Glycosylated trypsin-like proteases from earthworm Eisenia fetida

Wu, Jianhua; Zhao, Xiyang; Pan, Rong; He, Rong

doi:10.1016/j.ijbiomac.2006.10.001

Cited by 35 publications

(23 citation statements)

References 34 publications

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“…The two constituting subunits (26,000 Da and 18,000 Da) with different fibrinolytic activities are bound by hydrophobic interaction. Wu and colleagues isolated eight fibrinolytic enzymes (Ef P-0-1, Ef P-0-2, Ef P-I-1, Ef P-I-2, Ef P-II-1, Ef P-II-2, Ef P-III-1, and Ef P-III-2) through a stepwise-purification procedure in 2007 [26]. They are all glycoproteins (Table 1).…”

Section: Isozymes From Eisenia Fetidamentioning

confidence: 99%

“…α 2 M binds to the enzyme mole by mole equivalently and the interaction may undergo a chelate irreversible inhibition. Table 3, the N-terminal sequences of the isozymes from L. rubellus and E. fetida have been analyzed [26]. The sequences of the isozymes from L. rubellus and E. fetida have a lot of identical residues.…”

Section: Inhibitors Of the Earthworm Proteasementioning

confidence: 99%

“…Recent studies show that the earthworm proteases are glycosylated [26]. The result of staining on the native-SDS gel with Schiff 's reagent shows that the eight isozymes isolated from Eisenia fetida by Wu and colleagues are all glycoproteins.…”

Section: Primary Structure As Shown Inmentioning

confidence: 99%

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Earthworm Protease

Pan

Zhang

2010

Applied and Environmental Soil Science

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The alimentary tract of earthworm secretes a group of proteases with a relative wide substrate specificity. In 1983, six isozymes were isolated from earthworm with fibrinolytic activities and called fibriniolytic enzymes. So far, more isozymes have been found from different earthworm species such as Lumbricus rubellus and Eisenia fetida. For convenience, the proteases are named on the basis of the earthworm species and the protein function, for instance, Eisenia fetida protease (Ef P). The proteases have the abilities not only to hydrolyze fibrin and other protein, but also activate proenzymes such as plasminogen and prothrombin. In the light of recent studies, eight of the Ef Ps contain oligosaccharides chains which are thought to support the enzyme structure. Interestingly, Ef P-II has a broader substrate specificity presenting alkaline trypsin, chymotrypsin and elastase activities, but Ef P-III-1 has a stricter specificity. The protein crystal structures show the characteristics in their specificities. Earthworm proteases have been applied in several areas such as clinical treatment of clotting diseases, anti-tumor study, environmental protection and nutritional production. The current clinical utilizations and some potential new applications of the earthworm protease will be discussed in this paper.

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Section: Isozymes From Eisenia Fetidamentioning

confidence: 99%

Section: Inhibitors Of the Earthworm Proteasementioning

confidence: 99%

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Earthworm Protease

Pan

Zhang

2010

Applied and Environmental Soil Science

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“…To date, many other species of earthworm including Eisenia foetida [13] , Neanthes japonica [14] and Pheretima posthuma [15] have been explored for several fibrinolytic enzymes. EFE has been applied as an oral thrombolytic agents for the prevention of cardiac and cerebrovascular diseases due to its strong fibrinolytic activity [16] .…”

Section: Coworkers Frommentioning

confidence: 99%

Antitumor Studies of Earthworm Fibrinolytic Enzyme Component A from Eisenia foetida on Breast Cancer Cell Line MCF-7

Liu¹,

Chen²,

Pan³

et al. 2017

pharmaceutical-sciences

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Liu, et al.: Antitumor Studies of Earthworm Fibrinolytic Enzyme Component A on MCF-7Earthworm fibrinolytic enzyme from Chinese earthworm Eisenia foetida was isolated to investigate its antitumor activity in breast cancer cells. The protein isolated was characterised as earthworm fibrinolytic enzyme using the fibrin plate method. The molecular weight of earthworm fibrinolytic enzyme component was determined to be 25 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis assay using a standard protein ladder. Earthworm fibrinolytic enzyme can markedly inhibit the growth and migration of MCF-7 cells in a dose and time-dependent manner. In addition, MCF-7 cells treated with earthworm fibrinolytic enzyme (40 μg/ml) began to undergo apoptosis after 24 h. Expression of focal adhesion kinase and CD44v6 measured using reverse transcription polymerase chain reaction and Western blot was down-regulated in a concentration-dependent manner (20-80 μg/ml), resulting in the suppression of MCF-7 cells adhesion. The obtained earthworm fibrinolytic enzyme displayed an antitumor effect on MCF-7 cells in vitro, revealing the therapeutic potential of E. foetida.

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“…In this laboratory, eight trypsin-like isozymes with fibrinolytic activity were isolated from Eisenia fetida through a stepwise-purified procedure: sulfate ammonia precipitation, affinity chromatography with a Sepharose-4B column coupled with soybean trypsin inhibitor (SBTI), and ionic chromatography with a DEAE-cellulose-52 column [21]. Interestingly, all the proteases were glycosylated.…”

Section: Introductionmentioning

confidence: 99%

Eisenia fetida Protease-III-1 Functions in Both Fibrinolysis and Fibrogenesis

Zhao

Pan

et al. 2007

Journal of Biomedicine and Biotechnology

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The fibrinolytic function of earthworm protease-III-1 (Ef P-III-1) has been studied in recent years. Here, we found that Ef P-III-1 acted not only in fibrinogenolysis, but also in fibrogenesis. We have used Ef P-III-1 to hydrolyze fibrinogen, and to activate plasminogen and prothrombin. Based on the N-terminal sequences of the hydrolytic fragments, Ef P-III-1 was showed to specifically recognize the carboxylic sites of arginine and lysine. Analyses by fibrinogenolysis mapping and amino acid sequencing revealed that the isozyme could cleave the alpha, beta, and gamma chains of fibrinogen, showing a high α-fibrinogenase, moderate β-fibrinogenase, and low γ-fibrinogenase activities. Interestingly, Ef P-III-1 activated plasminogen and released active plasmin, suggesting a tPA-like function. Furthermore, Ef P-III-1 showed a factor Xa-like function on prothrombin, producing alpha-thrombin. The function in both activating prothrombin and catalyzing fibrinogenolysis suggests that Ef P-III-1 may play a role in the balance between procoagulation and anticoagulation.

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Glycosylated trypsin-like proteases from earthworm Eisenia fetida

Cited by 35 publications

References 34 publications

Earthworm Protease

Earthworm Protease

Antitumor Studies of Earthworm Fibrinolytic Enzyme Component A from Eisenia foetida on Breast Cancer Cell Line MCF-7

Eisenia fetida Protease-III-1 Functions in Both Fibrinolysis and Fibrogenesis

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