Increased plasma MMP-2 protein expression in lymph node-positive patients with colorectal cancer

Langenskiöld, Marcus; Holmdahl, Lena; Falk, Peter; Ivarsson, Marie‐Louise

doi:10.1007/s00384-004-0667-4

Cited by 81 publications

(45 citation statements)

References 19 publications

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“…This tendency is opposite to the results of Angenete et al who revealed that plasma levels of MMP-2 were higher in CRC patients with distant metastases [28]. However, our findings are in accordance with the study of Langenskiöld et al who found that plasma MMP-2 in CRC patients with T4 tumors was lower than in T3 and T2 subgroups [29]. The decrease of serum MMP-2 and TIMP-2 in more advanced tumor stages might reflect formation of MMP-TIMP complexes in colorectal tumor progression.…”

Section: Discussionsupporting

confidence: 62%

Matrix metalloproteinase 2 and tissue inhibitor of matrix metalloproteinases 2 in the diagnosis of colorectal adenoma and cancer patients.

Groblewska¹,

Mroczko²,

Gryko³

et al. 2011

Folia Histochem Cytobiol.

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Abstract:The aim of the study was to assess the importance of the measurement of matrix metalloproteinase 2 (MMP-2) and tissue inhibitor of matrix metalloproteinases 2 (TIMP-2) in patients with colorectal cancer (CRC) in relation to clinicopathological features of tumor and patients' survival. Additionally, we determined serum MMP-2 and TIMP-2 in colorectal adenoma (CA) patients and healthy controls and compared them with tumor markers, CEA and CA 19-9. The serum levels of MMP-2 and TIMP-2 in 91 CRC patients, 28 CA subjects and 91 healthy controls were determined by ELISA method, but concentrations of CEA and CA 19-9 using MEIA method. Nonparametric statistical analyses were used. Serum levels of MMP-2 and TIMP-2 were significantly lower in CRC patients than in healthy subjects and decreased with tumor stage. Additionally, MMP-2 concentrations were significantly lower in patients with CRC than in CA group. Diagnostic sensitivity of TIMP-2 (59%) was the highest among biomarkers tested and increased in combined use with CEA (79%). Moreover, the area under ROC curve (AUC) of TIMP-2 was larger than AUC of MMP-2 in differentiation between CRC and healthy subjects, but lower than AUC of matrix metalloproteinase 2 in differentiation between colorectal cancer and adenoma. Our findings suggest clinical usefulness of TIMP-2 as a biomarker in the diagnosis of CRC, especially in combination with CEA. However, further investigation is necessary.

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Section: Discussionsupporting

confidence: 62%

Matrix metalloproteinase 2 and tissue inhibitor of matrix metalloproteinases 2 in the diagnosis of colorectal adenoma and cancer patients.

Groblewska¹,

Mroczko²,

Gryko³

et al. 2011

Folia Histochem Cytobiol.

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“…[10][11][12][13][16][17][18][19] Moreover, our data indicated that conversion of the pro-form of MMP-9 to its active form, as represented by the ratio of the active MMP-9 to proMMP-9, was higher in tumour tissue. Although this finding was consistent with the majority of the studies mentioned above in which this ratio was investigated, Waas et al 11 and Moran et al 19 reported greater increases in the proform of MMP-9 than its active form during tumour progression in contrast to our finding.…”

Section: Discussionmentioning

confidence: 73%

Matrix metalloproteinase‐9,‐3 and tissue inhibitor of matrix metalloproteinase‐1 in colorectal cancer: relationship to clinicopathological variables

İşlekel

Oktay

Terzi

et al. 2006

Cell Biochemistry & Function

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The balance between matrix metalloproteinases (MMPs) and their physiological tissue inhibitors of matrix metalloproteinases (TIMPs) is crucial in tumour invasion and progression. The aim of this study was to investigate the levels of MMP-9, MMP-3 and TIMP-1 in colorectal cancer (CRC) and to evaluate these proteinases and their inhibitor with respect to clinicopathological variables. Activities of pro- and active MMP-9 were measured in paired tumour and distant normal tissue specimens from 43 patients with CRC using gelatin zymography. ELISA was employed for the determination of MMP-9, MMP-3 and TIMP-1 protein expressions. The activity levels of pro- and active MMP-9 and protein expression levels of MMP-9, MMP-3 and TIMP-1 were higher in tumour tissues than in the corresponding normal tissues; the differences being significant for all (p < 0.05), except TIMP-1. Similarly, active MMP-9/proMMP-9 and the ratio of protein expression level of MMP-9-TIMP-1 were found to be significantly higher in tumour tissues ( p < 0.01). Among all the clinicopathological variables investigated, significant correlations were found between MMP-9 and presence of perineural invasion, MMP-3 and lymph node status, TIMP-1 and tumour differentiation, MMP-9/TIMP-1 ratio and histological types ( p < 0.05). In conclusion, MMP-3 was not as notably increased as MMP-9 in tumour tissues. However, different roles may be attributed to MMP-9 and MMP-3 in CRC development and progression. Additionally, assessment of TIMP-1 in relation to MMPs appeared to be crucial in CRC studies to provide a basis for the re-evaluation of the clinical usefulness of TIMP-1 in colorectal cancer.

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“…Increased MMP-2, -9, -13 and decreased TIMP-1 was found to be significantly different between the patients with and without metastasis in prostate cancer (22). MMP-1, -2, -3, -7, -9 were elevated in colorectal cancers (23,24). Furthermore, Moran et al showed that a decrease in the MMP inhibitor TIMP-1 correlated with a poor outcome in colorectal cancer patients (24).…”

Section: Discussionmentioning

confidence: 99%

Matrix metalloproteinase expression in high grade soft tissue sarcomas

et al. 2007

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Abstract. Soft tissue sarcomas comprise a heterogeneous group of mesenchymal tumors with varying biological behavior ranging from indolent tumors with no or minimal metastatic risk to aggressive and frequently metastasizing tumors. Among the more common aggressive adult soft tissue sarcomas are malignant fibrous histiocytoma, synovial sarcoma and liposarcoma. Matrix metalloproteinases are enzymes which perform a homeostatic role in mesenchymal tissue and function in both tumorigenesis and metastasis. The objectives of this study are to determine the presence and relative quantity of matrix metalloproteinases (MMPs) -1, -2, -8, -9, and -13; extracellular matrix metalloproteinase inducer (EMMPRIN); and tissue inhibitors of matrix metalloproteinases (TIMP)-1 and -2 in high grade soft tissue sarcoma tumor specimens using real-time PCR. The second objective is to determine if a relationship exists between quantity of EMMPRIN, MMPs, and TIMPs expressed in tumor tissue and disease-free survival. One hundred and forty patients diagnosed with high grade soft tissue sarcomas between 1995-2003 were identified. Tissue blocks and histologic slides were acquired for 41 specimens. Tumor specimens included 29 malignant fibrous histiocytomas, 3 liposarcomas and 11 synovial sarcomas. RNA was extracted and RT-PCR was performed in triplicate. No significant differences were found between the three types of high grade soft tissue sarcomas studied and the expression of MMPs. Interestingly, no relationship was found between high or low levels of MMPs when compared with disease-free survival. Our data support other research which finds variable correlation between MMP expression in soft tissue sarcomas and disease-free survival. We assert that the difference in correlation between MMP expression in carcinomas and sarcomas and disease-free survival is based on the vast phenotypic and genotypic difference between the cells of origin.

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Increased plasma MMP-2 protein expression in lymph node-positive patients with colorectal cancer

Cited by 81 publications

References 19 publications

Matrix metalloproteinase 2 and tissue inhibitor of matrix metalloproteinases 2 in the diagnosis of colorectal adenoma and cancer patients.

Matrix metalloproteinase 2 and tissue inhibitor of matrix metalloproteinases 2 in the diagnosis of colorectal adenoma and cancer patients.

Matrix metalloproteinase‐9,‐3 and tissue inhibitor of matrix metalloproteinase‐1 in colorectal cancer: relationship to clinicopathological variables

Matrix metalloproteinase expression in high grade soft tissue sarcomas

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