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Longistatin, a novel plasminogen activator from vector ticks, is resistant to plasminogen activator inhibitor-1.

Abstract：

:Thrombo-occlusive diseases are major causes of morbidity and mortality, and tissue-type plasminogen activator (t-PA) is recommended for the treatment of the maladies. However, both t-PA and u-PA are rapidly inactivated by plasminogen activator inhibitor-1 (PAI-1). Here, we show that longistatin, a novel plasminogen activator isolated from the ixodid tick, Haemaphysalis longicornis is resistant to PAI-1. Longistatin was relatively less susceptible to the inhibitory effect of SDS-treated platelet lysate than physiologic PAs. Platelet lysate inhibited t-PA and tcu-PA with the IC(50) of 7.7 and 9.1 μg/ml, respectively, whereas for longistatin inhibition IC(50) was 20.1 μg/ml (p<0.01). Similarly, activated PAI-1 (20 nM) inhibited only 21.47% activity of longistatin but almost completely inhibited t-PA (99.17%) and tcu-PA (96.84%). Interestingly, longistatin retained 76.73% initial activity even after 3h of incubation with 20 nM of PAI-1. IC(50) of PAI-1 during longistatin inhibition was 88.3 nM while it was 3.9 and 3.2 nM in t-PA and tcu-PA inhibition, respectively. Longistatin completely hydrolyzed fibrin clot by activating plasminogen efficiently in the presence of 20 nM of PAI-1. Importantly, unlike t-PA, longistatin did not form complex with PAI-1. Collectively, our results suggest that longistatin is resistant to PAI-1 and maybe an interesting tool for the development of a PAI-1 resistant effective thrombolytic agent.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Anisuzzaman,Khyrul Islam M,Abdul Alim M,Miyoshi T,Hatta T,Yamaji K,Matsumoto Y,Fujisaki K,Tsuji N

doi

10.1016/j.bbrc.2011.09.009

subject

Has Abstract

pub_date

2011-10-07 00:00:00

pages

599-604

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(11)01580-4

journal_volume

413

pub_type

杂志文章

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