MINI PLASMINOGEN-LIKE MOLECULE IN SEPTIC PATIENTS

We have previously described (Thromb.Res.44(6),1986) an altered relation Plasminogen (Pig)/α₂~antiplasmin (APL) (Plg/APL<0.6) in the plasma of septic patients. A probable explanation of the mechanism whereby this alteration takes place would be the degradation of Pig to fragments of lower molecular weight due to the action of leukocyte elastase.In order to confirm this we studied 10 patients with sepsis, which did not have clinicalorlaboratory evidence of disseminated intravascular coagulation or septic shock, with positive blood cultures for bacterial germs .Elastase-α₁proteinase inhibitor complexes were measured by an enzyme-linked immunosorbent assay (mean:510±181.9ug/l;normal range:86±28.5ug/l). Pig and APL functional activities were assayed by the amidolytic method; Pig: 40±8.9%; normal range: 100±20% .APL: 95±10.1% formal range 100+20%. Two different behaviors were observed in the plasma Pig of these patients with regard to their capacity to bind to Lysi-ne-Sepharose 4B.0n the basis of this observation the patients were divided into two group.Group A(4 patients) only presented Pig activity in fraction 1 (Pig without lysine binding sites : LBS). Group B (6 patients) presented Pig activity in fraction 1 and in fraction 2 (Pig with LBS).The normal controls presented Pig activity only in fraction 2. All the fractions which presented functional Pig activity also presented immunologic Pig activity and developed areas of lysis in heated fibrin plates after activation with urokinase

It seems tenable the hypothesis that the action of the leukocyte elastase is responsible for the degradation of Pig and this modification in the molecule would give rise to a greater depuration thus explaining the marked drop of the plasmatic levels seen in septic patients.