Evaluation of the Role of Kinins in Experimental, Pathological, and Clinical Conditions; the Therapeutic Use of Kallikrein Inhibitor

Vogel, Rosmarie; Zickgraf-Rüdel, Gertrud

doi:10.1007/978-3-642-46222-1_27

Cited by 15 publications

(7 citation statements)

References 115 publications

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“…Activation of the kallikrein-kinin system occurs in the posttraumatic phase [11,20,24,29]. Kallikrein is also activated by AMCA through a direct action on the Hageman factor, and plasma kinin has been found to be increased after intravenous administration of AMCA in the dog [ 19], In the present study on rats, however, injection of very large amounts of AMCA was not followed by an increased lung weight.…”

Section: Discussioncontrasting

confidence: 40%

Pulmonary Insufficiency in the Rat after Intravascular Coagulation and Inhibition of Fibrinolysis

Gerdin¹,

Diffang²,

Saldeen³

1981

Eur Surg Res

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Thrombin-induced intravascular coagulation was followed by pulmonary dysfunction in rats treated with the fibrinolysis inhibitor AMCA (trans-4-aminoethyl-cyclohexane carboxylic acid). The pulmonary dysfunction developed after a latency period of about 60 min and led progressively to pulmonary insufficiency with a morphological and functional pattern similar to that in the human delayed microembolism syndrome. Neither activation of the kallikrein-kinin system nor inhibition of converting enzyme activity in the lungs was of major importance in the pathogenesis. Accumulation of fibrin degradation products (FDP) occurred in the lungs and may have played a casual role.

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Section: Discussioncontrasting

confidence: 40%

Pulmonary Insufficiency in the Rat after Intravascular Coagulation and Inhibition of Fibrinolysis

Gerdin¹,

Diffang²,

Saldeen³

1981

Eur Surg Res

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“…Trasylol was included as a comparison in this experiment, since it is known to have anticoagulant properties (Vogel & Zickgraf-Riidel, 1970). It was found to be more effective than the tick inhibitor in prolonging partial-thromboplastin time, but to have no effect on prothrombin times.…”

Section: Discussionmentioning

confidence: 99%

On the biological role of a proteolytic-enzyme inhibitor from the ectoparasitic tick Boophilus microplus

Willadsen¹,

Riding²

1980

Biochemical Journal

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The tick Boophilus microplus contains a protein that inhibits a range of proteolytic enzymes. Variations in the concentration of this protein throughout the life cycle were followed by measuring simultaneously the inhibition of trypsin and chymotrypsin and reaction with an antiserum to the purified inhibitor. The protein is present in large amounts in eggs and in unfed larvae, but its concentration falls very rapidly after the start of the parasitic stage of the life cycle. This, together with previous evidence, suggests that the inhibitor is important both in eggs and in the initial establishment of the parasite on its host. The activity of the protein towards several enzymes has been measured as an indication of its possible function. Bovine trypsin, chymotrypsin and plasmin and pig pancreatic kallikrein are all inhibited. The protein also affects the blood-coagulation system at several points, since it prolongs both activated-partial-thromboplastin time and prothrombin time. It. inhibits the complement-dependent lysis of erythrocytes, but is without significant effect on mitogen-induced lymphocyte stimulation. Thus the inhibitor could have several effects on the host that would be beneficial to the parasite.

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“…Aprotinin (17.5 ;tg/ml) was diluted with solution A with 0.05% gelatin. Other conditions were the same as in (1). (111) The immunoplate was prepared using 1% agarose in solution A with 0.4% (w/v) gelatin.…”

Section: Methodsmentioning

confidence: 99%

“…is used clinically to treat pancreatitis and shock due to acute peri tonitis, as this compound has inhibitory effects on trypsin, chymotrypsin, plasmin and kallikrein (1 ). In the enzyme immunoassay of aprotinin, the recovery of this protease inhibitor from serum was high, and there was an enhancing effect of serum on the antigen antibody precipitation of aprotinin in the gel.…”

Section: Aprotininmentioning

confidence: 99%

The enhancing effect of gelatin on aprotinin activity.

1984

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Abstract-Following preincubation of aprotinin with gelatin, the inhibitory effect on the trypsin activity was enhanced under the same condition as in the case of enhanced antigen-antibody reaction of aprotinin in gel in the presence of gelatin. In the immunochemical titration of aprotinin, gelatin treatment decreased the value of the equivalence point of aprotinin. Immunoprecipitation of aprotinin pre incubated with or without gelatin adjusted to equal activity per unit volume resulted in overlapping equivalence points.These data suggest that the increase in aprotinin activity in the presence of gelatin is due to increase in the active form of aprotinin. Aprotininis used clinically to treat pancreatitis and shock due to acute peri tonitis, as this compound has inhibitory effects on trypsin, chymotrypsin, plasmin and kallikrein (1 ). In the enzyme immunoassay of aprotinin, the recovery of this protease inhibitor from serum was high, and there was an enhancing effect of serum on the antigen antibody precipitation of aprotinin in the gel. The influence of serum on the assay was eliminated by using a gelatin-containing buffer as a sample diluent in the first step of the antigen-antibody reaction, and the antigen-antibody reaction of aprotinin was enhanced in the presence of gelatin. The enhancing effect of serum on the antigen antibody precipitation of aprotinin in the gel was not observed in the presence of gelatin (2). However, the effect of gelatin on apro tinin activity remained to be investigated. In the present study, we looked at the effect of gelatin on the inhibitory activity of aprotinin on trypsin, under the same con dition as in the case of enhanced antigen antibody reaction of aprotinin in gel. Materials and MethodsMaterials: A commercial sample of Trasylol, 10,000 kallikrein inhibitor units (KIU) per ml (Bayer A.G., W. Germany), served as apro tinin. The activity of one KIU corresponds to 0.14 ;cg of crystalline aprotinin. Gelatin and Antibody and IgG fraction of antibody: Antibody to aprotinin was produced in rabbits by injecting an emulsion of Trasylol and adjuvant (3). The IgG fraction of anti aprotinin serum was obtained by fractionation with Na2SO4 (4) followed by passage through a DEAF-cellulose column (5). Double diffusion test: The immuno diffusion plate was prepared using 1 % (w/v) agarose in solution A with or without gelatin. Aprotinin was serially diluted 2-fold with solution A with or without gelatin, and it was reacted with antiaprotinin IgG solution (4 mg/ml) at 4°C for 72 hr. After washout of the unreacted protein with 0.9% (w/v) NaCI solution, the precipitin line was stained with a solution of amido black 10 B.Effect of gelatin on aprotinin activity:Various amounts of aprotinin in solution A with or without gelatin were prepared. The solution was incubated at 4°C for 72 hr or at 37°C for 24 hr, and the aprotinin activity in the solution was measured. Inhibition study: Ninety-six KIU/ml of aprotinin in solution A was reacted with an equal volume of antiaprotinin IgG fraction (0 to 4 mg/...

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Evaluation of the Role of Kinins in Experimental, Pathological, and Clinical Conditions; the Therapeutic Use of Kallikrein Inhibitor

Cited by 15 publications

References 115 publications

Pulmonary Insufficiency in the Rat after Intravascular Coagulation and Inhibition of Fibrinolysis

Pulmonary Insufficiency in the Rat after Intravascular Coagulation and Inhibition of Fibrinolysis

On the biological role of a proteolytic-enzyme inhibitor from the ectoparasitic tick Boophilus microplus

The enhancing effect of gelatin on aprotinin activity.

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