- Tytuł:
- Cloning and expression of a new recombinant thrombolytic and anthithrombotic agent - a staphylokinase variant
- Autorzy:
-
Kowalski, Michał
Brown, George
Bieniasz, Magdalena
Oszajca, Katarzyna
Chabielska, Ewa
Pietras, Tadeusz
Szemraj, Zofia
Makandjou-Ola, Eusebio
Bartkowiak, Jacek
Szemraj, Janusz - Powiązania:
- https://bibliotekanauki.pl/articles/1040615.pdf
- Data publikacji:
- 2009
- Wydawca:
- Polskie Towarzystwo Biochemiczne
- Tematy:
-
K2 domain of t-PA
thrombolytic and antithrombotic agents
thrombolysis
staphylokinase
recombinant protein
hirulog
antiplatelet activity - Opis:
- To develop a more potent antithrombin agent with thrombolytic and antiplatelet properties, a new staphylokinase (SAK) variant was constructed. The kringle 2 domain (K2) of tissue type-plasminogen activator (t-PA) containing a fibrin-specific binding site (i), the RGD sequence (Arg-Gly-Asp) for the prevention of platelet aggregation (ii) and the antithrombotic agent - hirulog (iii) was assembled to the C-terminal part of recombinant staphylokinase (r-SAK). cDNA for the hybrid protein SAK-RGD-K2-Hirul was cloned into Pichia pastoris pPIC9K yeast expression vector. The introduction of K2 t-PA, the RGD sequence and hirulog into the C-terminus of r-SAK did not alter the staphylokinase activity. We observed a higher clot lysis potency of SAK-RGD-K2-Hirul as evidenced by a faster and more profound lysis of 125I-labeled human fibrin clots. The potency of thrombin inhibition by the hirulog C-terminal part of the recombinant fusion protein was almost identical to that of r-Hir alone. These results suggest that the SAK-RGD-K2-Hirul construct can be a more potent and faster-acting thrombolytic agent with better antithrombin and antiplatelet properties compared to r-SAK and SAK-RGD-K2-Hir.
- Źródło:
-
Acta Biochimica Polonica; 2009, 56, 1; 41-53
0001-527X - Pojawia się w:
- Acta Biochimica Polonica
- Dostawca treści:
- Biblioteka Nauki
Artykuł