High density lipoprotein uptake by freshly isolated human peripheral blood T lymphocytes.

A high density lipoprotein (HDL) receptor/binding site has been identified on peripheral blood lymphocytes, and some of its properties were compared with those of HDL receptors on other cell types. Binding studies were performed using fluorescent (dioctadecylindocarbocyanine)-labelled HDL (DiI-HDL) and analyzed by fluorescence microscopy and quantitative flow cytometry. Uptake of low levels of DiI-HDL during a 2 h incubation at 37 degrees C was a property of all lymphocytes, i.e. not of one particular subset only. Visual inspection of these cells in the fluorescence microscope revealed both membrane and cytoplasmic fluorescence, indicating that DiI-HDL become internalized during the 2 h incubation; internalization appeared to be a receptor-mediated process. In competitive binding studies, apo E-free HDL competed effectively for DiI-HDL binding, whereas LDL competed very weakly. Two features of DiI-HDL uptake are demonstrated which are unique to lymphocytes: 1) it was enhanced 3-6-fold by inclusion of EDTA in the incubation medium or by incubating in Ca2+/Mg2+ free medium, and 2) it was saturable at 37 degrees C.