Mode of binding and internalization into mouse macrophages of heparin complexed with polycations.
Heparin uptake by cultured macrophages was investigated from the standpoint of: (1) whether the increased uptake in the presence of polycations is due to charge neutralization, and (2) whether the heparin becomes internalized. Regarding the first point, our results are compatible with the notion that charge neutralization is mainly responsible for the enhanced uptake of heparin in the presence of protamine, histone, poly(DL-lysine) and poly(L-ornithine). As for the second point, chasing experiments at low and high temperatures strongly suggest that while heparin binds onto the cell membrane at both 4 degrees C and 37 degrees C, it undergoes internalization only at 37 degrees C.
D000818:Animals; D001692:Biological Transport; D002478:Cells, Cultured; D006493:Heparin / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D008264:Macrophages / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism*; D011107:Polylysine / Q000378:metabolism*; D011479:Protamines / Q000378:metabolism*; D013501:Surface-Active Agents / Q000378:metabolism*
D006657:Histones; D010455:Peptides; D011479:Protamines; D013501:Surface-Active Agents; C008973:polyornithine; D011107:Polylysine; D006493:Heparin