This review presents the contemporary knowledge on the epidermal growth factor receptor (EGFR) structure and function, and participation in neoplastic transformation. The EGFR has been implicated in the pathogenesis of multiple human cells and tissues. Altered levels of the receptor have been found in, among others, breast, prostate, and colon carcinomas. Usually, overexperssion of EGFR appears to confer a worse prognosis. Also some tumours types expressed structurally altered EGFR with deletion in extracellular domain. The correlation of EGFR expression with invasive or disseminated tumours and the connection with drug insensitivity provide ready justification for therapeutic intervention aimed at modulating the activity of this receptor.
Exposure of cells to hyperthermic temperatures (43° to 48°C) results in an increase of the total protein mass which coisolates with the nuclei. Prominent physiological effect of heat-shock on nuclear structure is inhibition of DNA replication and repair, and also RNA synthesis and processing. Heat-shock-induced p rotein mass increase has been shown to correlate with ultrastructural changes and polypeptide composition of nuclear skeleton - nuclear matrix.
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