Albumin-binding protein gp60 (gp60) (gp60)

Albumin-binding protein gp60, also known as albondin, is a 60 kDa cell surface glycoprotein primarily expressed on the luminal surface of vascular endothelial cells (Schnitzer et al., 1994, J. Biol. Chem. 269:6072-6082). It serves as a specific receptor for albumin, facilitating the transcytosis of albumin and albumin-bound molecules from the blood into the interstitial space (Tiruppathi et al., 1997, Proc. Natl. Acad. Sci. USA 94:1362-1367). This process is mediated through the activation of caveolae-mediated endocytosis upon albumin binding, involving interactions with caveolin-1 and Src-family kinases (Minshall et al., 2000, J. Cell Biol. 150:1057-1070). In the context of oncology, gp60 is exploited to enhance the delivery of albumin-bound chemotherapeutics, such as nab-paclitaxel (Abraxane), into tumor tissues (Desai et al., 2006, Clin. Cancer Res. 12:1317-1324). By leveraging the natural albumin transport pathway, these drugs can achieve higher intratumoral concentrations compared to conventional formulations. Beyond drug delivery, gp60 plays a critical role in maintaining vascular homeostasis and regulating fluid balance across the endothelium by controlling albumin flux. Dysregulation of gp60-mediated transport is associated with inflammatory conditions and increased vascular permeability (Vogel et al., 2001, Am. J. Physiol. Lung Cell Mol. Physiol. 281:L412-L422).

Other names

AlbondinGlycoprotein 60gp60 receptorEndothelial albumin receptor

Binding of albumin to gp60 on the endothelial surface triggers the clustering of gp60 and its association with caveolin-1, initiating the formation of caveolae that transport albumin across the endothelial cell layer via transcytosis.