Adhesins of Immunoglobulin-like Superfamily from Earthworm Eisenia foetida

Popović, Maja; Hrženjak, Terezija; Grdiša, Mira; Vuković, Snježana

doi:10.1016/s0306-3623(97)00014-1

Cited by 23 publications

(16 citation statements)

References 34 publications

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“…It was recently shown that G-90 is neither allergic nor toxic, and possesses antibacterial activity [61] and antioxidative effects [62]. G-90 exhibits many biological functions important in the proliferation [63] and adhesion [64] of cells. The G-90 mixture contains insulin like growth factors, immunoglobulin-like growth factor, serine proteases and epidermal growth factor (EGF) [6, 35, 59, 61, 63, 64].…”

Section: Discussionmentioning

confidence: 99%

Schwann Cell Migration Induced by Earthworm Extract via Activation of PAs and MMP2/9 Mediated through ERK1/2 and p38

Chang

Shih

Chen

et al. 2011

Evidence-Based Complementary and Alternative Medicine

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The earthworm, which has stasis removal and wound-healing functions, is a widely used Chinese herbal medicine in China. Schwann cell migration is critical for the regeneration of injured nerves. Schwann cells provide an essentially supportive activity for neuron regeneration. However, the molecular migration mechanisms induced by earthworms in Schwann cells remain unclear. Here, we investigate the roles of MAPK (ERK1/2, JNK and p38) pathways for earthworm-induced matrix-degrading proteolytic enzyme (PAs and MMP2/9) production in Schwann cells. Moreover, earthworm induced phosphorylation of ERK1/2 and p38, but not JNK, activate the downstream signaling expression of PAs and MMPs in a time-dependent manner. Earthworm-stimulated ERK1/2 and p38 phosphorylation was attenuated by pretreatment with U0126 and SB203580, resulting in migration and uPA-related signal pathway inhibition. The results were confirmed using small interfering ERK1/2 and p38 RNA. These results demonstrated that earthworms can stimulate Schwann cell migration and up-regulate PAs and MMP2/9 expression mediated through the MAPK pathways, ERK1/2 and p38. Taken together, our data suggests the MAPKs (ERK1/2, p38)-, PAs (uPA, tPA)-, MMP (MMP2, MMP9) signaling pathway of Schwann cells regulated by earthworms might play a major role in Schwann cell migration and nerve regeneration.

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Section: Discussionmentioning

confidence: 99%

Schwann Cell Migration Induced by Earthworm Extract via Activation of PAs and MMP2/9 Mediated through ERK1/2 and p38

Chang

Shih

Chen

et al. 2011

Evidence-Based Complementary and Alternative Medicine

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“…In order to inhibit the hyperactivity of the u-PA, inhibitors of plasminogen activators are synthesized by the surrounding cells for tissue protection, resulting in a high concentration of fibrin locally. The glycolipoprotein mixture (G-90) was isolated from the homogenate of E. fetida [15][16][17]19], which is assayed in a euglobulinic test applied to fibrin clot from blood plasma of patients who suffered from malignant tumors. The effect of G-90 on the fibrinolysis rate is related to not only its concentration, but also to histological type where the malignant tumors invade.…”

Section: Antitumormentioning

confidence: 99%

“…Subsequently different purification methods were applied to isolate the enzymes, including gel filtration, affinity chromatography, ion exchanging chromatography, and high-pressure liquid chromatography (HPLC). More proteases have been obtained from different species, such as lumbrokinase [4], earthworm-tissue plasminogen activator [5], earthworm plasminogen activator [6][7][8][9][10][11], component A of EFE (EFEa) [12,13], and biologically active glycolipoprotein complex (G-90) [14][15][16][17][18][19].…”

Section: Introductionmentioning

confidence: 99%

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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“…8. 9 Control experiments indicated that the antibody reacted speci®cally with phosphotyrosine-containing proteins (data not shown).…”

Section: Detection Of Phosphotyrosine-containing Proteinsmentioning

confidence: 94%

Alteration of phosphotyrosine-containing proteins during differentiation of chicken erythroleukemia cells (HD3)

Grdiša

1998

Cell Biochem. Funct.

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After treatment of HD3 cells with erythroid-inducing agents (hemin and butyric acid) at 42 degrees C, the profile of phosphotyrosine-containing proteins was altered. Upon induction the overall level of phosphotyrosine-containing proteins increased. To examine the role of protein phosphorylation in HD3 cells differentiation, the cells were treated with specific inhibitors. In the presence of okadaic acid, cell proliferation was arrested and accompanied by a marked increase in haemoglobin synthesis, a differentiation marker of erythroid cells. Okadaic acid caused decrease of the phosphotyrosine-containing proteins, presumably to maintain a balance between phosphorylation/dephosphorylation processes in the cells. Addition of 3-isobutyl-1-methyl-xanthine, an activator of phosphatases, caused a decrease or disappearance of almost all phosphotyrosine-containing proteins and, at the same time, prevented the erythroid differentiation of HD3 cells. Sodium orthovanadate, a specific inhibitor of phosphotyrosine phosphatase, increased the level of phosphotyrosine proteins and induced differentiation of HD3 cells. These results indicate that phosphorylation of cellular proteins is coupled with a reaction(s) which is responsible for triggering the differentiation of HD3 cells. The phosphorylation/dephosphorylation processes are associated with an early event(s) during the differentiation of HD3 cells and may not be connected to tyrosine residues.

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Adhesins of Immunoglobulin-like Superfamily from Earthworm Eisenia foetida

Cited by 23 publications

References 34 publications

Schwann Cell Migration Induced by Earthworm Extract via Activation of PAs and MMP2/9 Mediated through ERK1/2 and p38

Schwann Cell Migration Induced by Earthworm Extract via Activation of PAs and MMP2/9 Mediated through ERK1/2 and p38

Earthworm Protease

Alteration of phosphotyrosine-containing proteins during differentiation of chicken erythroleukemia cells (HD3)

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