The distribution of matrix metalloproteinases and tissue inhibitor of metalloproteinases in colorectal cancer

Gallegos, Nicolas; Smales, Caroline; Savage, F; Hembry, Rosalind M.; Boulos, PB

doi:10.1016/s0960-7404(10)80027-1

Cited by 30 publications

(17 citation statements)

References 31 publications

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“…Gallegos et al 21 described immunohistochemical staining of MMP-2 and -9 in colorectal cancers in surrounding stroma cells which is consistent to our findings. Poulsom et al undertook in situ hybridisation studies to detect MMP-2 and TIMP-2 in 12 colorectal carcinomas.…”

Section: Discussionsupporting

confidence: 93%

“…Levels of inactive proforms of MMP-2 did not differ between normal and malignant urothelium, but the activated MMP-2 levels were higher in malignant tissues. 25 An increased level of MMPs could be demonstrated in colorectal cancer, 21,26 in breast cancer, 22 skin cancers like melanoma 27 and many others.…”

Section: Discussionmentioning

confidence: 99%

“…MMP-2 is predominantly inhibited by TIMP-2 17 and TIMP-4, 18 while MMP-9 is inhibited mainly by TIMP-1. 19 An imbalance between MMPs and TIMPs expression was shown in recent studies to be connected with a variety of different tumours, for example, lung, 20 colon, 21 breast 22 and prostate. 23 In the present study, the expression of MMP-2 and -9, and TIMP-1 and -2 in prostate cancer tissue was examined using immunohistochemical methods.…”

Section: Introductionmentioning

confidence: 99%

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Expression of matrix metalloproteinases (MMP-2 and -9) and their inhibitors (TIMP-1 and -2) in prostate cancer tissue

Brehmer

Biesterfeld²,

Jakse

2003

Prostate Cancer Prostatic Dis

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Matrix metalloproteinases (MMPs) have been implicated in progression and metastases of different tumours. The balance between the MMPs and their natural inhibitors (tissue inhibitors of matrix metalloproteinases; TIMP) seems to be an important factor related to this role. Here, the expression of MMP-2 and -9 along with TIMP-1 and -2 was examined in prostate cancer tissue. A total of 40 radical prostatectomy specimens were embedded in paraffin and immunohistochemical staining was performed to detect MMP-2 and -9, and TIMP-1 and -2. The immunoreactivity was assessed semiquantitively using routine light microscopy. The intensity of staining was correlated to preoperative PSA, T category, Gleason score and clinical parameters of the specimens. The imbalance of MMPs and TIMPs was recognised as a significant loss of TIMP-1 in malignant epithelium and an upregulation of MMPs. Palpable tumours (T2, T3) expressed significantly more MMP-2 and significantly less MMP-9 than T1c tumours. Our data are in accordance with other literature reports in that an imbalance of MMPs and TIMPs is found in malignant tumours. The observed imbalance of MMP and TIMP is mainly caused by a loss of TIMP-1. Furthermore, palpable tumours demonstrated significantly more MMP-2 and significantly less MMP-9 expression than nonpalpable tumours.

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Section: Discussionsupporting

confidence: 93%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Expression of matrix metalloproteinases (MMP-2 and -9) and their inhibitors (TIMP-1 and -2) in prostate cancer tissue

Brehmer

Biesterfeld²,

Jakse

2003

Prostate Cancer Prostatic Dis

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“…Few studies have determined MMP-1 or MMP-3 expression in either breast (Polette et al, 1993;Heppner et al, 1996;Remacle et al, 1998) or colorectal cancer (Matrisian et al, 1994;Gallegos et al, 1995;Murray et al, 1996), and no study has compared the expression of these MMPs in both tissues. Latent MMP-3 alone was expressed by a greater proportion of breast samples than colorectal.…”

Section: Discussionmentioning

confidence: 99%

Proteolysis in human breast and colorectal cancer

1999

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Summary Proteolysis occurs when proteinase activity exceeds inhibitor activity. Proteolysis is normally tightly regulated and is involved in cancer invasion and metastasis. The aim of this study was to compare proteolysis in breast and colorectal cancer. Proteinase and inhibitor expression were analysed in paired tumour and normal tissue samples from 43 breast and 24 colorectal cancer patients using substrate zymography, Western blotting and quenched fluorescence substrate hydrolysis. The expression of the latent forms of matrix metalloproteinase-2 (MMP-2), MMP-3 and MMP-9, urokinase plasminogen activator (uPA), tissue inhibitor of metalloproteinase-1 (TIMP-1) and TIMP-2 expression were observed in both tumour and normal tissue samples from breast and colorectal tissue; however, expression was greater in the tumour tissue. Expression of active MMP-2 and MMP-9 and the total MMP activity were greater in tumour compared to normal samples in both tissues (P < 0.05). The expression of all proteinases and total MMP activity was greater in colorectal tissue than breast tissue samples. Breast and colorectal cancer demonstrated different proteinase profiles, however proteolysis in both tissues was greater in tumour tissue than normal tissue.

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“…Their role in malignancy is highlighted by the number of cancers that have elevated MMP levels, including breast (Basset et al, 1990), prostatic (Pajouh et al, 1991), gastric (Nomura et al, 1995), ovarian (Campo et al, 1992), pancreatic (Gress et al, 1995;Bramhall et al, 1997), and colorectal disease (Hewitt et al, 1991;Gallegos et al, 1995). This led to great interest in development of MMP inhibitors as potential tumour-control agents.…”

mentioning

confidence: 99%

Elevated serum matrix metalloproteinase 9 (MMP-9) concentration predicts the presence of colorectal neoplasia in symptomatic patients

et al. 2007

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Early detection of polyps or colorectal carcinoma can reduce colorectal carcinoma-associated deaths. Previous studies have demonstrated raised serum levels of matrix metalloproteinase 9 (sMMP-9) in a range of cancers. The aim of this study was to investigate the role of sMMP-9 levels in identifying colorectal neoplasia. Consenting patients donated a blood sample and were assessed by proforma-led history and physical examination. Samples were analysed for sMMP-9 concentration (enzyme-linked immuno-sorbant assay) and compared to final diagnoses. Logistic regression modelling determined independent factors associated with neoplasia. A total of 365 patients were recruited of whom 300 were analysed, including 46 normal controls. A total of 27 significant adenomas and 63 malignancies were identified. The median sMMP-9 concentration was 443ng ml À1 (IQR: 219 -782; mean: 546). Patients with neoplasia had significantly elevated sMMP-9 levels (Po0.001). Logistic regression modelling identified elevated log(sMMP-9) as the most significant predictor of neoplasia (w 2 ¼ 38.33, Po0.001). Other significant factors were age, sex, smoking history, abdominal pain and weight loss. The model accurately predicted neoplasia in 77.3% of cases. Sensitivity and specificity were 77.9 and 77.1%. sMMP-9 estimation can accurately stratify patient to low-or high-risk cohorts. Serum sampling is a potential means of avoiding unnecessary colonoscopy and reducing patient anxiety, iatrogenic morbidity and mortality, and cost.

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The distribution of matrix metalloproteinases and tissue inhibitor of metalloproteinases in colorectal cancer

Cited by 30 publications

References 31 publications

Expression of matrix metalloproteinases (MMP-2 and -9) and their inhibitors (TIMP-1 and -2) in prostate cancer tissue

Expression of matrix metalloproteinases (MMP-2 and -9) and their inhibitors (TIMP-1 and -2) in prostate cancer tissue

Proteolysis in human breast and colorectal cancer

Elevated serum matrix metalloproteinase 9 (MMP-9) concentration predicts the presence of colorectal neoplasia in symptomatic patients

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