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Pathway Description
EPO Signaling Pathway
Rattus norvegicus
Category:
Protein Pathway
Sub-Categories:
Cytokine Signaling
Kinase Signaling
Gene Regulatory
Cellular Response
Created: 2018-09-20
Last Updated: 2019-08-16
The hormone erythropoietin, is a 166 amino acid protein with an apparent molecular weight in its native form of 39,000 Da. The molecule is heavily glycosylated since its mass derived from its amino acid content is 18,398. The selective interaction of a hormone with its target cells is usually mediated by cell membrane receptors specific for the particular hormone. Erythropoietin-responsive cells have a trypsin-sensitive receptor for the hormone which requires protein synthesis for its maintenance. Erythropoietin-responsive cells can interact with other hematopoietic growth factors, and such interactions may lead to competition for pathway-specific differentiation, particularly under conditions of high cell density. The amino-terminal region of the hormone is not involved in receptor binding.
References
EPO Signaling Pathway References
Kazansky AV, Raught B, Lindsey SM, Wang YF, Rosen JM: Regulation of mammary gland factor/Stat5a during mammary gland development. Mol Endocrinol. 1995 Nov;9(11):1598-609. doi: 10.1210/mend.9.11.8584036.
Pubmed: 8584036
Krejci P, Salazar L, Kashiwada TA, Chlebova K, Salasova A, Thompson LM, Bryja V, Kozubik A, Wilcox WR: Analysis of STAT1 activation by six FGFR3 mutants associated with skeletal dysplasia undermines dominant role of STAT1 in FGFR3 signaling in cartilage. PLoS One. 2008;3(12):e3961. doi: 10.1371/journal.pone.0003961. Epub 2008 Dec 17.
Pubmed: 19088846
Lundby A, Secher A, Lage K, Nordsborg NB, Dmytriyev A, Lundby C, Olsen JV: Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues. Nat Commun. 2012 Jun 6;3:876. doi: 10.1038/ncomms1871.
Pubmed: 22673903
Wen D, Boissel JP, Tracy TE, Gruninger RH, Mulcahy LS, Czelusniak J, Goodman M, Bunn HF: Erythropoietin structure-function relationships: high degree of sequence homology among mammals. Blood. 1993 Sep 1;82(5):1507-16.
Pubmed: 8364201
Nagao M, Suga H, Okano M, Masuda S, Narita H, Ikura K, Sasaki R: Nucleotide sequence of rat erythropoietin. Biochim Biophys Acta. 1992 Nov 15;1171(1):99-102. doi: 10.1016/0167-4781(92)90146-q.
Pubmed: 1420369
Masuda S, Nagao M, Takahata K, Konishi Y, Gallyas F Jr, Tabira T, Sasaki R: Functional erythropoietin receptor of the cells with neural characteristics. Comparison with receptor properties of erythroid cells. J Biol Chem. 1993 May 25;268(15):11208-16.
Pubmed: 7684373
Fujita M, Takahashi R, Kitada K, Watanabe R, Kitazawa S, Ashoori F, Liang P, Saya H, Serikawa T, Maeda S: Alternative splicing of the erythropoietin receptor gene correlates with erythroid differentiation in rat hematopoietic and leukemic cells. Cancer Lett. 1997 Jan 15;112(1):47-55. doi: 10.1016/S0304-3835(96)04544-2.
Pubmed: 9029168
Suh PG, Ryu SH, Moon KH, Suh HW, Rhee SG: Inositol phospholipid-specific phospholipase C: complete cDNA and protein sequences and sequence homology to tyrosine kinase-related oncogene products. Proc Natl Acad Sci U S A. 1988 Aug;85(15):5419-23. doi: 10.1073/pnas.85.15.5419.
Pubmed: 2840660
Lee SJ, Ryu SH, Suh PG: Promoter region of the rat phospholipase C-gamma 1 gene. Biochem Biophys Res Commun. 1993 Jul 15;194(1):294-300. doi: 10.1006/bbrc.1993.1818.
Pubmed: 8392838
Vainikka S, Joukov V, Wennstrom S, Bergman M, Pelicci PG, Alitalo K: Signal transduction by fibroblast growth factor receptor-4 (FGFR-4). Comparison with FGFR-1. J Biol Chem. 1994 Jul 15;269(28):18320-6.
Pubmed: 7518429
Duhe RJ, Rui H, Greenwood JD, Garvey K, Farrar WL: Cloning of the gene encoding rat JAK2, a protein tyrosine kinase. Gene. 1995 Jun 9;158(2):281-5. doi: 10.1016/0378-1119(95)00041-4.
Pubmed: 7607555
Li JM, Mogi M, Tsukuda K, Tomochika H, Iwanami J, Min LJ, Nahmias C, Iwai M, Horiuchi M: Angiotensin II-induced neural differentiation via angiotensin II type 2 (AT2) receptor-MMS2 cascade involving interaction between AT2 receptor-interacting protein and Src homology 2 domain-containing protein-tyrosine phosphatase 1. Mol Endocrinol. 2007 Feb;21(2):499-511. doi: 10.1210/me.2006-0005. Epub 2006 Oct 26.
Pubmed: 17068200
Saether PC, Westgaard IH, Hoelsbrekken SE, Benjamin J, Lanier LL, Fossum S, Dissen E: KLRE/I1 and KLRE/I2: a novel pair of heterodimeric receptors that inversely regulate NK cell cytotoxicity. J Immunol. 2008 Sep 1;181(5):3177-82. doi: 10.4049/jimmunol.181.5.3177.
Pubmed: 18713988
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 SMP0069678
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