The saliva of the vampire bat Desmodus rotundus contains a family of p
otent plasminogen activators, which were named DSPAs after their origi
nal source (Desmodus salivary plasminogen activators), The DSPAs share
a high structural homology with t-PA, Four different variants of DSPA
have been discovered, called DSPA alpha(1), alpha(2), beta and gamma,
out of which, for its unique thrombolytic properties, DSPA alpha(1) h
as been selected for further development, It has a high potential to d
evelop into a third generation thrombolytic drug. DSPA alpha(1) is a p
rotein with high thrombolytic potency and efficacy, Unlike all other p
lasminogen activators currently in use, it is almost completely fibrin
specific, Furthermore, its prolonged half-life seems to warrant singl
e bolus administration, Above all, recanalization with DSPA alpha(1) s
eems to occur more rapidly and more completely and, unlike with other
plasminogen activators, is sustained over prolonged time periods, Desp
ite being a non human protein its antigenicity is low and only repeate
d administrations of the substance in short time intervals may non con
sistently produce low titers of nan neutralizing antibodies, The favor
able thrombolytic profile of DSPA alpha(1) warrants studying in future
thrombolytic trials.