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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.
Marein Prevented LPS-Induced Osteoclastogenesis by Regulating the NF-κB Pathway In Vitro
( Yuling Li ),( Jing Zhang ),( Caiping Yan ),( Qian Chen ),( Chao Xiang ),( Qingyan Zhang ),( Xingkuan Wang ),( Ke Jiang ) 한국미생물생명공학회 2022 Journal of microbiology and biotechnology Vol.32 No.2
Many bone diseases such as osteolysis, osteomyelitis, and septic arthritis are caused by gramnegative bacterial infection, and lipopolysaccharide (LPS), a bacterial product, plays an essential role in this process. Drugs that inhibit LPS-induced osteoclastogenesis are urgently needed to prevent bone destruction in infective bone diseases. Marein, a major bioactive compound of Coreopsis tinctoria, possesses anti-oxidative, anti-inflammatory, anti-hypertensive, antihyperlipidemic, and anti-diabetic effects. In this study, we measured the effect of marein on RAW264.7 cells by CCK-8 assay and used TRAP staining to determine osteoclastogenesis. The levels of osteoclast-related genes and NF-κB-related proteins were then analyzed by western blot, and the levels of pro-inflammatory cytokines were quantified by ELISA. Our results showed that marein inhibited LPS-induced osteoclast formation by osteoclast precursor RAW264.7 cells. The effect of marein was related to its inhibitory function on expressions of pro-inflammatory cytokines and osteoclast-related genes containing RANK, TRAF6, MMP-9, CK, and CAII. Additionally, marein leads to markedly inhibited NF-κB signaling pathway activation in LPS-induced RAW264.7 cells. Concurrently, when the NF-κB signaling pathway was inhibited, osteoclast formation and proinflammatory cytokine expression were decreased. Collectively, marein could inhibit LPS-induced osteoclast formation in RAW264.7 cells via regulating the NF-κB signaling pathway. Our data demonstrate that marein might be a potential drug for bacteria-induced bone destruction disease. Our findings provide new insights into LPS-induced bone disease.
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.
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 Ding,Chanipa Jiratchayamaethasakul,Eun-A Kim,Junseong Kim,Soo-Jin Heo,Seung-Hong Lee 한국해양바이오학회 2018 한국해양바이오학회지 Vol.10 No.2
An active ingredient with hyaluronidase (HAse) inhibitory effect is one of the anti-aging approaches in cosmeceuticals. Here, red sea cucumbers (RSCs), Stichopus japonicus, from Jeju Island were evaluated to examine their HAse inhibitory and antioxidant activity effect. In this study, RSCs were extracted by six enzymatic hydrolysis (Alcalase; Al, Trypsin; Try, Neutrase; Neu, Pepsin; Pep, Alpha-chymotrypsin; Chy and Protamex; Pro). Alcalase hydrolysate (AlH) showed the highest antioxidant capacities for both of oxygen radical absorbance capacity (ORAC) and trolox equivalent antioxidant capacity (TEAC) methods, compared to those of other hydrolysates, at 66.59±0.78 μM TE/mg and 135.78±3.24 μM TE/㎎, respectively. Furthermore, AlH performed the highest capacity of HAse inhibitory with IC<SUB>50</SUB> value of 3.21 ㎎/ml. Thus, RSCs hydrolyzed by Al were chosen to determine the cellular antioxidant activity and hyaluronic acid (HA) production effect on Human immortalized keratinocyte cell line (HaCaT). The results showed that AlH improved the cell viabilities and intracellular reactive oxygen species (ROS) induced by 2,2’-Azobis(2-amidinopropane) dihydrochloride (AAPH) were significantly decreased. In addition, AlH increased HA amount by regulating HYAL2 and HAS2 expressions in the HaCaT cells. Taken together, AlH of RSCs collected from Jeju Island showed HAse inhibitory and antioxidant activities against skin-aging which shows its potentials can be an optional natural bioactive ingredient for novel cosmeceuticals.
An Improved Coverless Text Steganography Algorithm Based on Pretreatment and POS
( Yuling Liu ),( Jiao Wu ),( Xianyi Chen ) 한국인터넷정보학회 2021 KSII Transactions on Internet and Information Syst Vol.15 No.4
Steganography is a current hot research topic in the area of information security and privacy protection. However, most previous steganography methods are not effective against steganalysis and attacks because they are usually carried out by modifying covers. In this paper, we propose an improved coverless text steganography algorithm based on pretreatment and Part of Speech (POS), in which, Chinese character components are used as the locating marks, then the POS is used to hide the number of keywords, the retrieval of stego-texts is optimized by pretreatment finally. The experiment is verified that our algorithm performs well in terms of embedding capacity, the embedding success rate, and extracting accuracy, with appropriate lengths of locating marks and the large scale of the text database.