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• W1582065993 abstract "Aims To demonstrate immunohistochemically the α3 and γ2 chain of laminin-5 in benign epithelial and malignant lesions of the human breast. Methods and results The α3 chain was identified by the monoclonal antibody BM165 and the γ2 chain by GB3 in shock frozen samples using APAAP (alkaline phosphatase monoclonal anti-alkaline phosphatase) technique. The pre-existing breast epithelium, the 12 benign ductal and lobular proliferations and the three fibroadenomas showed a continuous immunostaining in the basement membrane region. In contrast to benign epithelial lesions, the 44 cases of invasive breast carcinoma showed a loss of the laminin-5 chains in more than 50% of the carcinoma stroma interface. Twenty-four out of the 44 invasive carcinomas revealed a complete loss of laminin-5 immunostaining. Focal defects of the laminin-5 immunostaining were also found in ductal carcinoma in situ in its pure form. Conclusions As recently described, the malignant transformation of breast epithelium with expression of an invasive phenotype is associated with a decrease of hemidesmosomes. The reduced immunostaining of laminin-5 is in line with this finding because laminin-5 represents the major component of the anchoring filaments attaching hemidesmosomes to the basement membrane. We feel that immunohistochemical demonstration of laminin-5 may serve as a marker of benignity in epithelial breast lesions. While other carcinoma types exhibit an increased laminin-5 deposition, which has been suggested as an invasion promoting factor, the loss of laminin-5 in breast cancer supports the view that breast carcinomas do not utilize laminin-5 for invasion." @default.
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• W1582065993 date "1999-04-01" @default.
• W1582065993 modified "2023-09-25" @default.
• W1582065993 title "Loss of laminin-5 in the epithelium-stroma interface: an immunohistochemical marker of malignancy in epithelial lesions of the breast" @default.
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• W1582065993 doi "https://doi.org/10.1046/j.1365-2559.1999.00634.x" @default.
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