Immunohistochemical study of the expression of MUC5AC and MUC6 in breast carcinomas and adjacent breast tissues

Abstract

Aim - To study the protein expression patterns of MUC5AC and MUG6 in normal and diseased breast tissues and to compare their expression with that of a mucin (MUG1) normally expressed in mammary tissues. Methods - Formalin fixed, paraffin wax embedded tissue from 69 cases of invasive breast carcinoma and surrounding breast tissue was studied irnmunohistochemically with monoclonal antibodies against MUG1 (SM3), MUG5AG (CLH2), and MUG6 (CLH6), using the avidin-biotin-peroxidase method. Results - MUG5AG was detected in five of 68 cases of invasive carcinoma including one of three cases of pure colloid carcinoma. MUGSAG expression in the adjacent normal breast epithelium was present in one of 29 cases and in one of two cases of ductal carcinoma in situ. None of 15 cases of ductal hyperplasia without atypia was positive for MUG5AG. MUG6 was present in 15 of 65 cases of invasive carcinoma, in four of 29 cases of normal adjacent epithelium, two of 15 cases of ductal hyperplasia without atypia, and one of two cases of ductal carcinoma in situ. MUG1 immunoreactivity detected by the SM3 antibody was present in 50 of the 67 cases of invasive carcinoma, but expression was also detected in benign epithelium. All invasive carcinomas expressing MUGSAG were positive for MUG1 and four were positive for MUG6. No significant association was found between the expression of these mucins and tumour size, histological grade, node status, oestrogen receptor status, p53 positivity, or c-ErbB-2 overexpression. Conclusions - This study documents the expression of two different mucins (MUGSAG and MUG6) not described as being expressed by normal breast tissues in a minority of breast carcinomas, as well as in normal and hyperplastic epithelium. Although the role of mucins in malignant transformation and the progression of breast cancer is not well understood, in some cases, there is probably an upregulation of several genes that encode distinct mucin proteins.