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  1. Fulltext Antineutrophil Cytoplasmic Autoantibody-Negative Pauci-Immune Crescentic Glomerulonephritis in a Patient with Systemic Lupus Erythematosus
    Chan CE, Ng TJ, Ahmad MK, Mohamad Nor FS
    Case Rep Nephrol Dial, 2022;12(3):201-206.
    PMID: 36465575 DOI: 10.1159/000527248
    Renal involvement in systemic lupus erythematosus is usually exhibited as lupus nephritis, which is a form of immune complex-mediated glomerulonephritis and one of the most severe organ manifestations of systemic lupus erythematosus. The pathogenesis involved glomerular immune complex deposition, which leads to glomerular inflammation and typically shows a "full-house" pattern on immunofluorescence microscopy. Other forms of glomerulonephritis are rarely observed in patients with systemic lupus erythematosus. Pauci-immune crescentic glomerulonephritis is the pattern of injury most commonly observed in patients with antineutrophil cytoplasmic autoantibody-associated glomerulonephritis. The characteristic histological feature of pauci-immune crescentic glomerulonephritis is focal necrotizing and crescentic glomerulonephritis with little or no glomerular staining for immunoglobulin by immunofluorescence microscopy. We report a rare case of antineutrophil cytoplasmic autoantibody-negative pauci-immune crescentic glomerulonephritis in a patient with systemic lupus erythematosus.
  2. Fulltext Cytotoxic and apoptosis-inducing effects of wildtype and mutated Hydra actinoporin-like toxin 1 (HALT-1) on various cancer cell lines
    Ng TJ, Teo MYM, Liew DS, Effiong PE, Hwang JS, Lim CSY, et al.
    PeerJ, 2019;7:e6639.
    PMID: 31106043 DOI: 10.7717/peerj.6639
    Background: Hydra actinoporin like toxin -1 (HALT-1), is a small 18.5 kDa pore forming toxin derived from Hydra magnipapillata which has been shown to elicit strong haemolytic and cytolytic activity when in contact with cell membranes. Due to its cytotoxic potency, HALT-1 was further investigated for its potential as a toxin moiety candidate in immunotoxin developmental efforts, ideally as a form of targeted therapy against cancer.

    Methods: In this study, wtHALT-1 (wild type) and its Y110A mutated binding domain counterpart (mHALT-1) were produced and evaluated for their cytotoxic and apoptotic effects on various cancer cell lines. A total of seven different tumour and non-tumour cell lines including HeLa, HepG2, SW-620, MCF-7, CCD841CoN, NHDF and HCT116 were used. Immunofluorescence assays were used to observe membrane binding and localization changes between both HALT-1 recombinant proteins based on 6xHis-tag detection.

    Result: Based on MTT data, mHALT-1 demonstrated a significant reduction of 82% ±  12.21% in cytotoxic activity across all cell lines after the membrane recognition domain had been mutated in comparison to the wtHALT-1. Annexin V FITC/PI assay data also indicated that HeLa, HepG2 and MCF-7 demonstrated an apoptosis-mediated cell death after being treated with wtHALT-1. Additionally, a notable difference between wtHALT-1 and mHALT-1 binding affinity was clearly observed where emission of green fluorescence along the cell membrane was observed only in wtHALT-1 treated cells.

    Discussion: These results suggest that mHALT-1 (Y110A) can be potentially developed as a toxin-moiety candidate for the development of future immunotoxins against various human cell-based diseases.

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