• Title/Summary/Keyword: plasmin

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Effect of Fibroblast Growth Factor-2 on Migration and Proteinases Secretion of Human Umbilical Vein Endothelial Cells

  • Oh, In-Suk;Kim, Hwan-Gyu
    • Journal of Microbiology and Biotechnology
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    • v.14 no.2
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    • pp.379-384
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    • 2004
  • Fibroblast growth factor-2 (FGF-2) is known to modulate numerous cellular functions in various cell types, including cell proliferation, differentiation, survival, adhesion, migration, and motility, and also in processes such as wound healing, angiogenesis, and vasculogenesis. FGF-2 regulates the expression of several molecules thought to mediate critical steps during angiogenesis. This study examines the mechanisms underlying FGF-2-induced cell migration, using human umbilical vein endothelial cells (HUVECs). FGF-2 induced the nondirectional and directional migration of endothelial cells, which are inhibited by MMPs and plasmin inhibitors, and induced the secretion of matrix metalloproteinase-3 (MMP3) and MMP-9, but not MMP-l and MMP-2. FGF-2 also induced the secretion of the tissue inhibitor of metalloproteinase-l (TIMP-I), but not of TIMP- 2. Also, the pan-PKC inhibitor inhibited FGF-2-induced MMP-9 secretion. It is, therefore, suggested that FGF-2 induces the migration of cultured endothelial cells by means of increased MMPs and plasmin secretion. Furthermore, FGF-2 may increase MMP-9 secretion by activating the PKC pathway.

Studies on the Fibrinolytic Effect of Germinated Grain Seeds

  • Kwon, Su-Jung;Lee, Jang-Won;Park, Min-Hee;Kim, Sun-Min;Cha, Young-Ju
    • Proceedings of the Plant Resources Society of Korea Conference
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    • 2003.04a
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    • pp.104-104
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    • 2003
  • In this study, seven grain seeds(sorghum maize, buckwheat, soy bean, mung bean, red bean, and barngrass) and germinated seven grain seeds were examined the fibrinolytic activity through fibrin plate assay and SDS-PAGE. The results obtained were as follows : 1. In the fibrin plate assay, the extracts of maize, barngrass, sorghum and buckwheat showed fibrinolytic activity. Especially, Maize of them showed fibrinolytic activity that was almost similar to plasmin, fibrinolytic enzyme used as a positive control. 2. In the SDS-PAGE of seven grain seeds, fibrinolytic activity was remarkably shown in mung bean and red bean. 3. In the fibrin plate assay of germinated grain seeds, buckwheat(5 mm), buckwheat(10 mm) and soy bean(10 mm) showed a level of fibrinolytic activity that was about 0.3 fold than 1.0 unit of plasmin, Also maize(10 mm) of them showed a level of fibrinolytic activity that was about 0.5 fold than 1.0 unit of plasmin. As a result, maize of grain seeds was found that it has a strong fibrinolytic activity.

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Effect of Phellinus Extracts on Sprouting in Porcine Pulmonary Artery Endothelial Cells (혈관내피세포의 발아에 미치는 상황버섯 추출물의 효과)

  • Oh, In-Suk;Kim, Hwan-Gyu
    • KSBB Journal
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    • v.21 no.4
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    • pp.292-297
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    • 2006
  • One of the steps in angiogenesis is the degradation of the underlying basement membrane via proteases. Endothelial cells release proteinases to degrade the extracellular matrix for their sprouting in vivo. In this study, we examined the effect of water extracts of Phellinus linteusis(Phellinus extracts) and combination of Phellinus extracts and fibroblast growth factor(FGF-2) on cultured porcine pulmonary artery endothelial cells(PPAECs). Phellinus extracts induced sprouting of PPAECs, which was inhibited by MMPs and plasmin inhibitors, and induced the secretion of matrix metalloproteinase-3(MMP-3) and plasmin. At high concentration of Phellinus extracts($200{\sim}400{\mu}g/mL$), the active MMP-2 secretion was induced. It is therefore, suggested that Phellinus extracts induces the sprouting of cultured endothelial cells by means of increased active MMP-2 and plasmin secretion. Also, combination with Phellinus extracts and FGF-2 produced an enhanced effect on sprouting and secretion of active MMP-2, and MMP-3 and plasmin from PPAECs.

Sildenafil Citrate Induces Migration of Mouse Aortic Endothelial Cells and Proteinase Secretion

  • Kim, Young-Il;Oh, In-Suk;Park, Seung-Moon;Kim, Hwan-Gyu
    • Biotechnology and Bioprocess Engineering:BBE
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    • v.11 no.5
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    • pp.402-407
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    • 2006
  • Vascular endothelial cells release proteinases that degrade the extracellular matrix (ECM), thus enabling cell migration during angiogenesis and vasculogenesis. Sildenafil citrate stimulates the nitric oxide-cyclic guanosine monophosphate pathway through inhibition of phosphodiesterase type V (PDE5). In this report, we examined the mechanisms underlying sildenafil citrate-induced cell migration using cultured mouse aortic endothelial cells (MAECs). Sildenafil citrate induced migration and proteinase secretion by murine endothelial cells. Sildenafil citrate induced the secretion of matrix metalloproteinase-2 (MMP-2) and MMP-9, which is inhibited by $NF-{\kappa}B$ inhibitors. Sildenafil citrate also induced the secretion of plasmin, which is inhibited by PI 3'-kinase inhibitors. It is suggested that sildenafil citrate-induced migrating activity in endothelial cells may be accomplished by increased secretion of proteinases.

Comparative Study of Enzyme Activity and Stability of Bovine and Human Plasmins in Electrophoretic Reagents, β-mercaptoethanol, DTT, SDS, Triton X-100, and Urea

  • Choi, Nack-Shick;Hahm, Jeung-Ho;Maeng, Pil-Jae;Kim, Seung-Ho
    • BMB Reports
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    • v.38 no.2
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    • pp.177-181
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    • 2005
  • Effects of common electrophoretic reagents, reducing agents ($\beta$-mercaptoethanol [BME] and DTT), denaturants (SDS and urea), and non-ionic detergent (Triton X-100), on the activity and stability of bovine plasmin (b-pln) and human plasmin (h-pln) were compared. In the presence of 0.1% SDS (w/v), all reagents completely inhibited two plns, whereas SDS (1%) and urea (1 M) denatured plns recovered their activities after removal of SDS by treatment of 2.5% Triton X-100 (v/v). However, reducing agents (0.1 M of BME and DTT) treated plns did not restore their activities. Based on a fibrin zymogram gel, five (from b-pln) and four (from h-pln) active fragments were resolved. Two plns exhibited unusual stability in concentrated SDS and Triton X-100 (final 10%) and urea (final 6 M) solutions. Two bands, heavy chain-2 (HC-2) and cleaved heavy chain-2 (CHC-2), of b-pln were completely inhibited in 0.5% SDS or 3 M urea, whereas no significant difference was found in h-pln. Interestingly, 50 kDa (cleaved heavy chain-1, CHC-1) of b-pln and two fragments, 26 kDa (light chain, LC) and 29 kDa (microplasmin, MP), of h-pln were increased by SDS in a concentration dependent manner. We also found that the inhibition of SDS against both plns was reversible.

Comparison of fibrinolytic activity from Korean indigenous insects (국내 토착 곤충의 항혈전 비교)

  • Kim, Hyunae;Lee, Sang Han;Choi, Youngcheol;Park, Kwanho;Hwang, Jaesam;Kim, Namjung;Nam, Sunghee
    • Journal of Sericultural and Entomological Science
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    • v.51 no.2
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    • pp.147-152
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    • 2013
  • The fibrinolytic activity of aqueous extracts from Korean indigenous insects were studied. Fibrinolytic activity of aqueous extract from 5 insects (larva and adult parts of Meloimorpha japonica, Allomyrina dichotoma, Cetonia pilifera, Apis mellifera) showed 2.7-fold potent than that of plasmin used as a positive control. In addition, the fibrinolytic activity was observed through the degradation products by SDS-PAGE. The extracts efficiently hydrolyzed ${\alpha}-$, ${\beta}-$ and ${\gamma}$ chains of human fibrinogen. This study suggested that aqueous extracts from Korean indigenous insects have potential in developing a useful source of antithrombosis agent(s).

Purification and Characterization of a New Fibrinolytic Enzyme of Bacillus licheniformis KJ-31, Isolated from Korean Traditional Jeot-gal

  • Hwang, Kyung-Ju;Choi, Kyoung-Hwa;Kim, Myo-Jeong;Park, Cheon-Seok;Cha, Jae-Ho
    • Journal of Microbiology and Biotechnology
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    • v.17 no.9
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    • pp.1469-1476
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    • 2007
  • Jeot-gal is a traditional Korean fermented seafood and has long been used for seasoning. We isolated 188 strains from shrimp, anchovy, and yellow corvina Jeot-gal, and screened sixteen strains that showed strong fibrinolytic activities on a fibrin plate. Among those strains, the strain that had the largest halo zone was chosen and identified as Bacillus licheniformis by using 16S rDNA sequencing and an API CHB kit. The fibrinolytic activity of Bacillus licheniformis was characterized and designated as bpKJ-31. The active component of bpKJ-31 was identified as a 37 kDa protein, designated bacillopeptidase F, by internal peptide mapping and N-terminal sequencing. The optimum activity of bpKJ-31 was shown at pH 9 and $40^{\circ}C$, with a chromogenic substrate for plasmin. It had high degrading activity for the $B{\beta}$-chain and $A{\alpha}$-chain of fibrin(ogen), and also acted on thrombin, but not skim milk and casein. The amidolytic activity of bpKJ-31 was inhibited by 1 mM phenylmethanesulfonyl fluoride, but 1 mM EDTA did not affect the enzyme activity, indicating that bpKJ-31 is an alkaline serine protease, like a plasmin. The bpKJ-31 showed approximately 14.3% higher fibrinolytic activity than the plasmin. These features of bpKJ-31 make it attractive as a health-promoting biomaterial.

Studies on the biological activity of water extract and solvent fractions of wild Grifola frondosa (야생 잎새버섯 물추출물 및 유기용매 분획물의 생리활성 탐색)

  • Seok, Soon-Ja;Kim, Jun-Ho
    • Journal of Mushroom
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    • v.17 no.4
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    • pp.241-246
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    • 2019
  • Samples (10 mg/mL) of wild Grifola frondosa aqueous extract and solvent fractions were examined for fibrinolytic, thrombin inhibitory, acetylcholinesterase inhibitory, and antioxidative activities to determine the biological activities. The fibrinolytic activity of the aqueous extract and solvent fractions was 0.93 and 0.73 plasmin units/mL, respectively. The thrombin inhibitory activity of the butanol extract was 79.60%. The chloroform fraction had high acetylcholinesterase inhibitory activity (85.88%). The aqueous extract had low antioxidative activity (39.81%). The aqueous fraction hydrolyzed Bβ subunits of human fibrinogen but did not show any reactivity for the γ form of the human fibrinogen. The findings indicate the potential of wild Grifola frondosa for the development of drugs and bio-functional foods to prevent cardiovascular diseases.

Effect of Fibroblast Growth Factor-2 on the Sprouting in Vascular Endothelial Cells (혈관내피세포의 발아에 미치는 fibroblast growth factor-2의 효과)

  • 김환규
    • Journal of Life Science
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    • v.14 no.2
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    • pp.263-268
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    • 2004
  • The sprouting of vascular endothelial cells is an initial step in angiogenesis. Matrix metalloproteinases can associate with integrin on the surface of endothelial cells, thereby promoting angiogenesis. The purpose of this study was to test if fibroblast growth factor-2 (FGF-2) can regulate the sprouting in porcine pulmonary artery endothelial cells. FGF-2 induced sprouting and secretion of MMP-2 and plasmin. FGF-2 also induced the expression of integrin Mac-1, which is inhibited IS20I. Addition of BB-94, a 2-antiplasmin and IS20I inhibited FGF-2-induced sprouting activity. Therefore, FGF-2-induced sprouting activity in PPAECs may be accomplished by secretion of proteinases such as MMP-2 and plasmin and integrin expression.

Effect of Hepatocyte Growth Factor on the Migration of Human Umbilical Vein Endothelial Cells (혈관내피세포의 이동에 미치는 Hepatocyte Growth Factor의 영향)

  • 오인숙;소상섭;김환규
    • KSBB Journal
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    • v.18 no.6
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    • pp.485-489
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    • 2003
  • Hepatocyte growth factor (HGF) is a mesenchymal-derived cytokine. It exerts a motogenic effect on various target cells, which is displayed either by cell scattering, locomotion, and migration during the wound repair process of cultured cells, or invasiveness through the extracellular matrix, in vitro. Although it is known that HGF influences the motogenic effect of endothelial cells, the precise effects of HGF during migration are still poorly understood. To elucidate the role of HGF in endothelial cell migration, the effect of HGF on endothelial cell migration and MMPs and plasmin production were studied. We found that HGF induces the migration of cultured endothelial cells through increased MMPs and plasmin secretion.