Inhibition of Polymorphonuclear Leukocyte Activation by Acetylcholinesterase

ISSN： 1522-4724

Source： Molecular Cell Biology Research Communications, Vol.2, Iss.1, 1999-07, pp. : 11-14

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Abstract

Previously we had shown that basement membrane collagen (COL IV), and specifically residues 185-203 of the non-collagenous domain of the α3(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 (O^-₂) generation. AchE synthetic peptides, residues 139-154 and 252-266 of the catalytic subunit, with sequence homology to that of the α3(IV) peptide also inhibited O^-₂ production by PMN. Reactive pAb and mAb to the α3(IV) 185-203 peptide abolished the inhibitory effect of the AchE. The data show that the non-collagenous domain of the AchE down-regulates O^-₂ 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.