Abstract
Tissue inhibitor of metalloproteinase-1 (TIMP-1) is a natural inhibitor of matrix metalloproteinases (MMPs). Aim of this study was to assess the immunohistochemical expression of TIMP-1 in invasive breast carcinomas, and to examine its association with classical clinico-pathological parameters, oestrogen receptor, progesterone receptor and Her-2/neu protein expression. Immunohistochemistry was used to determine the expression of TIMP-1 on 38 paraffin-embedded breast tissue specimens - 18 with invasive ductal carcinoma, 10 with invasive lobular carcinoma, and 10 specimens from patients with fibrocystic breast disease. TIMP-1 protein was immunodetected in the carcinoma cells, fibroblasts and inflammatory cells of the stroma in 92,9%, 65,8%, and 65,8% of cases, respectively. TIMP-1 protein expression in carcinoma cells showed positive correlation with TIMP-1 protein expression in peritumoural fibroblasts (p=0,010). Positive peritumoural fibroblast TIMP-1 expression was associated with histological tumour type with higher frequency in ductal carcinomas (p=0,023). Negative association was found between TIMP-1 protein expression in carcinoma cells and HER-2/neu nuclear staining (p=0,005). TIMP-1 may be particularly useful as a predictive marker in breast carcinoma when evaluated along with HER-2/neu protein being a promising indicator of favourable prognosis in breast carcinoma.
Highlights
Matrix metalloproteinases (MMPs) belong to a family of zinc-dependent extracellular endopeptidase capable of degrading most components of the extracellular matrix ( )
We explored potential interaction of TIMP- expression in cytoplasm and in cell nucleus of the both invasive breast carcinoma and fibrocystic breast disease
Percentage of TIMP- protein positive cells was significantly higher in cancer cells comparing to fibrocystic breast disease cells (p=, )
Summary
Matrix metalloproteinases (MMPs) belong to a family of zinc-dependent extracellular endopeptidase capable of degrading most components of the extracellular matrix ( ). MMPs are proteolytic enzymes known to play an important role in tumour development, in tumour cell survival ( ), and in cancer dissemination ( ). Being an MMP inhibitor, TIMP- is capable of protecting against excessive degradation of the extracellular matrix rendering the dissemination of cancer cells difficult ( ). High levels of TIMP- mRNA, as well as, TIMP- protein have been demonstrated in several types of cancer, including breast cancer. This has been associated with a poor prognosis of the patients ( , ). TIMP- is a multifunctional protein, which in addition to the MMP-inhibitory effect has distinct tumour-promoting functions. The aim of our study was to determine immunohistochemically the presence and cellular location, as well as, expression of TIMP- in samples of breast tissue using serial sections
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