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      Molecular cloning and antifibrinolytic activity of a serine protease inhibitor from bumblebee (Bombus terrestris) venom.

      Toxicon

      Amino Acid Sequence, Animals, Antifibrinolytic Agents, chemistry, pharmacology, Baculoviridae, genetics, Base Sequence, Bee Venoms, metabolism, Bees, physiology, Cloning, Molecular, Drug Combinations, Electrophoretic Mobility Shift Assay, methods, Fibrinolysin, antagonists & inhibitors, Gene Expression, Insect Proteins, Insects, Molecular Sequence Data, Recombinant Proteins, Sequence Alignment, Serine Proteinase Inhibitors, Thrombin, drug effects

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          Abstract

          Bumblebee (Bombus spp.) venom contains a variety of components, including bombolitin, phospholipase A(2) (PLA(2)), serine proteases, and serine protease inhibitors. In this study, we identified a bumblebee (Bombus terrestris) venom serine protease inhibitor (Bt-KTI) that acts as a plasmin inhibitor. Bt-KTI consists of a 58-amino acid mature peptide that displays features consistent with snake venom Kunitz-type inhibitors, including six conserved cysteine residues and a P1 site. Recombinant Bt-KTI was expressed as a 6.5-kDa peptide in baculovirus-infected insect cells. The recombinant peptide demonstrated properties similar to Kunitz-type trypsin inhibitors. Bt-KTI showed no detectable inhibitory effects on factor Xa, thrombin, or tissue plasminogen activator; however, Bt-KTI strongly inhibited plasmin, indicating that it acts as an antifibrinolytic agent. These findings demonstrate the antifibrinolytic role of Bt-KTI as a plasmin inhibitor. Copyright © 2012 Elsevier Ltd. All rights reserved.

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          23164714
          10.1016/j.toxicon.2012.11.004

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