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Inhibition of chemotaxis Ng-monomethyl-L-arginine: a role for cyclic GMP
SS Kaplan, T Billiar, RD Curran, UE Zdziarski, RL Simmons and RE Basford
Department of Pathology, University of Pittsburgh School of Medicine, PA.
The metabolism of L-arginine to nitric oxide (NO) has been shown to be
important for the effector functions of many cell types, including
polymorphonuclear (PMN) leukocytes. Its effect appears to be mediated at
least in part by NO stimulation of soluble guanylate cyclase. We evaluated
the role of this pathway in two PMN effector functions: cell movement and
microbial killing, using the competitive inhibitor of L- arginine
conversion to NO, NG-monomethyl-L-arginine (NMA). We also evaluated the
effect of additional L-arginine and dibutyryl cyclic guanosine
monophosphate (cGMP) on any NMA-associated changes. Human peripheral blood
neutrophils were used and the cells were incubated with and without NMA.
Chemotaxis was evaluated using a 48-well micro- Boyden chamber. Microbial
killing was evaluated using S aureus strains D2C and 502A. These studies
demonstrated that chemotaxis to formyl- methionyl-leucyl-phenylalanine was
markedly inhibited in NMA-treated cells. This inhibition could be overcome
if L-arginine or dibutyryl cGMP were added with the NMA. In contrast,
microbial killing of S aureus was unaffected by NMA. These observations
support the hypothesis that the L-arginine metabolism to NO and its effect
on the cGMP level may be important for the dynamic changes required for
neutrophil chemotaxis.
Volume 74,
Issue 6,
pp. 1885-1887,
11/01/1989
Copyright © 1989 by The American Society of Hematology
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