Eireseptorityrosiinikinaasit

Eireseptorityrosiinikinaasit, often abbreviated as EGFR, are a family of cell surface receptors that play a crucial role in cellular processes such as growth, differentiation, and survival. They belong to the larger family of receptor tyrosine kinases. The EGFR family consists of four members: EGFR (also known as ErbB1), HER2 (ErbB2), HER3 (ErbB3), and HER4 (ErbB4). These receptors are activated by binding to specific ligands, which are growth factors like epidermal growth factor (EGF) and transforming growth factor alpha (TGF-α).

Upon ligand binding, the EGFR receptors undergo a conformational change, leading to their dimerization and activation of their intracellular tyrosine kinase domain. This activated kinase domain then phosphorylates specific tyrosine residues on the receptor itself and on other intracellular proteins. These phosphorylation events trigger downstream signaling cascades, including the Ras/MAPK pathway, the PI3K/Akt pathway, and the STAT pathway. These pathways ultimately regulate gene expression and control various cellular functions.

Dysregulation of EGFR signaling is implicated in the development and progression of numerous diseases, particularly various types of cancer. Mutations, amplifications, or overexpression of EGFR or its ligands can lead to uncontrolled cell proliferation, survival, and metastasis. Consequently, EGFR has become a significant target for cancer therapy, with several drugs designed to inhibit EGFR activity or block its signaling pathways. These targeted therapies have shown considerable success in treating certain cancers, such as non-small cell lung cancer and colorectal cancer. Research continues to explore the complex roles of EGFR in health and disease and to develop more effective therapeutic strategies.