About ITGB / Integrin:
ntegrin or ITGB as it is more commonly referred to has been discovered to be a transmembrane receptor. It is vital in cell to cell and cell to extracellular matrix adhesion (ECM).
Regulation of the cell cycle, intracellular cytoskeleton organization, and new receptor movement are all possible due to the ligand-binding activating the active signal transduction pathways.
ITGB’s presence in the body allows rapid response to cell surface events. There are a number of integrin types and they are found in all humans and animal species.
There are a number of clinical studies currently taking place which are investigating the pharmacological targeting of ITGB to treat tissue fibrosis in the lungs, kidney, and liver. The medical and pharmacological role of integrins is an important step in the quest to find new treatments for certain life-limiting and untreatable conditions.
ITGB Structure
ITGB consists of 18 a and 8 b subunits. These subunits can assemble to form 24 completely different receptors, each with a unique binding property. Each subunit has a helix spanning a single membrane and a relatively short cytoplasmic tail. The a subunits contain 1000 amino acids and the b subunits contain 750 amino acids.
Integrin Function
ITGBs are known to be traction receptors that can detect and transmit changes in the force that is acting on the ECM. In most mammals, ITGB is only found in particular cell types or tissue.
In fibronectin, the RGD sequence has been identified as an integrin-binding motif yet they also recognize non-RGD sequences in the ITGB ligands.