Document Detail

Alteration of the fibrinogen molecule and its phosphorylation state in myocardial infarction patients undergoing thrombolytic treatment.
MedLine Citation:
PMID:  10713316     Owner:  NLM     Status:  MEDLINE    
Fibrinogen was purified by protamine-agarose chromatography from plasma from three patients after their submission to hospital due to acute myocardial infarction. The total amount of phosphate bound to fibrinogen and the concentration of fibrinogen was determined in samples withdrawn immediately after submission and after thrombolytic treatment. Streptokinase treatment almost totally removed circulating fibrinogen while recombinant tissue plasminogen activator spared much of it. In patients treated with streptokinase, the new circulating fibrinogen was homogeneous according to the single alpha-band seen after sodium dodecyl sulphate polyacrylamide gel electrophoresis analysis under reducing conditions, whereas fibrinogen from the recombinant tissue plasminogen activator-treated patient as well as healthy controls exhibited two alpha-bands in the 66-kDa region. The molar ratios of phosphate to fibrinogen of healthy controls and commercial fibrinogen were 0.82 (+/-0.04) and 0. 87 (+/-0.05), respectively. For two streptokinase-treated patients the degree of phosphorylation increased threefold from a normal range of 0.97 (+/-0.11) and 0.67 (+/-0.09) mol/mol fibrinogen before treatment to 3.33 (+/-0.32) and 1.86 (+/-0.17) mol/mol in newly formed fibrinogen on day 1. Recombinant tissue plasminogen activator treatment led to a smaller increase in phosphorylation, from 1.14 (+/-0.13) pretreatment to 1.65 (+/-0.11) after treatment on day 1. In conclusion we show in this report that after streptokinase treatment of patients with acute myocardial infarction, the new Aalpha-chain of fibrinogen was a homogeneous single 66-kDa band on sodium dodecyl sulphate polyacrylamide gel electrophoresis under reducing conditions and that the degree of phosphorylation of plasma fibrinogen was elevated, approaching the theoretical limit of 4 mol phosphate/mol fibrinogen.
A C Haglund; G Ronquist; G Frithz; P Ek
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Thrombosis research     Volume:  98     ISSN:  0049-3848     ISO Abbreviation:  Thromb. Res.     Publication Date:  2000 Apr 
Date Detail:
Created Date:  2000-05-08     Completed Date:  2000-05-08     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0326377     Medline TA:  Thromb Res     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  147-56     Citation Subset:  IM    
Department of Medical Biochemistry and Microbiology, Biomedical Centre, University of Uppsala, University Hospital, Uppsala, Sweden.
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MeSH Terms
Case-Control Studies
Fibrinogen / chemistry*,  isolation & purification,  metabolism*
Middle Aged
Molecular Weight
Myocardial Infarction / blood*,  drug therapy*
Recombinant Proteins / therapeutic use
Streptokinase / therapeutic use
Thrombolytic Therapy*
Tissue Plasminogen Activator / therapeutic use
Reg. No./Substance:
0/Recombinant Proteins; 9001-32-5/Fibrinogen; EC 3.4.-/Streptokinase; EC Plasminogen Activator

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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