Glycoprotein 60 (gp60) (gp60)

Glycoprotein 60 (gp60), also known as albondin, is a 60-kDa sialoglycoprotein primarily expressed on the surface of continuous endothelial cells, where it serves as a high-affinity receptor for native albumin [1, 5, 6]. It plays a critical role in mediating the transcytosis of albumin across the vascular endothelium into the interstitial space, a process that involves the activation of caveolin-1 and the formation of caveolae [1, 10, 11]. In the field of oncology, gp60 is a key therapeutic target because it is often overexpressed in the tumor-associated vasculature, facilitating the delivery of albumin-bound chemotherapeutics like nab-paclitaxel (Abraxane) [1, 10, 23]. By binding to gp60, these albumin-based drug carriers can effectively bypass the endothelial barrier and accumulate within the tumor microenvironment, enhancing therapeutic efficacy while potentially reducing systemic toxicity [1, 7, 22]. Beyond its role in drug delivery, gp60 is involved in the regulation of capillary permeability and vascular tone through its interaction with the Src kinase signaling pathway and the production of nitric oxide [11, 26]. Despite its established role in pharmacology, the specific gene encoding gp60 remains a subject of ongoing research, with some studies suggesting it may be immunologically related to glycophorins or other membrane proteins [1, 19]. The interaction between albumin and gp60 is also being explored for the delivery of other therapeutic agents, including nanoparticles loaded with cisplatin or gemcitabine [1, 7]. Understanding the gp60-mediated transport pathway is essential for optimizing albumin-based drug delivery systems and improving patient outcomes in cancer and inflammatory diseases [1, 18].

Other names

Albondin60-kDa sialoglycoproteinAlbumin receptorgp60 receptorEndothelial albumin receptor

Drugs utilize albumin as a carrier to bind to gp60 on endothelial cells, triggering caveolin-1-mediated endocytosis and transcytosis to cross the endothelial barrier and enter the tumor microenvironment [1, 10, 11].