Proteolysis in human breast and colorectal cancer

Garbett, E A; Reed, Malcolm; Brown, Nicola J.

doi:10.1038/sj.bjc.6690689

Cited by 77 publications

(53 citation statements)

References 32 publications

(35 reference statements)

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“…These observations are consistent with previous observations on active and proform MMP-2 and proMMP-9 (Liabakk et al, 1996). The presence of active MMP-9 has also been described before (Yamagata et al, 1991;Garbett et al, 1999a;Zeng et al, 1999;Baker et al, 2000), but quantitative measurement in all samples had not been reported up until now. Active MMP-2 increases more than its proform in tumour tissue.…”

Section: Molecular and Cellular Pathologymentioning

confidence: 79%

“…To some degree, all show enhanced gelatinase levels in tumour tissue, at least for the latent forms of MMP-2 and MMP-9. However, some studies (Liabakk et al, 1996;Parsons et al, 1998) have not quantified active MMP-9, while others (Garbett et al, 1999a;Zeng et al, 1999;Baker et al, 2000) do not report specific activities but rather the absence or presence of the various enzyme forms. A consistent quantification of both the latent and active forms -and their ratio -of both gelatinases in matched tumour and normal tissue is still lacking.…”

mentioning

confidence: 99%

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Tissue levels of active matrix metalloproteinase-2 and -9 in colorectal cancer

Waas

Lomme

DeGroot³

et al. 2002

Br J Cancer

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The bioactivity of matrix metalloproteinases was studied in tissues from colorectal cancer patients by means of both quantitative gelatin zymography and a fluorometric activity assay. Next to paired samples of tumour tissue and distant normal mucosa (n=73), transitional tissue was analysed from a limited (n=33) number of patients. Broad-spectrum matrix metalloproteinase activity and both the active and latent forms of the gelatinases matrix metalloproteinase-2 and -9 were higher in tumour than in normal mucosa. The ratio's between active and latent forms of matrix metalloproteinase-2 and -9 were highest in tumour tissue and normal mucosa, respectively. Matrix metalloproteinase-2 levels, both active and latent forms, correlated inversely with stage of disease, the tumours without synchronous distant metastases containing significantly (P=0.005) more active matrix metalloproteinase-2 than the others. At much lower levels of activity, the same trend was observed in distant normal mucosa. The level of latent form of matrix metalloproteinase-9 in tumour depended on tumour location. Neither the active form of matrix metalloproteinase-9 nor broad-spectrum matrix metalloproteinase activity in tumour tissue did correlate with any of the clinicopathological parameters investigated. The results demonstrate explicit differences between the activity of matrix metalloproteinase-2 and -9, indicating different roles for both gelatinases in tumour progression. Such data are necessary in order to develop rational anti-cancer therapies based on inhibition of specific matrix metalloproteinases.

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Section: Molecular and Cellular Pathologymentioning

confidence: 79%

mentioning

confidence: 99%

Tissue levels of active matrix metalloproteinase-2 and -9 in colorectal cancer

Waas

Lomme

DeGroot³

et al. 2002

Br J Cancer

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“…MMP-9 (gelatinase B) is over-expressed in both breast and colorectal cancer (Garbett et al, 1999). Of the many identified polymorphisms in the MMP-9 gene, two (a (CA)n microsatellite polymorphism at position -90 and a single nucleotide polymorphism at position -1562) are functionally significant (Shimajiri et al, 1999;Zhang et al, 1999a).…”

Section: Matrix Metalloproteinasesmentioning

confidence: 99%

Role of genetic polymorphisms in tumour angiogenesis

2002

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Angiogenesis plays a crucial role in the development, growth and spread of solid tumours. Pro-and anti-angiogenic factors are abnormally expressed in tumours, influencing tumour angiogenesis, growth and progression. Polymorphisms in genes encoding angiogenic factors or their receptors may alter protein expression and/or activity. This article reviews the literature to determine the possible role of angiogenesis-related polymorphisms in cancer. Further research studies in this potentially crucial area of tumour biology are proposed.

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“…In many pathological conditions, modifications of their expression profile causes the lost of balance in the ECM homeostasis. Several studies demonstrated the association between MMP9 and tumour progression in breast [6][7][8][9], colorectal [9] and prostate cancer [10]. MMP9, also known as gelatinase B, is a 92 kDa type IV collagenase secreted as inactive glycosylated precursor and subsequently activated by the removal of 73 amino acids at the NH 2 terminus.…”

Section: Introductionmentioning

confidence: 99%

“…Among them, TIMP-1 has a selective binding with the pro-MMP-9 and is considered the main inhibitor for MMP-9 [13,15]. The detection of MMP9 expression has been performed in lung cancer by immunohistochemistry [1,7,[15][16][17][18][19], zymography [9,10,18,20], immunoenzymatic assays [21] and Northern analysis [8,15]. Increased plasma levels of MMP-9 protein were also detected in lung cancer patients [22,23].…”

Section: Introductionmentioning

confidence: 99%

Simultaneous measurement of MMP9 and TIMP1 mRNA in human non small cell lung cancers by multiplex real time RT-PCR

et al. 2004

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Summary Extracellular matrix (ECM) homeostasis is strictly maintained by a coordinated balance between the expression of matrix metalloproteinases (MMPs) and their specific inhibitors (TIMPs). Our study was focused on the simultaneous measurement of the expression profile of MMP9 mRNA and its principal inhibitor, TIMP-1, in 100 non small cell lung cancers (NSCLC) and in corresponding adjacent non malignant tissues. The measurement was performed with a multiplex quantitative RT-PCR assay based on TaqMan assay, using two probes labelled with different fluorocromes. We found that both MMP9 and TIMP-1 mRNAs were significantly higher in NSCLC (P < 0.0001) in comparison to corresponding controls as well as the MMP9/TIMP-1 ratio (P = 0.014). MMP9 and TIMP-1 mRNA expression was highly correlated in cancer samples (r = 0.73, P < 0.0001). The analysis in the two main histotypes revealed a significant increase of MMP9 mRNA in adenocarcinomas in comparison to normal tissues (P = 0.006) but not in squamous cell carcinomas, while TIMP-1 mRNA showed a significative increase both in adenocarcinomas and in squamous cell carcinoma samples (P = 0.02 and 0.01, respectively). Both MMP9 and TIMP-1 mRNAs were significantly correlated to lymphnode invasion and cancer stage. Survival analysis revealed that high levels of expression of MMP9 mRNA, but not of TIMP-1, were significantly associated to an unfavourable outcome in NSCLC patients in toto (P = 0.017). In addition our results showed that high levels of MMP9 expression are of independent prognostic impact in operable NSCLC.Our data seem to demonstrate a simultaneous and coordinated up-regulation of MMP9 and TIMP-1 expression at the mRNA level in NSCLC, even if this phenomenon seems variable according to the histotype. In addition, the increase of MMP9/TIMP-1 ratio may reflect an unbalance of their production in affected tissues. The increased expression of the two mRNAs, even not necessarily equate their enzymatic activities, seems to parallel a major cancer aggressiveness.

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Proteolysis in human breast and colorectal cancer

Cited by 77 publications

References 32 publications

Tissue levels of active matrix metalloproteinase-2 and -9 in colorectal cancer

Tissue levels of active matrix metalloproteinase-2 and -9 in colorectal cancer

Role of genetic polymorphisms in tumour angiogenesis

Simultaneous measurement of MMP9 and TIMP1 mRNA in human non small cell lung cancers by multiplex real time RT-PCR

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