Phospholipase C-delta 1 and oxytocin receptor signalling: evidence of its role as an effector
SCIE
SCOPUS
- Title
- Phospholipase C-delta 1 and oxytocin receptor signalling: evidence of its role as an effector
- Authors
- Park, ES; Won, JH; Han, KJ; Suh, PG; Ryu, SH; Lee, HS; Yun, HY; Kwon, NS; Baek, KJ
- Date Issued
- 1998-04-01
- Publisher
- PORTLAND PRESS
- Abstract
- Although the oxytocin receptor modulates intracellular Ca2+ ion levels in myometrium, the identities of signal molecules have not been clearly clarified. Our previous studies on oxytocin receptor signalling demonstrated that 80 kDa G(h) alpha is a signal mediator [Baek, Kwon, Lee, Kim, Muralidhar and Im (1996) Biochem. J. 315, 739-744]. To elucidate the effector in the oxytocin receptor signalling pathway, we evaluated the oxytocin-mediated activation of phospholipase C (PLC) by using solubilized membranes from human myometrium and a three-component preparation containing the oxytocin receptor-G(h) alpha-PLC-delta 1 complex. PLC-delta 1 activity in the three-component preparation, as well as PLC activity in solubilized membranes, was increased by oxytocin in the presence of Ca2+ and activated G(h) alpha (GTP-bound G(h) alpha). Furthermore the stimulated PLC-delta 1 activity resulting from activation of G(h) alpha via the oxytocin receptor was significantly attenuated by the selective oxytocin antagonist desGlyNH(2)d(CH2)5[Tyr(Me)(2),Thr(4)] ornithine vasotocin or GDP. Consistent with these observations, co-immunoprecipitation and co-immunoadsorption of PLC-delta 1 in the three-component preparation by anti-G(h7)alpha antibody resulted in the PLC-delta 1 being tightly coupled to activated G(h) alpha on stimulation of the oxytocin receptor. These results indicate that PLC-delta 1 is the effector for G(h) alpha-mediated oxytocin receptor signalling.
- Keywords
- GTP-BINDING PROTEIN; GUANOSINE 5' -O-(3-THIOTRIPHOSPHATE); PHOSPHOINOSITIDE HYDROLYSIS; ADENYLATE-CYCLASE; MYOMETRIAL CELLS; G(H); EXPRESSION; MEMBRANE; CALCIUM; RAT
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/20819
- DOI
- 10.1042/bj3310283
- ISSN
- 0264-6021
- Article Type
- Article
- Citation
- BIOCHEMICAL JOURNAL, vol. 331, page. 283 - 289, 1998-04-01
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- There are no files associated with this item.
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