Regulatory role of E-NTPase/NTPDase in fat/CD36-mediated fatty acid uptake.
Fatty acid translocase (FAT)/CD36-mediated long-chain fatty acid uptake in human umbilical vessel endothelial cells is associated with as yet uncharacterized translocase activity. The molecular mechanism of its function is not yet understood. Numerous attempts to purify rat cardiac sarcolemmal E-NTPase (an integral membrane protein also referred to as ecto-Ca(2+)/Mg(2+)ATPase) have revealed a complete amino acid sequence identity for FAT/CD36 protein. The most striking observation is that purified CD36 from human platelets shows significant E-NTPase activity. In view of recent progress in understanding CD36 functional properties, an attempt is made in this article to illustrate the point that association of E-NTPase (possibly extracellular Ca(2+)/Mg(2+)nucleotide triphosphate diphosphohydrolase) activity with CD36 may be of potential functional significance.
Kannan
Subburaj
S
Division of Gastroenterology, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. sukannan@utmb.edu
D017766:Acid Anhydride Hydrolases / Q000502:physiology*; D000818:Animals; D001692:Biological Transport; D018955:CD36 Antigens / Q000378:metabolism*; D004789:Enzyme Activation; D005227:Fatty Acids / Q000493:pharmacokinetics*; D006801:Humans; D008562:Membrane Glycoproteins / Q000378:metabolism*; D008954:Models, Biological; D043583:Nucleoside-Triphosphatase; D027361:Organic Anion Transporters / Q000378:metabolism*; D051381:Rats
D018955:CD36 Antigens; D005227:Fatty Acids; D008562:Membrane Glycoproteins; D027361:Organic Anion Transporters; D017766:Acid Anhydride Hydrolases; D043583:Nucleoside-Triphosphatase