PROGRESSIVE INACTIVATION OF CATHEPSIN-G AND ELASTASE RELEASED FROM ACTIVATED NEUTROPHILS IN-VITRO - LACK OF PARTICIPATION OF THE NEUTROPHILALPHA(1)-PROTEINASE INHIBITOR
P. Renesto et M. Chignard, PROGRESSIVE INACTIVATION OF CATHEPSIN-G AND ELASTASE RELEASED FROM ACTIVATED NEUTROPHILS IN-VITRO - LACK OF PARTICIPATION OF THE NEUTROPHILALPHA(1)-PROTEINASE INHIBITOR, The Journal of laboratory and clinical medicine, 123(6), 1994, pp. 906-913
Citations number
15
Categorie Soggetti
Medical Laboratory Technology","Medicine, General & Internal
Addition of platelets to activated human polymorphonuclear neutrophils
(PMNs) led to their aggregation and degranulation, with these respons
es decreasing as a function of the time interval between PMN activatio
n and platelet addition. Thus, for a 15-second interval platelet aggre
gation and serotonin release reached 51.3% +/- 6.7% (n = 11) and 64.3%
+/- 4.9% (n = 8), respectively, but after a 5-minute interval they we
re totally absent. This effect was correlated with the decrease in enz
ymatic activities of elastase (HLE) and cathepsin G (CAT-G) that were
released on PMN activation and responsible for the activation of nearb
y platelets (r = 0.86 and 0.90 for CAT-G and HLE, respectively; p < 0.
05). Because it has been recently shown that PMNs express an alpha(1)-
proteinase inhibitor (alpha(1)-PI) gene and secrete this antiproteinas
e at their surface, we investigated whether the PMN alpha(1)-PI could
regulate the biologic activities of both proteinases. Although superox
ide anions oxidize alpha(1)-PI and reduce its affinity for CAT-G and H
LE, maneuvers aimed at modifying their concentrations did not modify t
he loss of CAT-G and HLE. In fact, the progressive decrease of the two
proteinase enzymatic activities followed the same pattern whether PMN
s were present or not. It is concluded that PMN alpha(1)-PI is not inv
olved in the time-dependent inactivation of CAT-G and HLE released fro
m activated PMNs.