Objective: The aim of our study was to identify a combination of markers whose expression is predictive of invasion and metastasis of colorectal carcinoma. Method: The expression of E-cadherin, β-catenin, tenascin C, KAI-1, epidermal growth factor receptor (EGFR) and vascular endothelial growth factor (VEGF) was studied immunohistochemically and correlated clinicopathologically in 72 primary colorectal carcinoma cases (26 with metastatic lymph nodes). 17 patients (24 %) developed haematogenous metastases at median 6,5 months postoperatively (3-11). Results: Expression of following markers significantly correlated with depth of tumour invasion: cytoplasmic accumulation of E-cadherin (p=0,035), nuclear staining for β-catenin (p=0,03), increased tenascin C expression (p=0,001), and loss of EGFR and VEGF expression (p=0,015 and 0,02, respectively). Decreased tenascin C and KAI-1 expression associated with the presence of lymph node metastases (p= 0,027 and 0,046, respectively). Weak cytoplasmic E-cadherin expression correlated with distant metastases (p=0,045). Conclusion: Our results suggest that abnormal expression of proteins involved in cell adhesion and migration (E-cadherin, βcatenin, tenascin C, EGFR) and angiogenesis (VEGF) may be related to the invasion of colorectal carcinoma. Detecting the expression of E-cadherin, tenascin C and KAI-1 probably possesses clinical significance in evaluating lymph node and distant metastasis and predicting the prognosis of colorectal cancer. Objective: In colorectal adenocarcinomas (CRCs) microsatellite instability (MSI) can be documented by immunohistochemical detection of mismatch repair proteins (MMR). The aim of the present study is to identify the percentage of MSI-positive CRCs, in the Epirus region of Greece and compare it to the international data. Method: A total of 50 cases of sporadic CRCs, 25 adenomas and 10 hyperplastic polyps, formalin-fixed paraffinembedded, were examined immunohistochemically using standard methods (En Vision system), with the antibodies MLH1 (Clone ES05), MSH6 (Clone PU29) and PMS2 (Clone M0R4G) (Novocastra-Menarini). Immunostained sections were evaluated semi-quantitatively, taking in account the percentage of neoplastic positive cells and estimating nuclear staining intensity, compared to the internal positive controls (normal epithelium, lymphocytes). Results: All hyperplastic polyps and adenomas expressed the examined MMR. Two out of 50 CRCs were negative for MSH6 and PMS2, while one of them was also negative for MLH1. Interestingly, one of these two CRCs had an adjacent adenoma, which also showed negative staining for MSH6 and PMS2. Conclusion: Immunohistochemical staining for MMR is possible in archival material. Loss of MMR varies, depending on the protein examined. In CRCs from the Epirus region the estimated loss of at least two MMR is 4 %. Objective: Matrix metalloproteinases (MMPs) are a family of zinc-dependent neutral endopeptidases collectively capable of degrading essentially all extracellular matrix (ECM) components. Genetic alterations in MMP-2 and MMP-9 have been implicated to play an important role in colorectal carcinogenesis (CRC). The aim of this study was to investigate the hypothetic correlations between the MMP-2 and 9 mRNA expression and the clinicopathologic variables of the CRC. Method: The expression of MMP-2 and -9 mRNA was assayed by RT-PCR for 53 Tunisian sporadic colorectal adenocarcinomas. Results: MMP-2 was highly expressed in the 53 cases. MMP-9 was not detected in 18 cases and moderately or highly expressed in 35 cases. Absence of MMP-9 mRNA expression was significantly related to an advanced tumoral invasion stage (pT3) (p=0.003). Conclusion: Our study suggests that the overexpression of MMP-2 could be the result of an imbalance in the system of transcriptional regulation of MMP-2, which would involve the loss of expression or activity of its inhibitor: TIMP-2. A variable expression of transcripts of MMP-9 could be explained by the hypothesis of hypermethylation of the promoter or degradation of its transcript after protein translation.