gp130proteiini

gp130 proteiini, also known as the interleukin-6 receptor subunit beta or IL6ST, is a transmembrane glycoprotein that plays a crucial role in cell signaling. It is a member of the Type I cytokine receptor family and is essential for the biological activity of several cytokines, including interleukin-6 (IL-6), interleukin-11 (IL-11), leukemia inhibitory factor (LIF), oncostatin M (OSM), ciliary neurotrophic factor (CNTF), and cardiotrophin-1 (CT-1).

gp130 itself does not bind directly to these cytokines. Instead, it forms a functional receptor complex with specific cytokine-binding alpha subunits. For example, IL-6 initially binds to the IL-6 receptor alpha (IL6RA), and this complex then recruits gp130 to form a high-affinity signaling receptor. This trans-heterodimerization leads to the activation of intracellular signaling pathways, primarily the Janus kinase (JAK)/signal transducer and activator of transcription (STAT) pathway.

The activation of gp130-mediated signaling is involved in a wide range of physiological processes. These include inflammation, immune responses, hematopoiesis, cell differentiation, cell proliferation, and acute phase responses in the liver. Dysregulation of gp130 signaling has been implicated in various diseases, such as cancer, autoimmune disorders, and cardiovascular diseases. Therefore, gp130 is a significant target for therapeutic interventions aimed at modulating these disease processes.