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Title: Fibrin(ogen)olytic activity of bumblebee venom serine protease

Abstract

Bee venom is a rich source of pharmacologically active components; it has been used as an immunotherapy to treat bee venom hypersensitivity, and venom therapy has been applied as an alternative medicine. Here, we present evidence that the serine protease found in bumblebee venom exhibits fibrin(ogen)olytic activity. Compared to honeybee venom, bumblebee venom contains a higher content of serine protease, which is one of its major components. Venom serine proteases from bumblebees did not cross-react with antibodies against the honeybee venom serine protease. We provide functional evidence indicating that bumblebee (Bombus terrestris) venom serine protease (Bt-VSP) acts as a fibrin(ogen)olytic enzyme. Bt-VSP activates prothrombin and directly degrades fibrinogen into fibrin degradation products. However, Bt-VSP is not a plasminogen activator, and its fibrinolytic activity is less than that of plasmin. Taken together, our results define roles for Bt-VSP as a prothrombin activator, a thrombin-like protease, and a plasmin-like protease. These findings offer significant insight into the allergic reaction sequence that is initiated by bee venom serine protease and its potential usefulness as a clinical agent in the field of hemostasis and thrombosis. - Graphical abstract: Display Omitted Highlights: > Bumblebee venom serine protease (Bt-VSP) is a fibrin(ogen)olytic enzyme. > Bt-VSP activatesmore » prothrombin. > Bt-VSP directly degrades fibrinogen into fibrin degradation products. > Bt-VSP is a hemostatically active protein that is a potent clinical agent.« less

Authors:
 [1];  [2];  [1];  [3]; ; ;  [4];  [1];  [2];  [1];  [1];  [2]
  1. College of Natural Resources and Life Science, Dong-A University, Busan 604-714 (Korea, Republic of)
  2. (China)
  3. Department of Agricultural Biology, National Academy of Agricultural Science, Suwon (Korea, Republic of)
  4. Joint Laboratory between Dong-A University and Shenyang Pharmaceutical University, Shenyang Pharmaceutical University, Shenyang (China)
Publication Date:
OSTI Identifier:
21587832
Resource Type:
Journal Article
Resource Relation:
Journal Name: Toxicology and Applied Pharmacology; Journal Volume: 255; Journal Issue: 2; Other Information: DOI: 10.1016/j.taap.2011.06.020; PII: S0041-008X(11)00244-4; Copyright (c) 2011 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ALLERGY; ANTIBODIES; BEES; FIBRINOGEN; PLASMINOGEN; SERINE; THROMBIN; TOXICITY; VENOMS; AMINO ACIDS; ANIMALS; ARTHROPODS; BLOOD COAGULATION FACTORS; CARBOXYLIC ACIDS; DRUGS; ENZYMES; FIBRINOLYTIC AGENTS; GLOBULINS; HEMATOLOGIC AGENTS; HYDROLASES; HYDROXY ACIDS; HYMENOPTERA; INSECTS; INVERTEBRATES; ORGANIC ACIDS; ORGANIC COMPOUNDS; PATHOLOGICAL CHANGES; PEPTIDE HYDROLASES; PROTEINS; SERINE PROTEINASES

Citation Formats

Qiu Yuling, Joint Laboratory between Dong-A University and Shenyang Pharmaceutical University, Shenyang Pharmaceutical University, Shenyang, Choo, Young Moo, Yoon, Hyung Joo, Jia Jingming, Cui Zheng, Wang Dong, Kim, Doh Hoon, Joint Laboratory between Dong-A University and Shenyang Pharmaceutical University, Shenyang Pharmaceutical University, Shenyang, Sohn, Hung Dae, Jin, Byung Rae, E-mail: brjin@dau.ac.kr, and Joint Laboratory between Dong-A University and Shenyang Pharmaceutical University, Shenyang Pharmaceutical University, Shenyang. Fibrin(ogen)olytic activity of bumblebee venom serine protease. United States: N. p., 2011. Web.
Qiu Yuling, Joint Laboratory between Dong-A University and Shenyang Pharmaceutical University, Shenyang Pharmaceutical University, Shenyang, Choo, Young Moo, Yoon, Hyung Joo, Jia Jingming, Cui Zheng, Wang Dong, Kim, Doh Hoon, Joint Laboratory between Dong-A University and Shenyang Pharmaceutical University, Shenyang Pharmaceutical University, Shenyang, Sohn, Hung Dae, Jin, Byung Rae, E-mail: brjin@dau.ac.kr, & Joint Laboratory between Dong-A University and Shenyang Pharmaceutical University, Shenyang Pharmaceutical University, Shenyang. Fibrin(ogen)olytic activity of bumblebee venom serine protease. United States.
Qiu Yuling, Joint Laboratory between Dong-A University and Shenyang Pharmaceutical University, Shenyang Pharmaceutical University, Shenyang, Choo, Young Moo, Yoon, Hyung Joo, Jia Jingming, Cui Zheng, Wang Dong, Kim, Doh Hoon, Joint Laboratory between Dong-A University and Shenyang Pharmaceutical University, Shenyang Pharmaceutical University, Shenyang, Sohn, Hung Dae, Jin, Byung Rae, E-mail: brjin@dau.ac.kr, and Joint Laboratory between Dong-A University and Shenyang Pharmaceutical University, Shenyang Pharmaceutical University, Shenyang. Thu . "Fibrin(ogen)olytic activity of bumblebee venom serine protease". United States.
@article{osti_21587832,
title = {Fibrin(ogen)olytic activity of bumblebee venom serine protease},
author = {Qiu Yuling and Joint Laboratory between Dong-A University and Shenyang Pharmaceutical University, Shenyang Pharmaceutical University, Shenyang and Choo, Young Moo and Yoon, Hyung Joo and Jia Jingming and Cui Zheng and Wang Dong and Kim, Doh Hoon and Joint Laboratory between Dong-A University and Shenyang Pharmaceutical University, Shenyang Pharmaceutical University, Shenyang and Sohn, Hung Dae and Jin, Byung Rae, E-mail: brjin@dau.ac.kr and Joint Laboratory between Dong-A University and Shenyang Pharmaceutical University, Shenyang Pharmaceutical University, Shenyang},
abstractNote = {Bee venom is a rich source of pharmacologically active components; it has been used as an immunotherapy to treat bee venom hypersensitivity, and venom therapy has been applied as an alternative medicine. Here, we present evidence that the serine protease found in bumblebee venom exhibits fibrin(ogen)olytic activity. Compared to honeybee venom, bumblebee venom contains a higher content of serine protease, which is one of its major components. Venom serine proteases from bumblebees did not cross-react with antibodies against the honeybee venom serine protease. We provide functional evidence indicating that bumblebee (Bombus terrestris) venom serine protease (Bt-VSP) acts as a fibrin(ogen)olytic enzyme. Bt-VSP activates prothrombin and directly degrades fibrinogen into fibrin degradation products. However, Bt-VSP is not a plasminogen activator, and its fibrinolytic activity is less than that of plasmin. Taken together, our results define roles for Bt-VSP as a prothrombin activator, a thrombin-like protease, and a plasmin-like protease. These findings offer significant insight into the allergic reaction sequence that is initiated by bee venom serine protease and its potential usefulness as a clinical agent in the field of hemostasis and thrombosis. - Graphical abstract: Display Omitted Highlights: > Bumblebee venom serine protease (Bt-VSP) is a fibrin(ogen)olytic enzyme. > Bt-VSP activates prothrombin. > Bt-VSP directly degrades fibrinogen into fibrin degradation products. > Bt-VSP is a hemostatically active protein that is a potent clinical agent.},
doi = {},
journal = {Toxicology and Applied Pharmacology},
number = 2,
volume = 255,
place = {United States},
year = {Thu Sep 01 00:00:00 EDT 2011},
month = {Thu Sep 01 00:00:00 EDT 2011}
}