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Title: Insulin and epidermal growth factor stimulate phosphorylation of p185HER-2 in the breast carcinoma cell line, BT474. Author: Lin YZ, Li SW, Clinton GM. Journal: Mol Cell Endocrinol; 1990 Mar 05; 69(2-3):111-9. PubMed ID: 1691719. Abstract: The product of the HER-2 proto-oncogene, p185HER-2, was found to be amplified approximately 10-fold in the human breast carcinoma cell line, BT474, compared to a cell line, HBL-100, derived from normal breast tissue. To explore the possible role of p185HER-2 in growth of the breast carcinoma cells, we investigated factors that may modulate cell growth and phosphorylation of the HER-2 protein product. Two growth factors, epidermal growth factor (EGF) and insulin, stimulated phosphorylation of the HER-2 protein product. In response to insulin, the phosphoserine and phosphothreonine content in p185HER-2 was transiently enhanced about 6-fold. When EGF was added to BT474 cells there was 2- to 3-fold enhanced phosphorylation of serine and threonine residues in p185HER-2 which was maintained for at least 60 min. Although p185HER-2 has been found to be phosphorylated on tyrosine residues following EGF treatment of several different cell types, we estimate that less than 1% of the protein contained phosphotyrosine in the BT474 cells.[Abstract] [Full Text] [Related] [New Search]