction triggered by ET-1 is consecutive to the sequential activation of PLC, protein kinase C, SphK1 and Rho kinase. Prolonged exposure of the myometrium to S1P downregulated S1P<jats:sub>2<\/jats:sub>receptors and abolished the contraction induced by exogenous S1P. However, in these conditions, the tension triggered by ET-1 was not reduced, indicating that SphK activated by ET-1 contributed to its contractile effect via a S1P<jats:sub>2<\/jats:sub>receptor-independent process. Our findings demonstrated that exogenous S1P and SphK activity regulated myometrial contraction and may be of physiological relevance in the regulation of uterine motility during gestation and parturition.<\/jats:p>","DOI":"10.1152\/ajpcell.00023.2006","type":"journal-article","created":{"date-parts":[[2006,9,7]],"date-time":"2006-09-07T00:39:16Z","timestamp":1157589556000},"page":"C240-C250","source":"Crossref","is-referenced-by-count":34,"title":["Exogenous sphingosine 1-phosphate and sphingosine kinase activated by endothelin-1 induced myometrial contraction through differential mechanisms"],"prefix":"10.1152","volume":"292","author":[{"given":"Denis","family":"Leiber","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yoshiko","family":"Banno","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zahra","family":"Tanfin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"24","reference":[{"key":"R1","doi-asserted-by":"crossref","unstructured":"Amiot F, Leiber D, Marc S, Harbon S.GRP-preferring bombesin receptors increase generation of inositol phosphates and tension in rat myometrium.Am J Physiol Cell Physiol265: C1579\u2013C1587, 1993.","DOI":"10.1152\/ajpcell.1993.265.6.C1579"},{"key":"R2","doi-asserted-by":"crossref","unstructured":"Berridge MJ.Inositol trisphosphate and calcium signalling.Nature361: 315\u2013325, 1993.","DOI":"10.1038\/361315a0"},{"key":"R3","doi-asserted-by":"crossref","unstructured":"Bhattacharya M, Babwah AV, Ferguson SS.Small GTP-binding protein-coupled receptors.Biochem Soc Trans32: 1040\u20131044, 2004.","DOI":"10.1042\/BST0321040"},{"key":"R4","doi-asserted-by":"crossref","unstructured":"Bilodeau D, Lamy S, Desrosiers RR, Gingras D, Beliveau R.Regulation of Rho protein binding to membranes by rhoGDI: inhibition of releasing activity by physiological ionic conditions.Biochem Cell Biol77: 59\u201369, 1999.","DOI":"10.1139\/o99-004"},{"key":"R5","doi-asserted-by":"crossref","unstructured":"Blom T, Slotte JP, Pitson SM, Tornquist K.Enhancement of intracellular sphingosine-1-phosphate production by inositol 1,4,5-trisphosphate-evoked calcium mobilisation in HEK-293 cells: endogenous sphingosine-1-phosphate as a modulator of the calcium response.Cell Signal17: 827\u2013836, 2005.","DOI":"10.1016\/j.cellsig.2004.11.022"},{"key":"R6","doi-asserted-by":"crossref","unstructured":"Bolz SS, Vogel L, Sollinger D, Derwand R, Boer C, Pitson SM, Spiegel S, Pohl U.Sphingosine kinase modulates microvascular tone and myogenic responses through activation of RhoA\/Rho kinase.Circulation108: 342\u2013347, 2003.","DOI":"10.1161\/01.CIR.0000080324.12530.0D"},{"key":"R7","doi-asserted-by":"crossref","unstructured":"Cario-Toumaniantz C, Reillaudoux G, Sauzeau V, Heutte F, Vaillant N, Finet M, Chardin P, Loirand G, Pacaud P.Modulation of RhoA-Rho kinase-mediated Ca2+ sensitization of rabbit myometrium during pregnancy: role of Rnd3.J Physiol552: 403\u2013413, 2003.","DOI":"10.1111\/j.1469-7793.2003.00403.x"},{"key":"R8","doi-asserted-by":"crossref","unstructured":"Davenport AP.International Union of Pharmacology. 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