| http://purl.uniprot.org/citations/15358595 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15358595 | http://www.w3.org/2000/01/rdf-schema#comment | "The role of epidermal growth factor receptor (EGFR) tyrosine kinase and its downstream targets in the regulation of the transition from the G0/G1 phase into DNA synthesis in response to ANG II has not been previously investigated in intestinal epithelial IEC-18 cells. ANG II induced a rapid and striking EGFR tyrosine phosphorylation, which was prevented by selective inhibitors of EGFR tyrosine kinase activity (e.g., AG-1478) or by broad-spectrum matrix metalloproteinase (MMP) inhibitor GM-6001. Pretreatment of these cells with either AG-1478 or GM-6001 reduced ANG II-stimulated DNA synthesis by approximately 50%. To elucidate the downstream targets of EGFR, we demonstrated that ANG II stimulated phosphorylation of Akt at Ser473, mTOR at Ser2448, p70S6K1 at Thr389, and S6 ribosomal protein at Ser(235/236). Pretreatment with AG-1478 inhibited Akt, p70S6K1, and S6 ribosomal protein phosphorylation. Inhibition of phosphatidylinositol (PI)3-kinase with LY-294002 or mTOR/p70S6K1 with rapamycin reduced [3H]thymidine incorporation by 50%, i.e., to levels comparable to those achieved by addition of either AG-1478 or GM-6001. Utilizing Akt small-interfering RNA targeted to Akt1 and Akt2, Akt protein knockdown dramatically inhibited p70S6K1 and S6 ribosomal protein phosphorylation. In contrast, AG-1478 or Akt gene silencing exerted no detectable inhibitory effect on ANG II-induced extracellular signal-regulated kinase 1/2 phosphorylation in IEC-18 cells. Taken together, our results demonstrate that EGFR transactivation mediates ANG II-stimulated mitogenesis through the PI3-kinase/Akt/mTOR/p70S6K1 signaling pathway in IEC-18 cells."xsd:string |
| http://purl.uniprot.org/citations/15358595 | http://purl.org/dc/terms/identifier | "doi:10.1152/ajpgi.00200.2004"xsd:string |
| http://purl.uniprot.org/citations/15358595 | http://purl.uniprot.org/core/author | "Rozengurt E."xsd:string |
| http://purl.uniprot.org/citations/15358595 | http://purl.uniprot.org/core/author | "Chiu T."xsd:string |
| http://purl.uniprot.org/citations/15358595 | http://purl.uniprot.org/core/author | "Santiskulvong C."xsd:string |
| http://purl.uniprot.org/citations/15358595 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15358595 | http://purl.uniprot.org/core/name | "Am J Physiol Gastrointest Liver Physiol"xsd:string |
| http://purl.uniprot.org/citations/15358595 | http://purl.uniprot.org/core/pages | "G182-94"xsd:string |
| http://purl.uniprot.org/citations/15358595 | http://purl.uniprot.org/core/title | "EGF receptor transactivation mediates ANG II-stimulated mitogenesis in intestinal epithelial cells through the PI3-kinase/Akt/mTOR/p70S6K1 signaling pathway."xsd:string |
| http://purl.uniprot.org/citations/15358595 | http://purl.uniprot.org/core/volume | "288"xsd:string |
| http://purl.uniprot.org/citations/15358595 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15358595 |
| http://purl.uniprot.org/citations/15358595 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15358595 |
| http://purl.uniprot.org/uniprot/#_P62755-mappedCitation-15358595 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15358595 |
| http://purl.uniprot.org/uniprot/#_P47196-mappedCitation-15358595 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15358595 |
| http://purl.uniprot.org/uniprot/P47196 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/15358595 |
| http://purl.uniprot.org/uniprot/P62755 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/15358595 |