A novel fibrinolytic serine protease from the polychaete Nereis (Neanthes) virens (Sars): Purification and characterization

Zhang, Yunlong; Cui, Jiayue; Zhang, Rui; Yan-pin, Wang; Hong, Ming

doi:10.1016/j.biochi.2006.07.023

Cited by 25 publications

(11 citation statements)

References 53 publications

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“…Similarly, when Wbrin was incubated with Fu-P, the band was rapidly hydrolyzed, and the chain and -chain were slowly hydrolyzed (date not shown). This hydrolytic pattern was similar to that of other proteases puriWed from C. divaricatum and snake venom [3,50], but was diVerent from the Wbrinolytic enzymes of the medicinal mushroom Cordyceps militaris [25] and B. subtilis FS33 [48].…”

Section: The N-terminal Amino Acid Sequence Of the Wbrinolytic Enzymementioning

confidence: 81%

Purification and characterization of a novel fibrinolytic protease from Fusarium sp. CPCC 480097

Li-cheng

Chen

et al. 2009

J Ind Microbiol Biotechnol

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A novel fibrinolytic enzyme from Fusarium sp. CPCC 480097, named Fu-P, was purified to electrophoretic homogeneity using ammonium sulfate precipitation and ion exchange and gel filtration chromatography. Fu-P, a single protein had a molecular weight of 28 kDa, which was determined by SDS-PAGE and gel filtration chromatography. The isoelectric point of Fu-P determined by isoelectric focusing electrophoresis (IEF) was 8.1, and the optimum temperature and pH value were 45 degrees C and 8.5, respectively. Fu-P cleaved the alpha-chain of fibrin (ogen) with high efficiency, and the beta-chain and gamma-gamma (gamma-)-chain with lower efficiency. Fu-P activity was inhibited by EDTA and PMSF, and the enzyme exhibited a high specificity for the chymotrypsin substrate S-2586. Fu-P was therefore identified as a chymotrypsin-like serine metalloprotease. The first 15 amino acids of the N-terminal sequence of Fu-P were Q-A-S-S-G-T-P-A-T-I-R-V-L-V-V and showed no homology with that of other known fibrinolytic enzymes. This protease may have potential applications in thrombolytic therapy and in thrombosis prevention.

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Section: The N-terminal Amino Acid Sequence Of the Wbrinolytic Enzymementioning

confidence: 81%

Purification and characterization of a novel fibrinolytic protease from Fusarium sp. CPCC 480097

Li-cheng

Chen

et al. 2009

J Ind Microbiol Biotechnol

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“…Nereis (Neanthes) virens (Sars) are common intertidal marine polychaete (Annelida: Polychaeta) with a novel fibrinolytic serine protease from their coelomic fluid possessing a strong fibrinolytic activity. Thrombolytic agents generate plasmin from plasminogen suggesting that the availability of this protease from clamworm may be used as an attractive alternative approach for thrombolysis treatments [58]. A novel protease, extracted from the polychaeta, Periserrula leucophryna, is a novel alkaline protease having a strong stability against extreme of pH and temperature, detergents, oxidizing agents, heavy metals and another solvents that make it suitable for industrial targets [59].…”

Section: Proteases From Polychaetamentioning

confidence: 99%

Development of marine biotechnology as a resource for novel proteases and their role in modern biotechnology

Homaei

Lavajoo

Sariri

2016

International Journal of Biological Macromolecules

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Marine environment consists of the largest sources diversified genetic pool of material with an enormous potential for a wide variety of enzymes including proteases. A protease hydrolyzes the peptide bond and most of proteases possess many industrial applications. Marine proteases differ considerably from those found in internal or external organs of invertebrates and vertebrates. In common with all enzymes, external factors such as temperature, pH and type of media are important for the activity, catalytic efficiency, stability and proper functioning of proteases. In this review valuable characteristics of proteases in marine organisms and their applications are gathered from a wide literature survey. Considering their biochemical significance and their increasing importance in biotechnology, a thorough understanding of marine proteases functioning could be of prime importance.

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“…However, there were no references in relation to anti-lung cancer protease extracted from marine sources. In this study, purified Nereis serine protease (NAP) was obtained from Nereis virens , according to the previous study [ 17 ], and in vitro experiments carried out using lung cancer cells to determine the effectiveness of NAP in inducing apoptosis. Furthermore, in vivo experiments were also performed to determine whether NAP suppresses lung tumor growth.…”

Section: Introductionmentioning

confidence: 99%

A Purified Serine Protease from Nereis virens and Its Impaction of Apoptosis on Human Lung Cancer Cells

et al. 2017

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Nereis active protease (NAP) is a novel fibrinolytic active serine protease from the polychaete Nereis virens. In this study, NAP was purified from Nereis virens and the effects of NAP on human lung cancer cells were investigated. Our results indicated that NAP inhibited the proliferation and induced apoptosis of H1299 cells in a time- and dose-dependent manner. The loss of mitochondrial membrane potential, the activation of Bax and cleaved-caspase 3/9, the release of cytochrome C, and the suppression of Bcl-2 and poly-ADP ribose polymerase were observed in NAP-treated H1299 cells by flow cytometry and Western blotting. Moreover, the expression levels of Bax and Bcl-2 mRNA were determined by real-time quantitative polymerase chain reaction and the Bax/Bcl-2 expression ratio was increased in the NAP-treated cell lines. The results indicated that NAP-induced apoptosis may be related to mitochondria mediated apoptosis and occurs through caspase-dependent pathways. Then, the effects of NAP on tumor growth in animal models were observed, where 5 or 10 mg/kg of NAP noticeably reduced tumor volume and weight and increased apoptosis as determined by Western blotting when compared to the negative control group. Therefore, our findings suggest that NAP could be a hopeful anticancer medicine for its propensity to inhibit growth and induce of apoptosis in human lung cancer cells.

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A novel fibrinolytic serine protease from the polychaete Nereis (Neanthes) virens (Sars): Purification and characterization

Cited by 25 publications

References 53 publications

Purification and characterization of a novel fibrinolytic protease from Fusarium sp. CPCC 480097

Purification and characterization of a novel fibrinolytic protease from Fusarium sp. CPCC 480097

Development of marine biotechnology as a resource for novel proteases and their role in modern biotechnology

A Purified Serine Protease from Nereis virens and Its Impaction of Apoptosis on Human Lung Cancer Cells

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