Mammary carcinoma cells over‐expressing tissue inhibitor of metalloproteinases‐1show vascular endothelial growth factor expression

@article{Yoshiji1998MammaryCC,
  title={Mammary carcinoma cells over‐expressing tissue inhibitor of metalloproteinases‐1show vascular endothelial growth factor expression},
  author={Hitoshi Yoshiji and Steven R. Harris and Erzsebet Raso and Daniel Eduardo Gomez and Carol K. Lindsay and Masabumi Shibuya and C C Sinha and Unnur P. Thorgeirsson},
  journal={International Journal of Cancer},
  year={1998},
  volume={75}
}
The tissue inhibitor of metalloproteinases‐1 (TIMP‐1) has at least 2 independent functions, i.e., regulation of matrix metalloproteinases and erythroid‐potentiating activity. We investigated the effects of TIMP‐1 over‐expression on tumor growth, using cloned lines derived from a TIMP‐1‐transfected rat breast carcinoma cell line. The in vitro growth rate of the TIMP‐1‐transfected clones was indistinguishable from that of the control. In contrast, the highest TIMP‐1‐producing clone (159.0 ng/ml… Expand
Tissue inhibitor of metalloproteinases‐1 (TIMP‐1) inhibits tumor growth and angiogenesis in the TIMP‐1 transgenic mouse model
TLDR
Results suggested that the ectopically overexpressed TIMP‐1 inhibited the tumor growth by angiogenesis suppression, and this effect was not due to cytotoxicity. Expand
High levels of tissue inhibitor of metalloproteinase‐1 predict poor outcome in patients with breast cancer
TLDR
It is concluded that in human breast cancer, endogenous TIMP‐1 does not inhibit tumor progression but may enhance the process, contrary to what might be expected from published data on model systems. Expand
Tissue inhibitor of metalloproteinases‐1 promotes liver fibrosis development in a transgenic mouse model
TLDR
Transgenic mice overexpressing human TIMP‐1 in the liver under control of the albumin promoter/enhancer suggest that TIMP•1 does not by itself result in liver fibrosis, but strongly promotes Liver fibrosis development. Expand
Bcl‐2 overexpression in melanoma cells increases tumor progression‐associated properties and in vivo tumor growth
TLDR
The data suggest that bcl‐2 plays a pivotal role in the regulation of molecules associated with the migratory and invasive phenotype, contributing, in cooperation to hypoxia, to tumor progression. Expand
TIMP-1 Overexpression in Lung Carcinoma Enhances Tumor Kinetics and Angiogenesis in Brain Metastasis
TLDR
Results indicate tumor-promoting functions of TIMP-1 through alterations in angiogenesis, increased tumorigenicity, and invasive behavior are indicated. Expand
Tissue Inhibitor of Metalloproteinases-1 Stimulates Gene Expression in MDA-MB-435 Human Breast Cancer Cells by Means of its Ability to Inhibit Metalloproteinases
TLDR
A complex action of TIMP-1 on cancer cells mediated by constitutively active cell surface metalloproteinases that release factors regulating cell signaling pathways may account for the paradoxical observation that elevated levels of TIMp-1 in tumors can correlate with an adverse prognosis. Expand
Tissue inhibitor of metalloproteinases‐1 attenuates spontaneous liver fibrosis resolution in the transgenic mouse
TLDR
TIMP‐1 significantly attenuated spontaneous resolution of liver fibrosis by the combination of a net reduction of the MMP activity and suppression of apoptosis in HSC. Expand
Stimulatory effect of endogenous tissue inhibitor of metalloproteinases-1 (TIMP-1) overexpression on type IV collagen and laminin gene expression in rat mammary carcinoma cells.
TLDR
This is the first report to show an association between overexpression of TIMP-1 and increased tumor BM matrix production through stimulation of type IV collagen and laminin gene expression. Expand
The matrix metalloproteinase stromelysin-1 acts as a natural mammary tumor promoter
TLDR
By altering the cellular microenvironment, stromelysin-1 can act as a natural tumor promoter and enhance cancer susceptibility. Expand
TIMP-1 Alters Susceptibility to Carcinogenesis
TLDR
The combined implications of these studies suggest that TIMP-1 is an important contributor to epithelial neoplastic progression and supports the concept that TIMp-1 exerts differential regulation on tissues in a stage-dependent manner. Expand
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References

SHOWING 1-10 OF 27 REFERENCES
Enhanced RNA expression of tissue inhibitor of metalloproteinases‐1 (TIMP‐1) in human breast cancer
TLDR
The up‐regulation of TIMP‐1 expression in breast cancer may suggest that TIMp‐1 has an additional role to that of metalloproteinase inhibitor. Expand
Tissue inhibitor of metalloproteinase 1 is a negative regulator of the metastatic ability of a human gastric cancer cell line, KKLS, in the chick embryo.
TLDR
Data indicate that a reduced expression of TIMP-1 in KKLS cells is responsible for their consequent metastatic potential, and suggests that matrix metalloproteinase enzymatic activities are a prerequisite for metastatic activity in this experimental model system. Expand
Targeted disruption of the tissue inhibitor of metalloproteinases gene increases the invasive behavior of primitive mesenchymal cells derived from embryonic stem cells in vitro
TLDR
Using a basement membrane invasion assay, it was found that the mutant cells, differentiated in low concentrations of serum with retinoic acid, were more invasive than their normal cell counterparts, and that this was specifically reversed by adding exogenous TIMP-1 protein. Expand
Growth‐promoting activity of tissue inhibitor of metalloproteinases‐1 (TIMP‐1) for a wide range of cells A possible new growth factor in serum
Human tissue inhibitor of metalloproteinases‐1 (TIMP‐1), but not TIMP‐2, has potent growth‐promoting activity for a wide range of human and bovine cells, TIMP‐1 seems to be a new cell‐growth factorExpand
Tissue inhibitor of metalloproteinases-1 (TIMP-1) RNA is expressed at elevated levels in malignant non-Hodgkin's lymphomas.
TLDR
The data suggest the importance of tumor-stromal interactions in non-Hodgkin's lymphomas, and indicate a possible relationship between high-level, localized expression of TIMP-1 and the malignant phenotype of high-grade advanced-stage lymphomas. Expand
Cell cycle-dependent localization of tissue inhibitor of metalloproteinases-1 immunoreactivity in cultured human gingival fibroblasts.
TLDR
Results suggest a localization of TIMP-1 or a related substance in the nucleus of proliferating human fibroblasts, and its depletion from the nucleus due to an arrest of cell growth. Expand
Metalloproteinase inhibition and erythroid potentiation are independent activities of tissue inhibitor of metalloproteinases-1.
TLDR
It is shown that the antiproteolytic and growth factor activities of the TIMP-1 molecule are physically and functionally distinct. Expand
Targeted mutagenesis of Timp-1 reveals that lung tumor invasion is influenced by Timp-1 genotype of the tumor but not by that of the host.
TLDR
Timp-1 expression in tumorigenic cells could either increase or decrease tumor invasion of lungs in a tumor cell-specific manner, suggesting that depending on the tumor, Timp-1 can either suppress or potentiate metastasis. Expand
Inhibition of angiogenesis by tissue inhibitor of metalloproteinase
TLDR
Using an in vivo angiogenesis assay, the endothelial cell response to known angiogenic factors, basic fibroblast growth factor and adipocyte conditioned medium, was blocked by an inhibitor of matrix metalloproteinase activity, TIMP‐1. Expand
Inhibition by human recombinant tissue inhibitor of metalloproteinases of human amnion invasion and lung colonization by murine B16-F10 melanoma cells.
TLDR
The inhibition of lung colonization in C57BL/6 mice by rTIMP is one of the first examples showing an antimetastatic effect of a selective metalloproteinase inhibitor in a mammalian animal model, and supports an essential role for metalliproteinase(s) in the extravasation and invasion of tumor cells during lung colonization by blood-borne tumor cells. Expand
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