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Pathway Description
Intracellular Signalling Through Prostacyclin Receptor and Prostacyclin
Bos taurus
Category:
Metabolite Pathway
Sub-Category:
Signaling
Created: 2018-08-31
Last Updated: 2019-09-12
Cyclooxygenase is the major producer of prostacyclin. Prostacyclin binding to its receptor increases vasodilation and decreases platelet aggregation. The receptor is a G-protein coupled receptor, upon its binding it activates G proteins causing the activation of adenylyl cyclase and production of cAMP messenger molecules. cAMP activates PKA (protein kinase A) which phosphorylates downstream effectors that lead to a specific cellular response.In vasodilation, the PKA activity causes phosphorylation of MLCK, decreasing its activity, resulting in dephosphorylation of MLC of myosin. This leads to smooth muscle relaxation resulting in vasodilation.
References
Intracellular Signalling Through Prostacyclin Receptor and Prostacyclin References
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Pubmed: 8557110
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Pubmed: 3080331
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Pubmed: 3081893
Robishaw JD, Smigel MD, Gilman AG: Molecular basis for two forms of the G protein that stimulates adenylate cyclase. J Biol Chem. 1986 Jul 25;261(21):9587-90.
Pubmed: 3015900
Showers MO, Maurer RA: A cloned bovine cDNA encodes an alternate form of the catalytic subunit of cAMP-dependent protein kinase. J Biol Chem. 1986 Dec 15;261(35):16288-91.
Pubmed: 3023347
Wiemann S, Kinzel V, Pyerin W: Isoform C beta 2, an unusual form of the bovine catalytic subunit of cAMP-dependent protein kinase. J Biol Chem. 1991 Mar 15;266(8):5140-6.
Pubmed: 2002051
Jedrzejewski PT, Girod A, Tholey A, Konig N, Thullner S, Kinzel V, Bossemeyer D: A conserved deamidation site at Asn 2 in the catalytic subunit of mammalian cAMP-dependent protein kinase detected by capillary LC-MS and tandem mass spectrometry. Protein Sci. 1998 Feb;7(2):457-69. doi: 10.1002/pro.5560070227.
Pubmed: 9521123
Kobayashi H, Inoue A, Mikawa T, Kuwayama H, Hotta Y, Masaki T, Ebashi S: Isolation of cDNA for bovine stomach 155 kDa protein exhibiting myosin light chain kinase activity. J Biochem. 1992 Dec;112(6):786-91. doi: 10.1093/oxfordjournals.jbchem.a123976.
Pubmed: 1284247
Kohama K, Okagaki T, Hayakawa K, Lin Y, Ishikawa R, Shimmen T, Inoue A: A novel regulatory effect of myosin light chain kinase from smooth muscle on the ATP-dependent interaction between actin and myosin. Biochem Biophys Res Commun. 1992 May 15;184(3):1204-11. doi: 10.1016/s0006-291x(05)80010-5.
Pubmed: 1534225
Ye LH, Hayakawa K, Kishi H, Imamura M, Nakamura A, Okagaki T, Takagi T, Iwata A, Tanaka T, Kohama K: The structure and function of the actin-binding domain of myosin light chain kinase of smooth muscle. J Biol Chem. 1997 Dec 19;272(51):32182-9. doi: 10.1074/jbc.272.51.32182.
Pubmed: 9405419
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Pubmed: 19390049
Henry GD, Trayer IP, Brewer S, Levine BA: The widespread distribution of alpha-N-trimethylalanine as the N-terminal amino acid of light chains from vertebrate striated muscle myosins. Eur J Biochem. 1985 Apr 1;148(1):75-82. doi: 10.1111/j.1432-1033.1985.tb08809.x.
Pubmed: 3979397
Morishita R, Nakayama H, Isobe T, Matsuda T, Hashimoto Y, Okano T, Fukada Y, Mizuno K, Ohno S, Kozawa O, et al.: Primary structure of a gamma subunit of G protein, gamma 12, and its phosphorylation by protein kinase C. J Biol Chem. 1995 Dec 8;270(49):29469-75. doi: 10.1074/jbc.270.49.29469.
Pubmed: 7493986
Fong HK, Hurley JB, Hopkins RS, Miake-Lye R, Johnson MS, Doolittle RF, Simon MI: Repetitive segmental structure of the transducin beta subunit: homology with the CDC4 gene and identification of related mRNAs. Proc Natl Acad Sci U S A. 1986 Apr;83(7):2162-6. doi: 10.1073/pnas.83.7.2162.
Pubmed: 3083416
Sugimoto K, Nukada T, Tanabe T, Takahashi H, Noda M, Minamino N, Kangawa K, Matsuo H, Hirose T, Inayama S, et al.: Primary structure of the beta-subunit of bovine transducin deduced from the cDNA sequence. FEBS Lett. 1985 Oct 28;191(2):235-40. doi: 10.1016/0014-5793(85)80015-6.
Pubmed: 2414128
Cuello F, Schulze RA, Heemeyer F, Meyer HE, Lutz S, Jakobs KH, Niroomand F, Wieland T: Activation of heterotrimeric G proteins by a high energy phosphate transfer via nucleoside diphosphate kinase (NDPK) B and Gbeta subunits. Complex formation of NDPK B with Gbeta gamma dimers and phosphorylation of His-266 IN Gbeta. J Biol Chem. 2003 Feb 28;278(9):7220-6. doi: 10.1074/jbc.M210304200. Epub 2002 Dec 16.
Pubmed: 12486123
This pathway was propagated using PathWhiz -
Pon, A. et al. Pathways with PathWhiz (2015) Nucleic Acids Res. 43(Web Server issue): W552–W559.
Propagated from SMP0000354
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