The protein encoded by this gene is the fourth major glycoprotein of the platelet surface and serves as a receptor for thrombospondin in platelets and various cell lines. Since thrombospondins are widely distributed proteins involved in a variety of adhesive processes, this protein may have important functions as a cell adhesion molecule. It binds to collagen, thrombospondin, anionic phospholipids and oxidized LDL. It directly mediates cytoadherence of Plasmodium falciparum parasitized erythrocytes and it binds long chain fatty acids and may function in the transport and/or as a regulator of fatty acid transport. Mutations in this gene cause platelet glycoprotein deficiency. Multiple alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Feb 2014]
Forensic Context
A study in mice demonstrated that the CD36 is a marker for capillary endothelial cells involved in trans-endothelial lipid processing within brown adipose tissue [Behrens et al. DOI:10.1016/j.molmet.2025.102252]. In human skin, the CD36 was identified as a scavenger receptor marker expressed in an immune cell cluster within wound-edge tissues [Liu et al. DOI:10.1016/j.stem.2024.11.013]. A study in rats demonstrated that the CD36 was significantly down-regulated in liver tissue on day 2 following a 20% total body surface area burn injury, indicating its role in altered lipid catabolism during the metabolic response to trauma [Jayaraman et al. DOI:10.1016/j.jss.2007.05.025]. In a separate investigation in mice, the CD36 was identified as over-expressed in liver tissue following Kupffer cell-specific, endothelial cell-specific, and neutron exposures to radiation, as noted in comparative analyses with other hepatotoxicants [Roudkenar et al. DOI:10.1269/jrr.07078].