CNT3 (SLC28A3) is a concentrative nucleoside transporter that supports nucleoside salvage and therapeutic nucleoside-derivative uptake across plasma membranes
[1]. Mechanistically, hCNT3 shows broad substrate selectivity and uniquely transports nucleosides through both sodium- and proton-coupled mechanisms, unlike hCNT1 and hCNT2
[2]. Structural studies show that human CNT3 forms a trimeric architecture, and oligomerization supports transporter stability, function, and nucleoside translocation
[1][3]. In airway epithelial models, CNT3 contributes to apical adenosine elimination, thereby regulating adenosine-mediated inflammatory signaling
[4]. In HIV-1-infected adipose tissue, SLC28A3 mRNA is upregulated, linking CNT3 expression to antiretroviral and lipodystrophy-related research contexts
[5]. Compared with related isoforms, hCNT1 preferentially transports pyrimidine nucleosides, hCNT2 preferentially transports purine nucleosides, whereas hCNT3 has the broadest selectivity and widest expression profile
[2][3]. For experimental applications, CNT3 remains relevant to nucleoside analogue pharmacology because hCNT proteins mediate uptake of many antiviral and anticancer nucleoside-derived drugs
[2].