Albondin (Glycoprotein 60) (gp60)

Albondin, also known as Glycoprotein 60 (gp60), is a 60 kDa cell surface receptor primarily expressed on the vascular endothelium of continuous capillaries [1, 14]. It serves as a high-affinity receptor for native serum albumin, playing a pivotal role in maintaining vascular oncotic pressure by mediating the transcytosis of albumin across the endothelial barrier [7, 16]. Upon binding albumin, gp60 interacts with caveolin-1, triggering the formation of caveolae that transport the albumin-receptor complex from the luminal to the abluminal side of the cell [1, 18]. In the field of oncology, gp60 is a critical target for albumin-based drug delivery systems, most notably nab-paclitaxel (Abraxane) [1, 15]. These therapeutics exploit the gp60-mediated transcytosis pathway to achieve enhanced accumulation within the tumor microenvironment, bypassing the endothelial barrier that often limits the delivery of conventional chemotherapeutics [18, 26]. Beyond its role in drug delivery, gp60 is involved in regulating capillary permeability and the transport of various albumin-bound ligands, including hormones and fatty acids [3, 14]. The molecular identity of gp60 at the genetic level remains a subject of ongoing research, though its functional role as an albumin transporter is well-established in pharmacological contexts [17, 20].

Other names

gp60Glycoprotein 60Albumin receptor gp60Endothelial albumin receptor

Mediates the transport of albumin-bound drugs across the vascular endothelium into the tumor microenvironment via caveolae-mediated transcytosis [1, 16, 18].