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PMID: 9294612 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Radiation-induced proliferation of the human A431 squamous carcinoma cells is dependent on EGFR tyrosine phosphorylation.

Oncogene ·Vol. 15 ·No. 10 ·1997-09-04 ·Pages 1191-7

Schmidt-Ullrich RK, Mikkelsen RB, Dent P, Todd DG, Valerie K, Kavanagh BD, Contessa JN, Rorrer WK, Chen PB

Abstract

Accelerated cellular repopulation has been described as a response of tumors to fractionated irradiation in both normal tissue and tumor systems. To identify the mechanisms by which cells enhance their proliferative rate in response to clinically used doses of ionizing radiation (IR) we have studied human mammary and squamous carcinoma cells which are autocrine growth regulated by the epidermal growth factor receptor (EGFR) and its ligands, transforming growth factor-alpha and EGF. Both EGF and IR induced EGFR autophosphorylation, comparable levels of phospholipase C gamma activation as measured by inositol-1,4,5-triphosphate production, and as a consequence oscillations in cytosolic [Ca2+]. Activities of Raf-1 and mitogen-activated protein kinase (MAPK) were also stimulated by EGF and IR by Ca(2+)-dependent mechanisms. All these responses to EGF and IR were dependent upon activation of EGFR as judged by the use of the specific inhibitor of EGFR autophosphorylation, tyrphostin AG1478. Importantly, IR-induced proliferation of A431 cells was also inhibited by AG1478. This is the first report which demonstrates a link between IR-induced activation of proliferative signal transduction pathways and enhanced proliferation. We propose that accelerated repopulation of tumors whose growth is regulated by EGFR is initiated by an IR-induced EGFR activation mechanism that mimics the effects of growth factors.

MeSH Terms
Breast Neoplasms/pathology Calcium/metabolism Calcium-Calmodulin-Dependent Protein Kinases/metabolism Carcinoma, Squamous Cell/pathology Cell Division/drug effects Enzyme Activation/radiation effects Enzyme Inhibitors/pharmacology ErbB Receptors/metabolism Humans Inositol 1,4,5-Trisphosphate/metabolism Isoenzymes/metabolism Nitriles/pharmacology Phospholipase C gamma Phosphotyrosine/metabolism Protein Serine-Threonine Kinases/metabolism Proto-Oncogene Proteins/metabolism Proto-Oncogene Proteins c-raf Quinazolines/pharmacology Radiation, Ionizing Receptor Protein-Tyrosine Kinases/antagonists & inhibitors Signal Transduction Tumor Cells, Cultured Type C Phospholipases/metabolism Tyrphostins
Chemicals
Enzyme Inhibitors Isoenzymes Nitriles Proto-Oncogene Proteins Quinazolines Tyrphostins RTKI cpd Phosphotyrosine Inositol 1,4,5-Trisphosphate ErbB Receptors Receptor Protein-Tyrosine Kinases Protein Serine-Threonine Kinases Proto-Oncogene Proteins c-raf Calcium-Calmodulin-Dependent Protein Kinases Type C Phospholipases Phospholipase C gamma Calcium
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Schmidt-Ullrich R K
Department of Radiation Oncology, Medical College of Virginia/Virginia Commonwealth University, Richmond 23298-0058, USA.
Mikkelsen R B
Dent P
Todd D G
Valerie K
Kavanagh B D
Contessa J N
Rorrer W K
Chen P B
Article Info
Journal
Oncogene
Abbr.
Oncogene
ISSN
0950-9232
Published
1997-09-04
Pages
1191-7
Language
English
Region
England
NLM ID
8711562
Subset
IM
Grants
NCI NIH HHS · CA65896 · United States
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