Clinical Chemistry
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Clinical Chemistry 35: 69-73, 1989;
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Clinical Chemistry, Vol 35, 69-73, Copyright © 1989 by American Association for Clinical Chemistry

Streptokinase binds to lactate dehydrogenase subunit-M, which shares an epitope with plasminogen

SJ Podlasek and RA McPherson
Department of Laboratory Medicine, Georgetown University Hospital, Washington, DC 20007.

The bacterial thrombolytic agent streptokinase binds to human, porcine, and chicken lactate dehydrogenase (EC 1.1.1.27; LD) isoenzyme subunit M, but not to the H or C subunits. There is amino acid sequence homology between LD and the streptokinase binding site on plasminogen to account for this interaction that results in the formation of high- molecular-mass complexes in serum that contain LD activity. Binding of highly immunogenic streptokinase with LD may lead to induction of anti- LD autoantibodies, known to occur in some patients after therapeutic administration of streptokinase for treatment of acute myocardial infarction. This interaction may also be a general mechanism for inducing autoimmunity against other proteins that share the streptokinase binding epitope.




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Copyright © 1989 by the American Association for Clinical Chemistry.