Hepatocyte Growth Factor Receptor (HGFR), also known as c-Met or MET receptor, is a transmembrane protein that belongs to the tyrosine kinase receptor family. It is encoded by the MET gene and is primarily expressed on the cell surface of epithelial and endothelial cells. The HGFR plays a critical role in a variety of cellular processes, including cell growth, migration, angiogenesis, and tissue regeneration.
As a receptor, HGFR is activated by its ligand, hepatocyte growth factor (HGF), resulting in a series of cellular signaling events. Upon binding, HGF induces receptor dimerization and autophosphorylation of tyrosine residues in the intracellular domain of HGFR. This phosphorylation cascade activates downstream signaling pathways, such as the MAPK/ERK, PI3K/AKT, and STAT3 pathways, which regulate cellular processes necessary for cell proliferation, survival, and motility.
HGFR is essential for embryonic development, tissue homeostasis, and wound healing. However, dysregulation of HGFR signaling has been implicated in various pathological conditions, including cancer. Activation of HGFR can promote tumor progression by stimulating cell proliferation, invasion, angiogenesis, and resistance to apoptosis. Therefore, HGFR and its signaling pathways have become a potential target for therapeutic intervention in cancer treatment.
Overall, Hepatocyte Growth Factor Receptor is a transmembrane protein involved in various cellular processes, primarily regulating cell growth and migration. Dysregulation of HGFR signaling can have profound implications on both normal and pathological processes, making it an important focus of scientific research and potential therapeutic applications.
