Surface membrane clearing of receptor-ligand complexes in human blood platelets.
Human blood platelets were challenged sequentially in vitro with polyclonal anti-platelet antibodies and cationized ferritin. Both ligands bound to the surface membrane and were sequestered by internalization into a surface-connected membrane system (SCS) with a cleared surface membrane as the eventual result. Patching and capping of bound antibody preceded internalization, and platelets cooperated in the clearing process by adhering to each other at capped areas and by mutual covering up, a process dubbed platelet hugging. The internalization process was repeated upon challenge with the second ligand, the two ligands being sequestered as separate deposits in the SCS, mirroring the two cycles of internalization. Platelets were activated during internalization process and tended to aggregate. In aggregates, surfaces exposed to the medium were cleared of ligand, which accumulated in the intercellular spaces and within the SCS of the aggregated platelets. Aggregation but not internalization and hugging was prevented by adenosine and adenosine monophosphate.
Behnke
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Institute of Anatomy C, University of Copenhagen, Panum Institute.
D000241:Adenosine / Q000494:pharmacology; D000906:Antibodies / Q000276:immunology; D001792:Blood Platelets / Q000276:immunology / Q000378:metabolism* / Q000648:ultrastructure; D002462:Cell Membrane / Q000378:metabolism; D005293:Ferritins / Q000378:metabolism; D006801:Humans; D008024:Ligands; D046911:Macromolecular Substances; D010974:Platelet Aggregation / Q000187:drug effects; D011955:Receptors, Drug / Q000378:metabolism*
D000906:Antibodies; D008024:Ligands; D046911:Macromolecular Substances; D011955:Receptors, Drug; D005293:Ferritins; D000241:Adenosine