Inhibition of polymorphonuclear leukocyte activation by acetylcholinesterase.
Previously we had shown that basement membrane collagen (COL IV), and specifically residues 185-203 of the non-collagenous domain of the alpha3(IV) chain, inhibits PMN activation. Since acetylcholinesterase (AchE) possesses collagenous and non-collagenous domains, we tested its effect on PMN activation. Whole AchE and the AchE recombinant catalytic subunit inhibited PMN superoxide anion (O2-) generation. AchE synthetic peptides, residues 139-154 and 252-266 of the catalytic subunit, with sequence homology to that of the alpha3(IV) peptide also inhibited O2- production by PMN. Reactive pAb and mAb to the alpha3(IV) 185-203 peptide abolished the inhibitory effect of the AchE. The data show that the non-collagenous domain of the AchE down-regulates O2- production by PMN. We suggest that this inhibitory activity may serve as a protective mechanism against PMN-mediated injury at the level of vessel wall and the neuromuscular junction.
Ziaie
Z
Z
Connective Tissue Research Institute, University City Science Center and University of Pennsylvania, Philadelphia 19104, USA.
Kefalides
N A
NA
D000110:Acetylcholinesterase / Q000378:metabolism* / Q000494:pharmacology; D000906:Antibodies; D001485:Basement Membrane / Q000378:metabolism; D020134:Catalytic Domain; D003094:Collagen / Q000276:immunology / Q000378:metabolism; D015536:Down-Regulation; D006801:Humans; D066298:In Vitro Techniques; D018375:Neutrophil Activation; D009504:Neutrophils / Q000378:metabolism*; D010446:Peptide Fragments / Q000276:immunology / Q000494:pharmacology; D013481:Superoxides / Q000378:metabolism*
D000906:Antibodies; D010446:Peptide Fragments; D013481:Superoxides; D003094:Collagen; D000110:Acetylcholinesterase