RGD (Arg-Gly-Asp), sequence involved in cell adhesion

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Integrin alpha V also known as CD41 and Integrins beta 3 and beta 5 are transmembrane receptors with different masses according to their subunits. These integrins interact with the extracellular matrix facilitating cell adhesion and signaling. One key feature of these integrins is their binding to the arg-gly-asp (RGD) sequence found in matrix proteins important for cellular attachment. Integrin alpha V has a wide expression in various tissues including endothelial cells osteoclasts and epithelial tissues indicating its role in diverse cellular contexts.

Biological function summary

Integrins alpha V CD41 beta 3 and beta 5 contribute to cellular processes by forming heterodimers. These complexes participate actively in cell signaling migration and angiogenesis. The arg-gly-asp (RGD) motif serves as an important link between integrins and their matrix ligands impacting interactions with fibronectin and vitronectin. By mediating cellular activities through these complex formations integrins contribute to vital biological functions such as wound healing and tissue remodeling.

Pathways

These integrins play significant roles in both the PI3K/AKT and MAPK pathways. These pathways are critical for transmitting signals from the extracellular environment to intracellular effectors influencing cell proliferation survival and mobility. The integrins interact functionally with proteins like focal adhesion kinase (FAK) and Src family kinases which further propagate signaling events. Their involvement in these pathways links them to various cellular responses and physiological processes.

Integrins alpha V and beta 3 are associated with cancer progression and cardiovascular diseases. Their expression and signaling roles contribute to tumor invasion angiogenesis and atherosclerosis development. In cancer these integrins interact with matrix metalloproteinases which degrade extracellular matrix components and facilitate metastasis. Understanding their interactions and pathways offers insight into potential therapeutic targets for treating these conditions.