Association of matrix metalloproteinase-9 in eosinophilic meningitis of BALB/c mice caused by Angiostrongylus cantonensis

• Published in: Parasitology research (1987) 2004-11, Vol.94 (5), p.321-328
• Main Authors: LEE, H. H, CHOU, H. L, CHEN, K. M, LAI, S. C
• Format: Article
• Language: English
• Subjects: Angiostrongylus cantonensis - pathogenicity; Animals; Biological and medical sciences; Eosinophilia - parasitology; Fundamental and applied biological sciences. Psychology; General aspects; General aspects and techniques. Study of several systematic groups. Models; Invertebrates; Male; Matrix Metalloproteinase 9 - metabolism; Meningitis - parasitology; Mice; Mice, Inbred BALB C; Strongylida Infections - parasitology; Subarachnoid Space - immunology; Subarachnoid Space - metabolism
• ISSN: 0932-0113; 1432-1955
• DOI: 10.1007/s00436-004-1196-3

Induction of gelatinase in eosinophilic meningitis of BALB/c-strain mice was caused by Angiostrongylus cantonensis. Time-course studies showed that the molecular weight of 94-kDa gelatinase was detected at day 10 post-inoculation (PI), and reached a high intensity from days 15 to 25 PI. The 94-kDa gelatinase activity was clearly inhibited by EDTA and 1,10-phenanthroline, but not by leupeptin and phenylmethanesulphonyl fluoride. When immunoblots were performed using specific antiserums against the 94-kDa gelatinase B (matrix metalloproteinase-9; MMP-9) with cerebrospinal fluid (CSF), the 94-kDa immunopositive band was MMP-9. Immunohistochemistry studies demonstrated MMP-9 localisation within eosinophils and macrophages. The increased MMP-9 activity was closely associated with the rapid rise of CSF eosinophils, and the inflammatory reaction of the subarachnoid space. In contrast to changes in MMP-9, MMP-2 activity was constitutive and unaffected in this parasitic meningitis. These results show that MMP-9 was associated with eosinophilic meningitis, and that the enzyme may be a useful marker for angiostrongyliasis meningitis.