Effect of elastase-like and chymotrypsin-like neutral proteases from human granulocytes on isolated clotting factors

Schmidt, W; Egbring, R; Havemann, K.

doi:10.1016/0049-3848(75)90081-x

Cited by 130 publications

(57 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…However, proMMP-9 rose higher and more quickly in FS blood than in the VP samples, suggesting that this MMP might contribute to the increased rate of fibrinolysis in FS samples (Figure 3). We observed a similar phenomenon with neutrophil elastase, which is known to degrade fibrin (Figure 4) [14]. The mechanism for the greater increase in proMMP-9 and elastase in FS serum is unclear, but neutrophils that have exuded into wounds secrete more of their gelatinase granules, which contain proMMP-9, than peripheral blood neutrophils [15].…”

Section: Discussionsupporting

confidence: 62%

Enhanced fibrinolysis in fingerstick blood samples: A possible role for matrix metalloproteinase-9

Vanjani

Park

Holt

et al. 2007

Thrombosis Research

View full text Add to dashboard Cite

Section: Discussionsupporting

confidence: 62%

Enhanced fibrinolysis in fingerstick blood samples: A possible role for matrix metalloproteinase-9

Vanjani

Park

Holt

et al. 2007

Thrombosis Research

View full text Add to dashboard Cite

“…The isolated enzyme yielded a single band on SDS polyacrylamide gels under nonreducing condition ( Fig. 1 of 5 ,iCi/,ug, >95% of the radioactivity migrated as a single peak on a SDS polyacrylamide gel with a mobility identical to that of the stained protein ( Fig. 1A and B).…”

Section: Resultsmentioning

confidence: 99%

“…A variety of neutral proteases (5,(14)(15)(16)(17)(18) and acidic cathepsins (3) of neutrophils are capable of degrading fibrin (ogen). Within leukocyte granules, elastase has been identified as one of the major fibrinolytic proteases active at neutral pH (19).…”

mentioning

confidence: 99%

Leukocyte Elastase Release during Blood Coagulation

Plow¹

1982

J. Clin. Invest.

184

View full text Add to dashboard Cite

A B S T R A C T Immunological detection of elastase, an enzyme present within leukocyte granules, has been used as a marker for polymorphonuclear leukocyte activation. Polymorphonuclear leukocytes contained 4.6 gg/107 cells, whereas erythrocytes, mononuclear cells, and platelets contained < 1% of this level. In plasma that was separated from blood cells after 1 h at 22°C, the mean level of elastase-related antigen in seven normal donors was 25±6 ng/ml. This level was unaltered by immediate separation of the plasma from the cells, by inclusion of protease inhibitors, or by anticoagulation of the plasma with either EDTA or acidcitrate-dextrose (the level in heparinized plasma was approximately threefold higher). In serum, the level of elastase-related antigen was 288±125 ng/ml, representing an 11.5-fold increase above plasma levels. The antigen detected in serum was immunochemically indistinguishable from the leukocyte enzyme. Release of elastase was observed when isolated polymorphonuclear leukocytes were added to nonanticoagulated platelet-rich or platelet-poor plasma, recalcified plasma, or to serum. Addition of a chelating agent to serum prevented elastase release, but calcium or magnesium did not induce release in the absence of plasma. Coagulation induced by addition of thrombin to plasma also failed to induce release. In whole blood or in anticoagulated plasma reconstituted with polymorphonuclear leukocytes and then recalcified, initial release of elastase occurred concomitantly with or slightly after clotting and reached maximal levels within 20-40 min after clot formation. The data indicates that early events in coagulation or other pathways that occur in parallel with coagulation induce leukocyte release. The release of elastase, a major fibrinolytic protease of leukocytes, from the cells provides a mechanism Portions of this study were presented at the

show abstract

“…In a few early studies it has been demonstrated that HNE and cathepsin G proteolytically degrade FXIII [10][11][12]. More recently, it was shown that HNE induced a limited cleavage of pFXIII or cFXIII that resulted in their activation, followed by much slower proteolytic inactivation (Fig.…”

Section: Factor Xiii-leukocyte Interactionmentioning

confidence: 98%