Behaviour and enzyme release by <i>Anisakis</i> sp. larvae (Nematoda: Ascaridida)

Matthews, Bernard E.

doi:10.1017/s0022149x0003457x

Cited by 25 publications

(15 citation statements)

References 12 publications

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“…Generally, in helminth infections, including those by Anisakis , pathological changes in the gastrointestinal tract result from the interaction of the larva and its products secreted during tissue penetration, and the complex immune reaction of the host. Such secreted products, which are mainly released from dorsal esophageal glands and excretory cells of the parasite, are strong proteolytic enzymes that induce mechanical tissue damage by degrading the extracellular matrix [53–58]. In the case of ES-treated cells, observed mortality of the fibroblast line is strongly dose/time-dependent, with corresponding exacerbation of oxidative stress (Fig.…”

Section: Discussionmentioning

confidence: 99%

Anisakis pegreffii (Nematoda: Anisakidae) products modulate oxidative stress and apoptosis-related biomarkers in human cell lines

et al. 2016

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BackgroundIn countries with elevated prevalence of zoonotic anisakiasis and high awareness of this parasitosis, a considerable number of cases that associate Anisakis sp. (Nematoda, Anisakidae) and different bowel carcinomas have been described. Although neoplasia and embedded larvae were observed sharing the common site affected by chronic inflammation, no association between the nematode and malignancy were directly proved. Similarly, no data are available about the effect of secretory and excretory products of infecting larvae at the host’s cellular level, except in respect to allergenic interaction.MethodsTo test the mechanisms by which human non-immune cells respond to the larvae, we exposed the fibroblast cell line HS-68 to two Anisakis products (ES, excretory/secretory products; and EC, crude extract) and evaluated molecular markers related to stress response, oxidative stress, inflammation and apoptosis, such as p53, HSP70, TNF-α, c-jun and c-fos, employing cell viability assay, spectrophotometry, immunoblotting and qPCR.ResultsBoth Anisakis products led to increased production of reactive oxygen species (ROS), especially in EC-treated cells. While the ES treatment induces activation of kinases suggesting inflammation and cell proliferation (or inhibition of apoptosis), in EC-treated cells, other signaling pathways indicate the inhibition of apoptosis, marked by strong upregulation of Hsp70. Elevated induction of p53 in fibroblasts treated by both Anisakis products, suggests a significantly negative effect on the host DNA.ConclusionsThis study shows that in vitro cell response to Anisakis products can result in at least two different scenarios, which in both cases lead to inflammation and DNA damage. Although these preliminary results are far from proving a relationship between the parasite and cancer, they are the first to support the existence of conditions where such changes are feasible.Electronic supplementary materialThe online version of this article (doi:10.1186/s13071-016-1895-5) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Anisakis pegreffii (Nematoda: Anisakidae) products modulate oxidative stress and apoptosis-related biomarkers in human cell lines

et al. 2016

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“…The production of proteolytic enzymes and their release as excretory-secretory (ES) products have been reported for various helminthes (Matthews 1982;McKerrow and Doenhoff 1988;McKerrow et al 1990). Cysteine proteases have been found in Ancylostoma caninum (Harrop et al 1995) and Toxocara canis (Loukas et al 1998).…”

Section: Introductionmentioning

confidence: 98%

Matrix metalloproteinases activity demonstrated in the infective stage of the nematodes, Angiostrongylus cantonensis

et al. 2005

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Ingestion of the larval nematode Angiostrongylus cantonensis can cause the human eosinophilic meningitis known as angiostrongyliasis. Analysis of the extracts and excretory-secretory (ES) products of A. cantonensis larvae and adult stages on gelatin substrate zymography demonstrated the presence of distinct gelatinolytic enzymes. In worm extracts, inhibitor studies showed that the metalloproteinases revealed in L(1) (23 kDa), L(3) (66, 42 and 30 kDa), young adult worm (72 and 94 kDa) and adult worm (72 and 94 kDa). In ES products, the L(1) revealed one low (42 kDa) and two high (105 and 94 kDa) molecular weight proteolytic bands that degraded gelatin in substrate gels. The L(3) revealed three low (66, 50, and 30 kDa) and one high (105 kDa) molecular weight proteolytic bands. Inhibitor studies confirmed that the 105 and 94 proteolytic bands of the L(1), and the 50 and 30 kDa proteolytic bands of the L(3) classification were metalloproteinases. These metalloproteinases secreted in the infective larvae may be associated with the parasite dissemination or pathogenesis.

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“…The production of proteolytic enzymes and their release as excretory-secretory products were reported to be essential to parasite survival in the host environment for various helminthes and/or in parasite evasion of the host's immune system (Petralanda et al 1986;Robertson et al 1989;Uparanukraw et al 2001;Wada et al 1998;McKerrow 1989;McKerrow and Doenhoff 1988;McKerrow et al 1990;Matthews 1982;Morris and Sakanari 1994;Trancart et al 1992).…”

Section: Introductionmentioning

confidence: 99%

A relevant enzyme in granulomatous reaction, active matrix metalloproteinase-9, found in bovine Echinococcus granulosus hydatid cyst wall and fluid

et al. 2006

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In addition to the ability of matrix metalloproteinases (MMP) to degrade components of the extracellular matrix and their involvement in pathology-related processes of tissue remodeling, they were recently reported to enhance inflammation by activation of proinflammatory cytokines, or their release from the cell surface. In the work reported here, proteolytic activity previously found for hydatid cysts was further characterized as MMP-9. Active host MMP-9 was found in walls and fluids of bovine hydatid cysts of Echinococcus granulosus in the environment of granulomatous reaction. Pooled walls and fluids of hydatid cysts obtained from infected cattle were processed. Strong proteolytic activity was detected by zymography. The proteolytic fraction was purified by anion exchange and gelatin-agarose affinity chromatography. Major proteinases of the purified fraction were subjected to mass spectrometry and their identities were further confirmed by Western blotting using commercial anti-human MMP-9 monoclonal antibodies. Two proteinases were characterized as latent and active forms of host MMP-9. Using the same antibody for immunoblot, activity was localized, in paraffin-embedded sections of the parasite and the local host environment, to epithelioid and giant multinucleated cells. It is proposed here that MMP-9 is secreted by specialized host cells of monocytic lineage (epithelioid/giant cells) as an effector, in an attempt to digest the persistent foreign body. In vivo activation of MMP-9 suggests its involvement in inflammatory reaction and in the chemotaxis of inflammatory cells to the cyst. However, E. granulosus can deal efficiently with MMP-9. Research is suggested into possible immune evasion mechanisms, including the secretion of an inhibitory molecule.

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Behaviour and enzyme release by Anisakis sp. larvae (Nematoda: Ascaridida)

Cited by 25 publications

References 12 publications

Anisakis pegreffii (Nematoda: Anisakidae) products modulate oxidative stress and apoptosis-related biomarkers in human cell lines

Anisakis pegreffii (Nematoda: Anisakidae) products modulate oxidative stress and apoptosis-related biomarkers in human cell lines

Matrix metalloproteinases activity demonstrated in the infective stage of the nematodes, Angiostrongylus cantonensis

A relevant enzyme in granulomatous reaction, active matrix metalloproteinase-9, found in bovine Echinococcus granulosus hydatid cyst wall and fluid

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