Sir Peter MacCallum Department of Oncology - Research Publications

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Author: McKenzie, Ian × End date: 1993 × Start date: 1990 × Type: Journal Article ×

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    THE PROGNOSTIC VALUE OF IMMUNOPEROXIDASE STAINING WITH MONOCLONAL-ANTIBODIES NCRC-11 AND 3E1.2 IN BREAST-CANCER
    MUIR, IM ; REED, RG ; STACKER, SA ; ALEXANDER, AI ; MCKENZIE, IFC ; BENNETT, RC (STOCKTON PRESS, 1991-07)
    The variation in survival of women with clinically similar breast cancers may lead to difficulty in clinical management so it is important to recognise factors which indicate the prognosis. Immunoperoxidase staining patterns of primary breast tumours using monoclonal antibody NCRC-11 have been shown to relate to overall survival (Ellis et al., 1985) but the results have not been reproducible in other centres. In this study paraffin sections of 483 primary breast cancers were stained with NCRC-11 and 3E1.2 using an immunoperoxidase system. The tumour staining patterns were compared with overall survival using life tables and tested for relative prognostic significance by Cox's multivariate analysis. NCRC-11 related to survival in all 483 cases (chi 2 5.8, P = 0.02) but both antibodies achieved maximum prognostic significance in lymph node negative patients (chi 2 9.4, P less than 0.002 and chi 2 10.7, P less than 0.001) in whom no other factor was more significant. Immunoperoxidase staining patterns produced by monoclonal antibodies NCRC-11 and 3E1.2 are important prognostic factors in breast cancer.
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    PRODUCTION OF ANTI-BREAST CANCER MONOCLONAL-ANTIBODIES USING A GLUTATHIONE-S-TRANSFERASE-MUC1 BACTERIAL FUSION PROTEIN
    APOSTOLOPOULOS, V ; XING, PX ; TRAPANI, JA ; MCKENZIE, IFC (NATURE PUBLISHING GROUP, 1993-04)
    Two murine Mabs VA1(IgG1) and VA2(IgG1) were produced against a bacterial fusion protein comprising glutathione S-transferase and five tandem repeats of the MUC1 protein. Using the immunoperoxidase staining technique, VA1 detected 46/53 and VA2 detected 48/53 breast cancers and both also reacted with a range of other human epithelial carcinomas. In addition VA1 gave weak reactions with normal breast tissues whereas VA2 was non-reactive and could be a relatively tumour specific antibody for breast cancer. The antibodies were also tested by ELISA-VA1 reacted weakly with glycosylated HMFG but strongly with deglycosylated HMFG, whereas VA2 reacted strongly with both forms of HMFG. The reactivities of the two Mabs with synthetic peptides of the MUC1 tandem repeat were used to map the epitopes recognised by VA1 (amino acids RPAPGS) and VA2 (amino acids DTRPA). The use of fusion proteins provides another means of immunisation to produce anti-tumour antibodies.