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Albondin, commonly known as the albumin receptor gp60, is a 60 kDa glycoprotein primarily expressed on the luminal surface of microvascular endothelial cells (Schnitzer et al., 1994). Its primary biological role is to facilitate the transcytosis of albumin across the endothelial barrier, a process mediated by the activation of caveolae (Tiruppathi et al., 1997). Upon albumin binding, gp60 interacts with caveolin-1 and activates Src family kinases, leading to the budding of caveolae that transport albumin from the blood into the interstitial space. In the context of pharmacology, gp60 is a critical target for the delivery of albumin-bound drugs, such as nanoparticle albumin-bound (nab) paclitaxel, which exploits this pathway to enhance drug accumulation within tumors (Desai et al., 2006). This mechanism is particularly relevant in oncology, where tumors often exhibit increased albumin uptake to meet metabolic demands. Beyond cancer, gp60-mediated transport plays a role in maintaining vascular homeostasis and regulating fluid balance.
Binding of albumin or albumin-drug conjugates to gp60 on the endothelial cell surface triggers caveolae-mediated transcytosis, allowing the cargo to bypass the endothelial barrier and enter the underlying tissue or tumor microenvironment.
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