Endothelial cell surface integrins

Endothelial cell surface integrins are a family of heterodimeric transmembrane receptors, primarily including alpha-v beta-3, alpha-v beta-5, and alpha-5 beta-1, that mediate the attachment of endothelial cells to the extracellular matrix (ECM) and facilitate cell-cell interactions (NIH, 2006). These receptors are critical regulators of vascular biology, governing processes like cell survival, migration, and proliferation, which are essential for both normal vessel maintenance and the formation of new blood vessels, a process known as angiogenesis (Physiological Reviews, 2006). In pathological conditions such as cancer and chronic inflammation, specific endothelial integrins are significantly upregulated to support the metabolic demands of growing tissues and the recruitment of immune cells (Journal of Nuclear Medicine, 2005). Consequently, they have become significant therapeutic targets, with drugs like the RGD-mimetic peptide cilengitide and various monoclonal antibodies designed to block their function and inhibit pathological angiogenesis (Nature, 2005). These drugs typically work by competitively inhibiting the binding of ECM ligands to the integrin's extracellular domain or by inducing conformational changes that prevent activation (MDPI, 2020). Despite their potential, therapeutic development has faced challenges, including the need for precise dosing to avoid paradoxical pro-angiogenic effects observed at low concentrations (NIH, 2020). Additionally, safety concerns such as bleeding risks and thrombocytopenia can arise due to cross-reactivity with related integrins on platelets (PubMed, 2010). Overall, endothelial integrins remain a key focus for developing anti-angiogenic and anti-inflammatory therapies across oncology, ophthalmology, and cardiovascular medicine (ACS, 2020).

Other names

Vascular integrinsAngiogenic integrinsEndothelial integrinsAdhesion receptors of the endothelium

Competitive inhibition of ligand binding (e.g., RGD-mimetic peptides), monoclonal antibody-mediated blockade of the extracellular domain, and allosteric modulation of integrin activation.