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Pathway Description
Nitric Oxide Signaling Pathway
Bos taurus
Category:
Protein Pathway
Sub-Categories:
Neurological Signaling
Cellular Response
Created: 2018-08-31
Last Updated: 2019-08-16
Nitric oxide (NO) is a neurotransmitter that synthesized from L-arginine with faciltation of nitric oxide synthase (NOS). Nitric oxide is essential and required in central nervous system (CNS) and peripheral nervous system (PNS). Nitric oxide has several important functions such as immune responses, blood flow regulation and modulation of neurotransmission. Nitric oxide also participates in controlling sleep, adjusting body temperature, neurosecretion as well as synaptic modulation and plasticity in CNS. While in PNS, nitric oxide participates in visceral smooth muscle relaxation as well as vasodilation mediation.
References
Nitric Oxide Signaling Pathway References
Zimin AV, Delcher AL, Florea L, Kelley DR, Schatz MC, Puiu D, Hanrahan F, Pertea G, Van Tassell CP, Sonstegard TS, Marcais G, Roberts M, Subramanian P, Yorke JA, Salzberg SL: A whole-genome assembly of the domestic cow, Bos taurus. Genome Biol. 2009;10(4):R42. doi: 10.1186/gb-2009-10-4-r42. Epub 2009 Apr 24.
Pubmed: 19393038
Lamas S, Marsden PA, Li GK, Tempst P, Michel T: Endothelial nitric oxide synthase: molecular cloning and characterization of a distinct constitutive enzyme isoform. Proc Natl Acad Sci U S A. 1992 Jul 15;89(14):6348-52. doi: 10.1073/pnas.89.14.6348.
Pubmed: 1378626
Nishida K, Harrison DG, Navas JP, Fisher AA, Dockery SP, Uematsu M, Nerem RM, Alexander RW, Murphy TJ: Molecular cloning and characterization of the constitutive bovine aortic endothelial cell nitric oxide synthase. J Clin Invest. 1992 Nov;90(5):2092-6. doi: 10.1172/JCI116092.
Pubmed: 1385480
Sessa WC, Harrison JK, Barber CM, Zeng D, Durieux ME, D'Angelo DD, Lynch KR, Peach MJ: Molecular cloning and expression of a cDNA encoding endothelial cell nitric oxide synthase. J Biol Chem. 1992 Aug 5;267(22):15274-6.
Pubmed: 1379225
Ishiwata H, Katsuma S, Kizaki K, Patel OV, Nakano H, Takahashi T, Imai K, Hirasawa A, Shiojima S, Ikawa H, Suzuki Y, Tsujimoto G, Izaike Y, Todoroki J, Hashizume K: Characterization of gene expression profiles in early bovine pregnancy using a custom cDNA microarray. Mol Reprod Dev. 2003 May;65(1):9-18. doi: 10.1002/mrd.10292.
Pubmed: 12658628
Watterson DM, Sharief F, Vanaman TC: The complete amino acid sequence of the Ca2+-dependent modulator protein (calmodulin) of bovine brain. J Biol Chem. 1980 Feb 10;255(3):962-75.
Pubmed: 7356670
Laub M, Steppuhn JA, Bluggel M, Immler D, Meyer HE, Jennissen HP: Modulation of calmodulin function by ubiquitin-calmodulin ligase and identification of the responsible ubiquitylation site in vertebrate calmodulin. Eur J Biochem. 1998 Jul 15;255(2):422-31. doi: 10.1046/j.1432-1327.1998.2550422.x.
Pubmed: 9716384
Griffith JP, Kim JL, Kim EE, Sintchak MD, Thomson JA, Fitzgibbon MJ, Fleming MA, Caron PR, Hsiao K, Navia MA: X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex. Cell. 1995 Aug 11;82(3):507-22. doi: 10.1016/0092-8674(95)90439-5.
Pubmed: 7543369
Selvakumar P, Lakshmikuttyamma A, Anderson DH, Sharma RK: Molecular cloning, expression, purification and characterization of calcineurin from bovine cardiac muscle. Biochimie. 2005 Nov;87(11):975-83. doi: 10.1016/j.biochi.2005.04.010.
Pubmed: 15967565
Liu J, Farmer JD Jr, Lane WS, Friedman J, Weissman I, Schreiber SL: Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell. 1991 Aug 23;66(4):807-15. doi: 10.1016/0092-8674(91)90124-h.
Pubmed: 1715244
Parker PJ, Coussens L, Totty N, Rhee L, Young S, Chen E, Stabel S, Waterfield MD, Ullrich A: The complete primary structure of protein kinase C--the major phorbol ester receptor. Science. 1986 Aug 22;233(4766):853-9. doi: 10.1126/science.3755547.
Pubmed: 3755547
Nishizuka Y: The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature. 1988 Aug 25;334(6184):661-5. doi: 10.1038/334661a0.
Pubmed: 3045562
Cazaubon SM, Parker PJ: Identification of the phosphorylated region responsible for the permissive activation of protein kinase C. J Biol Chem. 1993 Aug 15;268(23):17559-63.
Pubmed: 8349635
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
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 SMP0063777
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