Expression and localization of the matrix metalloproteinase pump‐1 (MMP‐7) in human gastric and colon carcinomas

McDonnell, Susan; Navre, Marc; Coffey, Robert J.; Matrisian, Lynn M.

doi:10.1002/mc.2940040617

Cited by 250 publications

(159 citation statements)

References 21 publications

(8 reference statements)

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“…MMP level in carcinoma is identical to that of the gastric mucosa. of plasminogen activators, cathepsins and matrix metalloproteinases in different types of human carcinomas (McDonnell et al, 1991;Yamagata et al, 1991;Duffy, 1992;Matrisian, 1992;Poulsom et al, 1992;Kimura et al, 1993;Zucker et al, 1993;Emmert-Buck et al, 1994;Grigioni et al, 1994;Duffy et al, 1995). In the present study we show that in a majority of gastric carcinomas the MMP-2 and MMP-9 levels are significantly higher than in the corresponding gastric mucosa, irrespective of the activity state of the enzymes.…”

Section: Tissue Extraction and Protein Concentrationmentioning

confidence: 99%

“…This local proteolysis enables tumour cells to penetrate normal surrounding tissue. Immunohistochemical and in situ hybridisation studies in human gastrointestinal neoplasias have shown that these carcinomas contain enhanced amounts of matrix metalloproteinases (McDonnell et al, 1991;Poulsom et al, 1992;Grigioni et al, 1994). The enhanced proteolytic capacity of tumour tissues is confirmed by studying tissue homogenates, using quantitative methods like activity assays, and ELISAs (Yamagata et al, 1991;Kimura et al, 1993;Duffy et al, 1995).…”

mentioning

confidence: 99%

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Tissue levels of matrix metalloproteinases MMP-2 and MMP-9 are related to the overall survival of patients with gastric carcinoma

Sier

Kubben²,

Ganesh³

et al. 1996

Br J Cancer

265

171

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Section: Tissue Extraction and Protein Concentrationmentioning

confidence: 99%

mentioning

confidence: 99%

Tissue levels of matrix metalloproteinases MMP-2 and MMP-9 are related to the overall survival of patients with gastric carcinoma

Sier

Kubben²,

Ganesh³

et al. 1996

Br J Cancer

265

171

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“…Furthermore, the 92 kDa gelatinase is elevated in the plasma of colon cancer patients (Zucker et al, 1993). In a study evaluating stromelysins 1 and 2 and matrilysin (PUMP-1) expression in colorectal cancer, the mRNA of the latter enzyme was expressed in 75% of colon carcinomas, whereas the mRNA of the former was not detected (McDonnell et al, 1991). In a recent study, stromelysin 3 mRNA was overexpressed in primary colorectal adenocarcinomas and liver metastases and expression was shown in stromal fibroblasts adjacent to the neoplastic lesions (Porte et al, 1995).…”

mentioning

confidence: 99%

Therapeutic effect of the matrix metalloproteinase inhibitor, batimastat, in a human colorectal cancer ascites model

Watson

Morris²,

Parsons³

et al. 1996

Br J Cancer

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Summary The matrix metalloproteinase inhibitor batimastat was administered to a human colorectal cancer ascites model, which was initiated by injection of C170HM2 cells into the peritoneal cavity of SCID mice and resulted in solid tumour deposits and ascites formation. The cell line expressed both the 72 and 92 kDa forms of gelatinase by zymography. Batimastat administered from day 0 (40 mg kg-1) reduced the volume of ascites to 21 % of control in mice treated from day 0 (P <0.002) but not day 10. Formation of solid peritoneal deposits was significantly reduced to 77% of vehicle control when batimastat was administered from day 0 (P<0.01) and 69% of control when administered from day 10 (P<0.05). Thus, batimastat has the ability to reduce the volume of ascites forming in SCID mice injected intraperitoneally with the human colorectal cell line, C170HM2, when administered from day 0 but not from day 10. Solid peritoneal tumour deposits were significantly reduced in both treatment groups, highlighting the therapeutic potential of batimastat in this clinical condition.Keywords: metalloproteinase; colorectal cancer; batimastat A large body of evidence now suggests that matrix metalloproteinases (MMPs) play a role in the metastasis of tumour cells (Brown, 1993). Secretion of these enzymes by both normal and malignant cells is in the form of a latent precursor, which is activated by removal of an amino terminal domain (Stetler-Stevenson et al., 1989). These enzymes are implicated in the breakdown of extracellular matrix and vascularisation, which are both critical for successful metastasis, and recent clinical studies have shown MMP to play a role in the spread of human tumour cells Davies et al., 1993).The role of individual enzymes from the MMP family, in both the growth and metastatic spread of colorectal tumours, has been investigated. Activity of type I fibrillar collagenase, a member of the MMP family, has been shown to correlate with histological grade (van der Strappen, 1990). The 72 kDa gelatinase, which breaks down type IV collagenase of basement membrane, correlates with tumour progression, and mRNA studies have revealed the presence of this enzyme in the tissue stroma adjacent to the invasive edge of the cancer (D'Errico et al., 1991; Poulson et al., 1992). The 92 kDa form of gelatinase has been demonstrated by immunocytochemistry to be widespread in colorectal carcinoma, especially in tumours of advanced stage (Jeziorska et al., 1994). In the same study, expression of the enzyme at specific sites in the tumour has been shown to be inversely related to the localisation of type IV collagen. Furthermore, the 92 kDa gelatinase is elevated in the plasma of colon cancer patients (Zucker et al., 1993). In a study evaluating stromelysins 1 and 2 and matrilysin (PUMP-1) expression in colorectal cancer, the mRNA of the latter enzyme was expressed in 75% of colon carcinomas, whereas the mRNA of the former was not detected (McDonnell et al., 1991). In a recent study, stromelysin 3 mRNA was overexpressed in primary col...

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“…A role for MMPs in experimental tumour invasion and metastasis is suggested by a variety of evidence DeClerck et al, 1991;Alexander and Werb, 1992;DeClerck et al, 1992;Cha et al, 1996;Imren et al, 1996). Although there is little direct evidence for MMP function in human tumour spread under in situ conditions, MMP expression is elevated in various human tumours relative to the normal counterpart tissues (McDonnell et al, 1991;Muller et al, 1991Muller et al, , 1993Gray et al, 1992;Pyke et al, 1992;Assam et al, 1993;Majmudar et al, 1994;MacDougall et al, 1995;Murray et al, 1996;Johansson et al, 1997).…”

mentioning

confidence: 99%

Matrix metalloproteinases (MMPs) in fresh human prostate tumour tissue and organ-cultured prostate tissue: Levels of collagenolytic and gelatinolytic MMPs are low, variable and different in fresh tissue versus organ-cultured tissue

et al. 2001

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Summary Prostate tissue was obtained from 22 radical prostatectomies (performed for clinical management of prostate carcinoma) immediately after surgery. A small piece of tissue was fixed immediately in formalin and used for routine histology while a second piece was frozen in OCT and used for immuno-histochemistry. Another small piece was used for isolation of epithelial and stromal cells. The remainder of the tissue was cut into 2 × 2 mm pieces and incubated in organ culture for 8 days. In organ culture, non-malignant, basal epithelial cells underwent a proliferative response. This was accompanied by de-differentiation of glandular structures and by migration of epithelial cells across the surface of the tissue. Erosion of the basement membrane could also be seen in places, but was not widespread. Invasion of epithelial cells into the adjacent stroma was not evident. Production of matrix metalloproteinases (MMPs) with gelatinolytic activity or collagenolytic activity was assessed in organ culture and compared to expression patterns in fresh tissue. MMP-1 (interstitial collagenase) and MMP-9 (92-kDa gelatinase B) were undetectable or low in fresh tissue specimens. Both enzymes were detected in organ culture and both increased over time. Even after 6 days, however, there was only a low level of gelatin-hydrolytic activity and no measurable collagenhydrolytic activity. In past studies we used organ cultures of normal skin and malignant skin tumours (basal cell carcinomas) to help elucidate the role of collagenolytic and gelatinolytic MMPs in epithelial cell invasion (Varani et al, 2000). Compared to MMP levels observed in skin, levels of these enzymes in prostate are low. The low level of collagenolytic and gelatinolytic MMPs in fresh prostate tissue and in organcultured prostate tissue may help explain why there is little tissue destruction in many primary prostate tumours and why the majority of such tumours remain confined to the prostate for extended periods. Although these past studies clearly indicate that several MMPs are elaborated in prostate tumours and suggest differences between malignant and non-malignant tissue, the heterogeneity in prostate tumour presentation and the variability in the analytical methods used make elucidating the relationship between enzyme elaboration and disease-state difficult to ascertain. Furthermore, the presence of active forms of the enzymes has not been established in these studies, and the biological significance of the reported differences is unclear. In the present study, a combination of approaches has been employed to assess expression of collagenolytic and gelatinolytic MMPs in prostate tissue removed for treatment of prostate carcinoma. We report here that gelatinolytic and collagenolytic MMPs can be detected in freshly isolated prostate tissue or in short-term (2-3 day) organ culture. Expression is heterogeneous from tissue to tissue, consistent with the variation in disease presentation. Expression patterns in fresh tissue and organ-cultured tissue also differ. E...

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Expression and localization of the matrix metalloproteinase pump‐1 (MMP‐7) in human gastric and colon carcinomas

Cited by 250 publications

References 21 publications

Tissue levels of matrix metalloproteinases MMP-2 and MMP-9 are related to the overall survival of patients with gastric carcinoma

Tissue levels of matrix metalloproteinases MMP-2 and MMP-9 are related to the overall survival of patients with gastric carcinoma

Therapeutic effect of the matrix metalloproteinase inhibitor, batimastat, in a human colorectal cancer ascites model

Matrix metalloproteinases (MMPs) in fresh human prostate tumour tissue and organ-cultured prostate tissue: Levels of collagenolytic and gelatinolytic MMPs are low, variable and different in fresh tissue versus organ-cultured tissue

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