자궁경부암 조직에서 표피성장인자 수용체의 함량 측정과 임상적 예후인자와의 관계

Abstract

It has been investigated over recent decades that the molecular mechanisms involved in the development and uncontrolled proliferation of cancers involve abnormalities of oncogenes and growth factor-receptor systems. Epidermal growth factor(EGF) is a single-chain polypeptide(MW 6045) that was first isolated from the mouse submaxillary gland by Cohen in 1962. It is known that the epidermal growth factor-stimulated growth regulatory system is involved in cellular proliferation, both normal and neoplastic(Cowley et al., 1986 ; Ozanne et al., 1986 ; Stoscheck et al., 1986 ; Fixher et al., 1990). In order for EGF to interact with the cell, a specific receptor located at the cell surface is required. Epidermal growth factor receptor(EGFR) is a 170 KDa membrane-bound glycoprotein encoded for by the c-erbB-1 oncogene. It was first purified from the A431 cellline which was derived from the epidermoid carcinoma of the vulva(Cohen, 1983 ; Carpenter et al., 1986 ; Carpenter et al., 1987 ; Yarden et al., 1988). EGFR is a member of growth factor receptor family of protein tyrosine kinases, a class of cell cycli regulatory molecules. The receptor is capable of binding several ligands such as EGF, transforming growth factor(TGF)a(Fisher et al., 1990), amphiregulin(Shoyab et al.,1989), and heparin-binding EGF(Higashiyama et al., 1991). It is activated when its ligand binds to the extracellular domain, resulting in autophosphorylation of the receptor`s intracellular tyrosine kinase domain(Cohen et al., 1980 ; Schreiber et al., 1983). Dimerization, conformational changes ans internalization of EGFR function to transmit intracellular signals leading to regulation of cell growth(Carpenter and Cohen, 1979).