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Yuling Qiu,Yali Chen,Haiyang Yu,Qianxiang Zhou,Ran Wang,Meihua Jin,Dexin Kong 한국응용곤충학회 2017 Journal of Asia-Pacific Entomology Vol.20 No.2
Bee venom has been used for treating various diseases for a long time. However, the bioactive constituents of bee venom and its mechanisms remain poorly understood. In the present study, phospholipase A2 (Bt-PLA2) cDNA was cloned, and a mature form of Bt-PLA2 was purified from bumblebee venom (Bombus terrestris). The differentiation induction and apoptosis induction activities of Bt-PLA2 on chronic myelogenous leukemia (CML) K562 cells were also evaluated. Bt-PLA2 cDNA has 540 nucleotides that encode a 180-amino-acid protein. The purified, mature form of Bt-PLA2 was an 18-kDa protein, and it inhibited K562 cell growth, determined by an IC50 value of 29.5 ng/μl. Moreover, Bt-PLA2 induced erythroid differentiation of K562 cells in a dose-dependent manner, and this was supplemented with the upregulation of glycophorin A (GPA) mRNA expression. Bt-PLA2- induced apoptosis, analyzed by DAPI staining, was correlated with the result analyzed by AnnexinV-FITC/PI binding. Furthermore, activation of caspase 3 and poly ADP-ribose polymerase (PARP) and inhibition of p-Akt, determined by western blot, further demonstrated that Bt-PLA2 induced apoptosis mainly through the Akt pathway. The parallel induction of erythroblasts differentiation of K562 cells and apoptosis due to Bt-PLA2 treatment demonstrated the potential use of Bt-PLA2 as an anti-leukemia drug lead.
Molecular characterization of a venom serine protease from the bumblebee Bombus terrestris
Yuling Qiu,Young Moo Choo,Mi Ri Sohn,Hyung Joo Yoon,Hung Dae Sohn,Byung Rae Jin 한국응용곤충학회 2010 한국응용곤충학회 학술대회논문집 Vol.2010 No.05
Bee venom contains a variety of peptides and enzymes, including serine proteases. Here we describe the molecular cloning and characterization of a serine protease (Bt-VSP) isolated from the venom of the bumblebee Bombus terrestris. The Bt-VSP gene consists of six exons encoding a 358-amino acid protein. The form of Bt-VSP detected in bee venom was the 34-kDa mature protein, which is created by cleavage of the catalytic domain of Bt-proVSP between Arg111 and Val112. Bt-VSP activates prothrombin and directly degrades fibrinogen into fibrin degradation products, defining roles for Bt-VSP as a prothrombin activator, a thrombin-like protease, and a plasmin-like protease. The finding that Bt-VSP acts as a fibrin(ogen)olytic enzyme is similar to a previous finding that Bi-VSP, a venom serine protease of B. ignitus, exhibits fibrin(ogen)olytic activity. We also compared major venom components in honeybee and bumblebee, and found that bumblebee venom contains a larger amount of serine protease. Furthermore, unlike bumblebee venom, which exhibits fibrin(ogen)olytic activity owing to the presence of a serine protease, it is likely that honeybee venom lacks fibrin(ogen)olytic activity.
Yuling Qiu,Hyung Joo Yoon,Byung Rae Jin 한국응용곤충학회 2011 한국응용곤충학회 학술대회논문집 Vol.2011 No.10
We cloned venom serine proteases from two bumblebee species, Bombus hypocrita sapporoensis and B. ardens ardens. We compared the predicted mature protein sequences of these serine proteasegenes to those previously reported from other bees. Using B. h. sapporoensis venom serine protease(Bs-VSP), we identify that Bs-VSP acts as a fibrin(ogen)olytic enzyme. Bs-VSP activates prothrombin and directly degrades fibrinogen into fibrin degradation products, as demonstrated for B. ignitus and B. terrestrisvenom serine proteases. Our results further define roles for bumblebee venom serine proteases as fibrin(ogen)olytic enzyme, providing strong evidence that bumblebee venom serine proteases are hemostatically active proteins that are potentially promising therapeutic agents.
Qiu, Yuling,Yoon, Hyung-Joo,Jin, Byung-Rae Korean Society of Sericultural Science 2012 International Journal of Industrial Entomology Vol.25 No.1
The bumblebee Bombus terrestris is widely used in greenhouses to pollinate crops. Here, we report the molecular cloning and characterization of chymotrypsin inhibitor and chitin-binding protein homologs from B. terrestris. Two cDNAs encoding chymotrypsin inhibitor (Bt-CI) and chitin-binding protein (Bt-CBP) homologs were cloned from B. terrestris. Gene sequence analysis showed that Bt-CI gene consists of three exons encoding 75 amino acids, including a predicted 20-amino acid signal peptide, while Bt-CBP consists of two exons encoding 78 amino acids, including a predicted 26-amino acid signal peptide. The mature Bt-CI and Bt-CBP peptides contain ten and six conserved cysteine residues, respectively. Database searches using the deduced sequences of Bt-CI and Bt-CBP showed similarity to those from B. impatiens (96% peptide sequence identities). Bt-CI and Bt-CBP were expressed in both the venom gland and fat body of B. terrestris worker bees. The recombinant Bt-CI and Bt-CBP peptides were expressed in baculovirus-infected insect cells. Taken together, our findings describe the molecular characterization of Bt-CI and Bt-CBP from B. terrestris.
Molecular characterization of bee venom serine proteases
Yuling Qiu,Hyung Joo Yoon,Byung Rae Jin 한국응용곤충학회 2011 한국응용곤충학회 학술대회논문집 Vol.2011 No.10
We present evidence that the serine protease found in bumblebee (Bombus terrestris) venom exhibits fibrin(ogen)olytic activity. Compared to honeybee (Apis mellifera) 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 B. 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, providing significant support for thepotential use of bumblebee venom serine protease as a clinical agent.
Fibrin(ogen)olytic Activity of Bee Venom Serine Protease
Yuling Qiu,Young Moo Choo,Hyung Joo Yoon,Byung Rae Jin 한국응용곤충학회 2011 한국응용곤충학회 학술대회논문집 Vol.2011 No.05
Bee venom contains a variety of protein allergens, including serine proteases. Additionally, bee venom has been used in therapeutic application through immunotherapy for bee venom hypersensitivity and venom therapy as an alternative medicine. Here we present a novel view of the application of bee venom through which bee venom serine protease exhibits fibrin(ogen)olytic activity. Compared to honeybee venom, bumblebee venom contains a larger amount of a serine protease as one of its major components. Immunologically, venom serine proteases from bumblebees did not show cross-reactivity with 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, defining roles for Bt-VSP as a prothrombin activator, a thrombin-like protease, and a plasmin-like protease. However, Bt-VSP did not activate plasminogen and the fibrinolytic activity of Bt-VSP is less than plasmin. These findings offer insight into the allergic reaction sequence of bee venom serine protease and its potential usefulness as a clinical agent in the field of hemostasis and thrombosis.
Antifibrinolytic Role of a Bumbleee (Bombus terrestris) Venom Serine Protease Inhibitor
Yuling Qiu,Kwang Sik Lee,Hyung Joo Yoon,Byung Rae Jin 한국응용곤충학회 2012 한국응용곤충학회 학술대회논문집 Vol.2012 No.05
Bee venom is a rich source of pharmacologically active substances. In this study, we characterized a B. terrestris venom Kunitz-type serine protease inhibitor (Bt-KTI). Bt-KTI consists of two exons encoding 82-amino acids (aa), including a predicted 24-aa signal peptide and a 58-aa mature peptide. Recombinant Bt-KTI was expressed as a 6.5-kDa peptide in baculovirus-infected insect cells. Bt-KTI showed no detectable inhibitory effect on factor Xa, thrombin, or tissue plasminogen activator. In contrast, Bt-KTI strongly inhibited plasmin, indicating that it acts as a plasmin inhibitor. The electrophoretic mobility shift assay showed that Bt-KTI binds to plasmin, indicating the formation of a plasmin-Bt-KTI complex. These results demonstrate that Bt-KTI acts as an antifibrinolytic agent, suggesting a role for Bt-KTI as an anti-bleeding agent.
Yuling Qiu,Young Moo Choo,윤형주,진병래 한국응용곤충학회 2012 Journal of Asia-Pacific Entomology Vol.15 No.1
Three major components of bumblebee venom are bombolitin, phospholipase A2, and a serine protease, with bombolitin being the most abundant. Here, we describe the molecular cloning of bombolitin isolated from the venom of a bumblebee, Bombus terrestris, and demonstrate its antibacterial activity. The B. terrestris bombolitin gene consists of 2 exons encoding 56 amino acid residues. Comparative analysis shows that mature B. terrestris bombolitin consists of 18 amino acid residues, which are identical to those of B. ignitus bombolitin. B. terrestris bombolitin displayed antibacterial activity against both the Gram-negative bacterium Klebsiella pneumoniae and the Gram-positive bacterium Staphylococcus aureus, indicating that B. terrestris bombolitin may be a potential antimicrobial agent.
Yuling Qiu,Young Moo Choo,윤형주,진병래 한국응용곤충학회 2012 Journal of Asia-Pacific Entomology Vol.15 No.1
Although several bee venom serine protease genes have been previously described, fibrin(ogen)olytic activity of these serine proteases has been reported for only two bumblebees to date, Bombus ignitus and B. terrestris. Here, we cloned venom serine proteases from the other bumblebee species, B. hypocrita sapporoensis and B. ardens ardens. The venom serine protease genes of B. h. sapporoensis and B. a. ardens consist of 358 amino acids and 357 amino acids, respectively. We compared the predicted mature protein sequences of these serine protease genes to those previously reported for other bees. A phylogenetic analysis shows that B. h. sapporoensis venom serine protease is further immediately close to B. ignitus and B. terrestris venom serine proteases, excluding the venom serine protease of B. a. ardens. Using B. h. sapporoensis venom serine protease (Bs-VSP), we identified that Bs-VSP acts as a fibrin(ogen)olytic enzyme. We also found that Bs-VSP activates prothrombin and directly degrades fibrinogen into fibrin degradation products. Our results further define roles for bumblebee venom serine proteases as fibrin(ogen)olytic agents.