Enhanced production and activation of matrix metalloproteinase-7 (matrilysin) in human endometrial carcinomas

Ueno, Hideki; Yamashita, Kaname; Azumano, Isao; Inoue, Masakí; Okada, Yasunori

doi:10.1002/(sici)1097-0215(19991022)84:5<470::aid-ijc4>3.0.co;2-d

Cited by 62 publications

(54 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…However, no studies have elucidated the molecular mechanism regulating MMP-7 localization to the basal epithelial compartment or the depolarized diffuse cytoplasmic distribution of MMP-7 in adenocarcinoma cells at the invasive front. Similar to other MMPs such as MMP-2, the activated form of MMP-7 is readily detected within both carcinoma 11,17 and normal intestinal tissues. 6 Our previous in vitro biochemical studies have shown that proMMP-7 is fully activated by treatment with trypsin or MMP-3, and partially with plasmin or leukocyte elastase.…”

mentioning

confidence: 82%

“…Importantly, there is a large difference in the distribution of MMP-7 between adenomas and adenocarcinomas; MMP-7 is predominantly immunolocalized to the apical surface of dysplastic glands of the adenomas, 7 whereas the cytoplasm of carcinoma cells at the invasive front is diffusely immunostained in human gastrointestinal and endometrial carcinomas. 11,14 Thus, the data, together with the broad range of substrate specificity of MMP-7, 3,15 suggest the possibility that different functions of this proteinase under various pathophysiological conditions may be dictated by vectorial secretion of MMP-7. Yu et al 16 have demonstrated that CD44 heparan sulfate proteoglycan (CD44HSPG), which is selectively expressed on the apical site of gland cells, anchors active MMP-7 to the lumenal site of postpartum uterine and lactating mammary gland epithelium in normal mice, but that in CD44 À/À mice MMP-7 is redistributed from the apical to the basal compartment of the epithelia.…”

mentioning

confidence: 98%

“…6 On the other hand, MMP-7 is overexpressed in human adenoma cells of the breast and colon, 7,8 as well as carcinoma cells in the human gastrointestinal, endometrial and lung adenocarcinomas. [9][10][11][12] Thus, MMP-7 is considered to contribute to early tumor development during carcinogenesis. 7 However, since the expression and/or activation of MMP-7 zymogen (proMMP-7) correlates well with invasion and metastases in adenocarcinomas of the stomach, colon and endometrium, 11,13,14 it is likely that MMP-7 is also implicated in cancer progression.…”

mentioning

confidence: 99%

“…[9][10][11][12] Thus, MMP-7 is considered to contribute to early tumor development during carcinogenesis. 7 However, since the expression and/or activation of MMP-7 zymogen (proMMP-7) correlates well with invasion and metastases in adenocarcinomas of the stomach, colon and endometrium, 11,13,14 it is likely that MMP-7 is also implicated in cancer progression. Importantly, there is a large difference in the distribution of MMP-7 between adenomas and adenocarcinomas; MMP-7 is predominantly immunolocalized to the apical surface of dysplastic glands of the adenomas, 7 whereas the cytoplasm of carcinoma cells at the invasive front is diffusely immunostained in human gastrointestinal and endometrial carcinomas.…”

mentioning

confidence: 99%

See 3 more Smart Citations

Pericellular activation of proMMP-7 (promatrilysin-1) through interaction with CD151

Shiomi

Inoki

Kataoka

et al. 2005

Laboratory Investigation

Self Cite

View full text Add to dashboard Cite

Matrix metalloproteinase-7 (MMP-7) (also known as matrilysin-1) is secreted as a proenzyme (proMMP-7) and plays a key role in the degradation of various extracellular matrix (ECM) and non-ECM molecules after activation. To identify the binding proteins related to proMMP-7 activation, a human lung cDNA library was screened by yeast two-hybrid system using proMMP-7 as bait. We identified a candidate molecule CD151, which is a member of the transmembrane 4 superfamily. Complex formation of proMMP-7 with CD151 was demonstrated by immunoprecipitation of the molecules from CaR-1 cells, a human rectal carcinoma cell line, expressing both proMMP-7 and CD151, and CD151 stable transfectants incubated with proMMP-7. Yeast twohybrid assays using deletion mutants of proMMP-7 and CD151 suggested an interaction between the propeptide of proMMP-7 and the COOH-terminal extracellular loop of CD151. The binding activity of 125 I-labeled proMMP-7 to CD151 on the cell membranes was shown with CD151 stable transfectants. Laser-scanning confocal microscopy demonstrated that proMMP-7 colocalizes with CD151 on the cell membranes of CD151 stable transfectants and CaR-1 cells. In situ zymography using crosslinked carboxymethylated transferrin, a substrate of MMP-7, demonstrated proteinase activity on and around CD151 stable transfectants and CaR-1 cells, while the activity was abolished by their treatment with MMP inhibitors, anti-MMP-7 antibody or anti-CD151 antibody. In human lung adenocarcinoma tissues, colocalization of MMP-7 and CD151 was demonstrated on the carcinoma cells. Metalloproteinase activity was present in these tissues and could be inhibited by antibodies to MMP-7 or CD151. These data demonstrate for the first time that proMMP-7 is captured and activated on the cell membranes through interaction with CD151, and suggest the possibility that similar to the MT1-MMP/MMP-2 system, MMP-7 is involved in the pericellular activation mechanism mediated by CD151, a crucial step in proteolysis on the cell membranes under various pathophysiological conditions including cancer invasion and metastasis.

show abstract

mentioning

confidence: 82%

mentioning

confidence: 98%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Pericellular activation of proMMP-7 (promatrilysin-1) through interaction with CD151

Shiomi

Inoki

Kataoka

et al. 2005

Laboratory Investigation

Self Cite

View full text Add to dashboard Cite

show abstract

“…Many laboratories have shown that MMPs are overexpressed in cancers and play an important role in cancer invasion and metastases (25)(26)(27). In particular, MMP7 is upregulated in endometrial, gastric, and colorectal cancers, and the MMP7 activity correlates with vascular invasion and metastases (28)(29)(30). Thus, MMPs that mediate the cleaving of FasL could be expressed on the tumor cells and/or present within the ocular and hepatic environment.…”

Section: Discussionmentioning

confidence: 99%

Control of Ocular Tumor Growth and Metastatic Spread by Soluble and Membrane Fas Ligand

et al. 2007

View full text Add to dashboard Cite

Fas ligand (FasL) can be either membrane bound, or cleaved by metalloproteinases (MMP) to produce a soluble protein.The two different forms of FasL are reported to have opposite functions-membrane-bound FasL (mFasL) is proinflammatory and soluble FasL (sFasL) is antiinflammatory. We previously showed that, within the immune-privileged eye, tumors expressing high levels of mFasL overcame the suppressive ocular environment, triggered an inflammatory response, and were subsequently rejected. By contrast, eye tumors expressing low levels of mFasL grew progressively. To evaluate the effect of sFasL on the tumor growth and metastatic potential of ocular FasL-expressing tumors, we compared tumor cell clones that expressed equal amounts of (low) mFasL in the presence or absence of sFasL. Tumor cells transfected with a modified FasL gene expressed only mFasL (noncleavable), grew progressively within the eye, and induced systemic protective immunity that prevented metastatic spread of tumor cells to the liver. Unexpectedly, tumors transfected with wild-type FasL (wtFasL; cleavable), which could produce both sFasL and mFasL, elicited considerably more inflammation and grew more slowly within the eye. However, the cleavable wtFasL eye tumors failed to trigger protective immunity and gave rise to liver metastases. Interestingly, exposure to the ocular environment was required for the wtFasL tumors to gain metastatic potential. We conclude that the fate of FasL-expressing tumors is determined by a combination of the following: (a) the relative proportion of membrane and sFasL, and (b) the local environment that determines the extent of FasL cleavage.

show abstract

HIV-1 Tat neurotoxicity is prevented by matrix metalloproteinase inhibitors

et al. 2001

View full text Add to dashboard Cite

Enhanced production and activation of matrix metalloproteinase-7 (matrilysin) in human endometrial carcinomas

Cited by 62 publications

References 24 publications

Pericellular activation of proMMP-7 (promatrilysin-1) through interaction with CD151

Pericellular activation of proMMP-7 (promatrilysin-1) through interaction with CD151

Control of Ocular Tumor Growth and Metastatic Spread by Soluble and Membrane Fas Ligand

HIV-1 Tat neurotoxicity is prevented by matrix metalloproteinase inhibitors

Contact Info

Product

Resources

About