ArticleParasitology research2005
Matrix metalloproteinases activity demonstrated in the infective stage of the nematodes, Angiostrongylus cantonensis.
Article in Parasitology research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Assessment of the efficacy of thymol againstJournal of parasitic diseases : official organ of the Indian Society for Parasitology · 2022Article
- Haemonchus contortus: siRNA mediated knockdown of matrix metalloproteinase 12A (MMP-12) results in reduction of infectivity.Parasites & vectors · 2020Article
- Identification of a phenoloxidase- and melanin-dependent defence mechanism in Achatina fulica infected with Angiostrongylus vasorum.Parasites & vectors · 2018Article
- A 24-48 h fed Amblyomma americanum tick saliva immuno-proteome.BMC genomics · 2014Article
- The significance of matrix metalloproteinases in parasitic infections involving the central nervous system.Pathogens (Basel, Switzerland) · 2013Review
- Differences of larval development and pathological changes in permissive and nonpermissive rodent hosts for Angiostrongylus cantonensis infection.Parasitology research · 2012Article
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Authors and funding
4 authors.
Funding
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Abstract
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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