Human plasma kallikrein releases neutrophil elastase during blood coagulation.

Abstract

A B S T R A C T Elastase is released from human neutrophils during the early events of blood coagulation. Human plasma kallikrein has been shown to stimulate neutrophil chemotaxis, aggregation, and oxygen consumption. Therefore, the ability of kallikrein to release neutrophil elastase was investigated. Neutrophils were isolated by dextran sedimentation, and elastase release was measured by both an enzyme-linked immunosorbent assay, and an enzymatic assay using t-butoxycarbonyl-Ala-Ala-Pro-Val-amino methyl coumarin as the substrate. Kallikrein, 0.1-1.0 U/ml, (0.045-0.45 ,M), was incubated with neutrophils that were preincubated with cytochalasin B (5 Mg/ml). The release of elastase was found to be proportional to the kallikrein concentration. Kallikrein released a maximum of 34% of the total elastase content, as measured by solubilizing the neutrophils in the nonionic detergent Triton X-100. A series of experiments was carried out to determine if kallikrein was a major enzyme involved in neutrophil elastase release during blood coagulation. When 10 million neutrophils were incubated in 1 ml of normal plasma in the presence of 30

In vivo stimulation of neutrophil function by lenograstim (glycosylated rHug‐CSF) in oncohematologic patients: Results of a phase I trial

“…The NAP scores were evaluated on a scale from 0 to 4. Plasma elastase was evaluated using an indirect, competitive enzyme-linked immunosorbent assay (ELISA) [8].…”

Expression of Plasma Prekallikrein mRNA in Human Nonhepatic Tissues and Cell Lineages Suggests Special Local Functions of the Enzyme

“…Both enzymes can activate granulocytes (Schapira et al, 1982van der Graaf et al, 1982;Wachtfogel et al, 1983Wachtfogel et al, , 1986) and the complement system (Ghebrehiwet et al, 1981(Ghebrehiwet et al, , 1983DiScipio, 1982). FXIIa activates factor XI and in this manner triggers the intrinsic blood coagulation cascade.…”

Cellular expression of plasma prekallikrein in human tissues

“…The protease activity of PK is also involved in the activation of circulating neutrophils (Schapira et al, 1982Wachtfogel et al, 1983); it efficiently converts prourokinase plasminogen activator, thereby inducing the fibrinolytic cascade (Ichinose et al, 1986;Hauert et al, 1989). A major function of PK is the release from highmolecular-weight kininogen of the nonapeptide bradykinin, which through its specific receptor-coupling of second messengers regulates cellular events Blais et al, 2000).…”