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Plasmin is a potent and specific chemoattractant for human peripheral
monocytes acting via a cyclic guanosine monophosphate-dependent pathway
T Syrovets, B Tippler, M Rieks and T Simmet
Department of Pharmacology and Toxicology, Ruhr University, Bochum,
Germany.
We have previously reported that the serine protease plasmin generated
during contact activation of human plasma triggers biosynthesis of
leukotrienes (LTs) in human peripheral monocytes (PMs), but not in
polymorphonuclear neutrophils (PMNs). We now show that purified plasmin
acts as a potent chemoattractant on human monocytes, but not on PMNs. Human
plasmin or plasminogen activated with urokinase, but not active
site-blocked plasmin or plasminogen, elicited monocyte migration across
polycarbonate membranes. Similarly, stimulation of monocytes with plasmin,
but not with active site-blocked plasmin or plasminogen, induced actin
polymerization. As assessed by checkerboard analysis, the plasmin-mediated
monocyte locomotion was a true chemotaxis. The plasmin- induced chemotactic
response was inhibited by the lysine analog trans-4-
(aminomethyl)cyclohexane-1-carboxylic acid (t-AMCA), which prevents binding
of plasmin/ogen to the appropriate membrane binding sites. In addition,
active site-blocked plasmin inhibited monocyte migration triggered by
active plasmin. Further, plasmin-induced monocyte chemotaxis was inhibited
by pertussis toxin (PTX) and 1-O-hexadecyl-2-O- methyl-rac-glycerol (HMG)
and chelerythrine, two structurally unrelated inhibitors of protein kinase
C (PKC). Plasmin, but not active site- blocked plasmin or plasminogen,
triggered formation of cyclic guanosine monophosphate (cGMP) in monocytes.
LY83583, an inhibitor of soluble guanylyl cyclase, inhibited both
plasmin-induced cGMP formation and the chemotactic response. The latter
effect could be antagonized by 8-bromo- cGMP. In addition, KT5823 and
(Rp)-8-(p-chlorophenylthio)guanosine- 3',5'-cyclic monophosphorothioate
[(Rp)-8-pCPT-cGMPs], two structurally unrelated inhibitors of
cGMP-dependent protein kinase, inhibited plasmin-mediated monocyte
chemotaxis. Thus, beyond being a stimulus for lipid mediator release,
plasmin is a potent and specific chemoattractant for human monocytes acting
via a cGMP-dependent mechanism. Therefore, plasmin represents a
proinflammatory activator for human monocytes.
Volume 89,
Issue 12,
pp. 4574-4583,
06/15/1997
Copyright © 1997 by The American Society of Hematology
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