Inhibition of human neutrophil aggregation by albumin. Relationship with cytoskeleton reorganization.
Albumin, at concentration normally present in plasma (approximately 600 microM), significantly inhibited leukotriene B4 formation induced by a receptor mediated (fMet-Leu-Phe) and a receptor independent (calcium ionophore A23187) stimuli in human neutrophils. The inhibition of leukotriene B4 synthesis was accompanied by a concomitant reduction of neutrophil aggregation. In addition, this plasma protein prevented the increase in F-actin content of neutrophils stimulated with fMet-Leu-Phe and A23187, thus suppressing actin polymerization. These data indicate that albumin profoundly affects biochemical and functional aspects of neutrophils suggesting, for this plasma protein, a regulatory role in the overall pattern of the inflammatory reaction.
Colli
S
S
Institute of Pharmacological Sciences, University of Milan, Italy.
Marinovich
M
M
Stragliotto
E
E
Galli
C L
CL
Tremoli
E
E
D000199:Actins / Q000097:blood; D000001:Calcimycin / Q000494:pharmacology; D002449:Cell Aggregation / Q000187:drug effects; D003599:Cytoskeleton / Q000502:physiology*; D006801:Humans; D007975:Leukotriene B4 / Q000096:biosynthesis; D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000494:pharmacology; D009504:Neutrophils / Q000502:physiology* / Q000648:ultrastructure; D012710:Serum Albumin, Bovine / Q000494:pharmacology*; D013050:Spectrometry, Fluorescence
D000199:Actins; D007975:Leukotriene B4; D012710:Serum Albumin, Bovine; D000001:Calcimycin; D009240:N-Formylmethionine Leucyl-Phenylalanine