{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Varghese B"],"funding":["NCI NIH HHS"],"pagination":["2356-65"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2999476"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["24(12)"],"pubmed_abstract":["Mitogenic and prosurvival effects underlie the tumorigenic roles of prolactin (PRL) in the pathogenesis of breast cancer. PRL signaling is mediated through its receptor (PRLr). A proteomics screen identified the pyruvate kinase M2 (PKM2), a glycolytic enzyme known to play an important role in tumorigenesis, as a protein that constitutively interacts with PRLr. Treatment of cells with PRL inhibited pyruvate kinase activity and increased the lactate content in human cells in a manner that was dependent on the abundance of PRLr, activation of Janus kinase 2, and tyrosine phosphorylation of the intracellular domain of PRLr. Knockdown of PKM2 attenuated PRL-stimulated cell proliferation. The extent of this proliferation was rescued by the knock-in of the wild-type PKM2 but not of its mutant ins"],"journal":["Molecular endocrinology (Baltimore, Md.)"],"pubmed_title":["Prolactin inhibits activity of pyruvate kinase M2 to stimulate cell proliferation."],"pmcid":["PMC2999476"],"funding_grant_id":["R01 CA115281","T32CA09140","T32 CA009140","R01 CA118740","CA118740","CA115281"],"pubmed_authors":["Swaminathan G","Rui H","Yang N","Tzimas C","Plotnikov A","Fuchs SY","Varghese B"],"additional_accession":[]},"is_claimable":false,"name":"Prolactin inhibits activity of pyruvate kinase M2 to stimulate cell proliferation.","description":"Mitogenic and prosurvival effects underlie the tumorigenic roles of prolactin (PRL) in the pathogenesis of breast cancer. PRL signaling is mediated through its receptor (PRLr). A proteomics screen identified the pyruvate kinase M2 (PKM2), a glycolytic enzyme known to play an important role in tumorigenesis, as a protein that constitutively interacts with PRLr. Treatment of cells with PRL inhibited pyruvate kinase activity and increased the lactate content in human cells in a manner that was dependent on the abundance of PRLr, activation of Janus kinase 2, and tyrosine phosphorylation of the intracellular domain of PRLr. Knockdown of PKM2 attenuated PRL-stimulated cell proliferation. The extent of this proliferation was rescued by the knock-in of the wild-type PKM2 but not of its mutant ins","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Dec","modification":"2025-04-05T14:46:11.184Z","creation":"2019-03-27T00:37:16Z"},"accession":"S-EPMC2999476","cross_references":{"pubmed":["20962042"],"doi":["10.1210/me.2010-0219"]}}