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pubmed:abstractText |
Human low-density lipoproteins (LDL) bind specifically and saturably to the surface of the trematode parasite, Schistosoma mansoni, in vitro. Here we have tested whether human monocytes process the bound LDL. Monocytes obtained by leukapheresis generate H2O2, kill schistosomula, and were seen here endocytosing fluorescently labeled human LDL that was bound to the surface of the parasites. Compounds known to inhibit uptake of LDL via the scavenger receptor, namely, acetylated LDL, polyinosinic acid, dextran sulfate, fucoidan, and polyvinyl sulfate, inhibited both endocytosis of LDL and cell-mediated killing. Non-functional analogs of these inhibitors, namely, polycytidylic acid and dextran, did not inhibit either endocytosis or killing. Monocytes obtained from whole blood after venipuncture neither killed the parasite nor endocytosed LDL from the worm surface. Thus, human monocyte killing of schistosomula may involve removal of LDL from the parasite surface via scavenger receptors.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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