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      Degradation of human matrix metalloprotease-9 by secretory metalloproteases of Angiostrongylus cantonensis infective stage.

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          Abstract

          Angiostrongylus cantonensis infection is the major cause of eosinophilic meningitis. Successful migration and evasion of the immune system by infective-stage larvae (L3) rely heavily on secreted proteases, which activate human pro-matrix metalloprotease (MMP-9) into active MMP-9. This study showed that the proteases in excretory-secretory (ES) products of A. cantonensis third stage larvae degraded recombinant and native human proMMP-9 in a dose- and time-dependent manner. Protease inhibitory assays showed that metalloproteases were the key enzymes involved in the degradation of human proMMP-9. To assess the effects of ES products on inflammation, ES products were incubated with THP-1 human monocytic cells, which showed induction of MMP-2 and not MMP-9 production. These results indicated that degradation of human MMP-9 was due to metalloproteases present in ES of A. cantonensis L3, which may be involved in suppressing the host's immune response to allow parasite migration to the host central nervous system.

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          Author and article information

          Journal
          Southeast Asian J. Trop. Med. Public Health
          The Southeast Asian journal of tropical medicine and public health
          0125-1562
          0125-1562
          Sep 2012
          : 43
          : 5
          Affiliations
          [1 ] Department of Helminthology, Faculty of Tropical Medicine, Mahidol University, Bangkok, Thailand. tmpad@mahidol.ac.th
          Article
          23431816
          93488ede-7a62-4e28-9937-8f8489f3c392

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