Albondin (Gp60) (Gp60)

Albondin, commonly referred to as Gp60, is a 60-kDa cell surface glycoprotein primarily localized on the luminal membrane of vascular endothelial cells. It functions as a high-affinity receptor for albumin, playing a critical role in the transendothelial transport (transcytosis) of albumin and its associated ligands from the intravascular compartment to the interstitial space. The binding of albumin to Gp60 initiates a signaling cascade involving the activation of Src family kinases, which subsequently phosphorylate caveolin-1, leading to the budding and fission of caveolae (Schnitzer et al., 1994; Tiruppathi et al., 1997). This receptor-mediated pathway is a major target for nanoparticle albumin-bound (nab) technology, such as nab-paclitaxel (Abraxane), which exploits Gp60 to enhance drug delivery across the blood-vessel wall and into the tumor microenvironment (Desai et al., 2006). Beyond its role in drug delivery, Gp60 is a key determinant of vascular barrier function, and its dysregulation is associated with increased vascular permeability in inflammatory conditions and solid tumors (Minshall et al., 2002).

Other names

Glycoprotein 60Gp60 albumin receptorAlbumin-binding protein 60 kDaEndothelial albumin receptorABP60

Albondin (Gp60) facilitates the transcytosis of albumin and albumin-bound drugs across the vascular endothelium by triggering a Src kinase-dependent signaling pathway that induces caveolae formation (Schnitzer et al., 1994; Tiruppathi et al., 1997).