title: Mediators of immune complex-induced aggregation of polymorphonuclear neutrophils. I. C5a anaphylatoxin, neutrophil cationic proteins and their cleavage fragments.
abstract: This study reports the results of in vitro investigations on the aggregation of polymorphonuclear neutrophils (PMN) induced by the C5a anaphylatoxin complement component as well as the cationic proteins (CP), which are released by challenging PMN with immune complexes (IC). The carboxy-peptidase-derived des-Arg fragments of CP and C5a; CPi and C5ai, inactive in terms of anaphylactic and chemotactic activity, nevertheless showed a more potent ability to aggregate PMN than CP and C5a. The process of PMN aggregation required metabolic energy and divalent cations, Ca++ and Mg++. The microtubular system and the subplasmalemmal microfilaments appeared to be of critical importance. Electron microscopic studies on aggregates of PMN obtained on stimulation with CP, C5a, CPi and C5ai showed parallel tracts of variable length of cell membranes at the points where cells were in contact with each other.
mesh_terms: D000706:Anaphylatoxins / Q000302:isolation & purification / Q000494:pharmacology*; D000818:Animals; D000936:Antigen-Antibody Complex; D001798:Blood Proteins / Q000378:metabolism; D002449:Cell Aggregation; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003182:Complement C5 / Q000031:analogs & derivatives* / Q000302:isolation & purification; D015937:Complement C5a, des-Arginine; D003594:Cytoplasmic Granules / Q000032:analysis; D004588:Electrophoresis, Cellulose Acetate; D005966:Glucuronidase / Q000378:metabolism; D006801:Humans; D008970:Molecular Weight; D009504:Neutrophils / Q000276:immunology* / Q000648:ultrastructure; D010455:Peptides / Q000494:pharmacology*; D011817:Rabbits
chemical_list: D000706:Anaphylatoxins; D000936:Antigen-Antibody Complex; D001798:Blood Proteins; D003182:Complement C5; D015937:Complement C5a, des-Arginine; D010455:Peptides; D005966:Glucuronidase