Growth factor receptor inhibitor

About: Growth factor receptor inhibitor is a research topic. Over the lifetime, 4730 publications have been published within this topic receiving 297500 citations.

Targeting the type 1 insulin-like growth factor receptor as anti-cancer treatment.

Abstract: The type 1 insulin-like growth factor receptor (IGF1R) is overexpressed by many tumors, and mediates growth, motility and protection from apoptosis. Inhibition of IGF1R expression or function has been shown to block tumor growth and metastasis, and enhance sensitivity to cytotoxic drugs and irradiat

Mechanism of action of retinoids

Abstract: In several recent reviews, we have suggested that the mechanism of action of retinoids in controlling cell differentiation is related to their effects on the expression of oncogenes and peptide growth factors. It is currently believed that oncogenes control metabolic pathways that involve peptide growth factors and their receptors, as well as postreceptor signaling mechanisms. Retinoids, therefore, have been valuable probes to study the function of oncogenes and peptide growth factors. In several tumor cells, including human promyelocytic leukemia, human and murine neuroblastoma, and murine teratocarcinoma, retinoic acid induces terminal differentiation, accompanied by suppression of the expression of either the c-myc or the N-myc gene. Many studies have indicated that retinoic acid can markedly increase the number of cellular receptors for epidermal growth factor, which is partially encoded by another oncogene, erb-B. We have shown that retinoic acid greatly inhibits the anchorage-independent growth of a rat fibroblast cell line that has been transfected with the c-myc gene, particularly when these cells are stimulated by the combination of platelet-derived growth factor and transforming growth factor-beta. At present, the mechanisms by which retinoids control oncogene and growth factor expression are unknown. A wide range of new compounds, including the retinoidal benzoic acid derivatives, are now available to study these mechanisms, and will necessitate the identification of a high-affinity receptor for retinoids and the elucidation of the interaction of this receptor with the genome of the cell. The recent synthesis of new terephthalic acid anilides and chalcone carboxylic acid derivatives, which have retinoid-like activity, offers a particularly useful approach to this problem.

Nuclear accumulation of epidermal growth factor in cultured rat pituitary cells.

Abstract: Epidermal growth factor (EGF) is a mitogen for epidermal cells in vivo1,2 and for a wide variety of cells in culture3–5. Recently, we and others have reported that EGF can also regulate the cellular levels of various hormones6 and fibronectin7 at concentrations which only minimally influence cell division. In addition, EGF treatment of GH3 cells affects chromatin structure such that isolated nuclei from treated cells have an increased capacity to bind bacterial RNA polymerase in initiation site complexes6. Thus, the data suggest that various nuclear functions are modulated by EGF in GH3 cells despite its failure to affect DNA synthesis or cell proliferation. Recently, Yanker and Shooter8 have reported on the nuclear accumulation of nerve growth factor (NGF) in PC12 cells in which NGF does not promote cell division but does influence RNA and protein synthesis while inducing overt differentiation (neurite outgrowth). The similarities between the two systems and the various theories regarding the mechanism by which mitogens exert their growth-promoting and other effects9,10 led us to investigate whether an interaction between EGF and the cell nucleus can be demonstrated after surface binding and internalization of EGF in GH3 cells. We report here that when its lysosomal degradation is inhibited by chloroquine, EGF accumulates in the nucleus.