Allergic reactions to streptokinase consistent with anaphylactic or antigen-antibody complex-mediated damage

McGrath, Kris G.; Zeffren, Barry; Alexander, Jay; Kaplan, Kerry; Patterson, Roy

doi:10.1016/0091-6749(85)90726-2

Cited by 64 publications

(21 citation statements)

References 12 publications

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“…For instance, both deplete plasminogen within the thrombus, converting circulating plasminogen to plasmin [31]. Streptokinase is also immunogenic such that its use results in drug resistance, fever, and allergic reactions [20]. Second-generation agents such as t-PA and scu-PA are fibrin specific; however, they not only decrease the levels of circulating fibrinogen and plasminogen but also increase the risk of intracranial hemorrhage [19,28].…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of a fibrinolytic subtilisin-like protease of Bacillus subtilis TP-6 from an Indonesian fermented soybean, Tempeh

Kim

Lee

Cheigh

et al. 2006

J IND MICROBIOL BIOTECHNOL

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We have isolated a bacterium (TP-6) from the Indonesian fermented soybean, Tempeh, which produces a strong fibrinolytic protease and was identified as Bacillus subtilis. The protease (TPase) was purified to homogeneity by ammonium sulfate fractionation and octyl sepharose and SP sepharose chromatography. The N-terminal amino acid sequence of the 27.5 kDa enzyme was determined, and the encoding gene was cloned and sequenced. The result demonstrates that TPase is a serine protease of the subtilisin family consisting of 275 amino acid residues in its mature form. Its apparent K (m) and V (max) for the synthetic substrate N-succinyl-Ala-Ala-Pro-Phe-pNA were 259 microM and 145 micromol mg(-1) min(-1), respectively. The fibrinogen degradation pattern generated by TPase as a function of time was similar to that obtained with plasmin. In addition, N-terminal amino acid sequence analysis of the fibrinogen degradation products demonstrated that TPase cleaves Glu (or Asp) near hydrophobic acids as a P1 site in the alpha- and beta-chains of fibrinogen to generate fragments D', E', and D' similar to those generated by plasmin. On plasminogen-rich fibrin plates, TPase did not seem to activate fibrin clot lysis. Moreover, the enzyme converted the active plasminogen activator inhibitor-1 to the latent form.

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Section: Introductionmentioning

confidence: 99%

Purification and characterization of a fibrinolytic subtilisin-like protease of Bacillus subtilis TP-6 from an Indonesian fermented soybean, Tempeh

Kim

Lee

Cheigh

et al. 2006

J IND MICROBIOL BIOTECHNOL

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“…In most cases these symptoms develop 20 to 30 min after initiation of the streptokinase infusion [9]. However, McGrath et al [10] reported an allergic reaction to streptokinase 4 h after the first dose of streptokinase was finished and during the second one. In our patient the reaction was observed 3 h and 20 min after the start of the first dose and during the second infusion.…”

Section: Discussionmentioning

confidence: 99%

Adverse reaction to streptokinase with multiple systemic manifestations

et al. 1995

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We report the case of a 47-year-old woman with a history of mitral valve replacement with a mechanical prosthesis who was admitted to the hospital with a 3-month history of progressive exertional dyspnoea and was diagnosed as suffering from prosthetic valve thrombosis. Two consecutive courses of streptokinase were given as an intravenous infusion over 90 min at a dose of 1,500,000 IU each. Twenty minutes after the start of the second infusion (3 h and 20 min after the first one) she developed chills, fever, tachycardia and hypotension: symptomatic treatment was given and the infusion was completed. Two days later jaundice and choluria appeared with laboratory findings of hepatic cytolysis and cholestasis and renal insufficiency. The results of extensive microbiological and immunological investigations were not revealing. All the laboratory values spontaneously returned to baseline levels over the next 4 weeks. These abnormalities were attributed to an allergic reaction to streptokinase, although the exact pathogenic mechanisms involved are not known. We believe that further studies to elucidate the mechanism involved in the production of these effects are warranted in view of their potential clinical severity.

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“…This therapy generates signi®-cant T-cell responses to SK (Bruserud et al, 1986(Bruserud et al, , 1992Bruserud, 1990;Youkeles et al, 1991) and causes Ab titers and the neutralizing capacity of the Ab to rise signi®cantly (Lynch et al, 1991(Lynch et al, , 1994Elliot et al, 1993;Lee et al, 1993;Patel et al, 1993;Parhami-Seren et al, 1995). The neutralizing Abs reduce the ef®ciency of thrombolytic therapy (Massel et al, 1991) and may cause allergic reactions ranging from fever to immune complex disease to anaphylactic shock (Davis et al, 1990;McGrath & Patterson, 1984;McGrath et al, 1985;Schweitzer et al, 1991).…”

Section: Introductionmentioning

confidence: 95%

Sequences of antigenic epitopes of streptokinase identified via random peptide libraries displayed on phage 1 1Edited by J. A. Wells

Parhami-Seren

Keel

Reed

1997

Journal of Molecular Biology

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Allergic reactions to streptokinase consistent with anaphylactic or antigen-antibody complex-mediated damage

Cited by 64 publications

References 12 publications

Purification and characterization of a fibrinolytic subtilisin-like protease of Bacillus subtilis TP-6 from an Indonesian fermented soybean, Tempeh

Purification and characterization of a fibrinolytic subtilisin-like protease of Bacillus subtilis TP-6 from an Indonesian fermented soybean, Tempeh

Adverse reaction to streptokinase with multiple systemic manifestations

Sequences of antigenic epitopes of streptokinase identified via random peptide libraries displayed on phage 1 1Edited by J. A. Wells

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