Beta 1 and beta 4 integrin expression in methacarn and formalin-fixed material from in situ ductal carcinoma of the breast.

The integrins are alpha beta heterodimeric transmembrane proteins mediating cell-substratum as well as cell-cell interactions. Previous distribution studies on integrin expression have been limited by the requirement of cryostat sectioned tissues, and consequent poor resolution. We have examined 40 examples of ductal carcinoma in situ (DCIS) for the expression of both beta 1 and beta 4 integrin chains. These showed strong polarized membrane staining of residual myoepithelial cells (correlating with expression of smooth muscle specific actin) and of the basement membrane region with beta 1 and beta 4 antibodies respectively. In 12 out of 40 cases, the DCIS was negative for the beta 1 chain and a variable pattern of reactivity was seen in the remaining cases. The beta 4 chain was detected focally and weakly in the tumour cells of 7/40 DCIS and strongly in one; all of these cases were also positive for the beta 1 chain. Of the 22 cases where co-existent invasion was present, the infiltrating component showed either a similar degree or a diminution of the extent of immunostaining when compared with the in situ component; only one showed enhanced staining (beta 1 only). This study demonstrates that two of the main beta chains, beta 1 and beta 4, can be effectively demonstrated on methacarn and cold (4 degrees C) formalin-fixed tissues by avidin-biotin indirect immunoperoxidase staining and that the results are similar to those achieved using frozen tissue.