Differential regulation of TIMP-1 and TIMP-2 mRNA expression in normal and Ha-ras-transformed murine fibroblasts

Leco, Kevin J.; Hayden, Lawrence J.; Sharma, Rajesh; Rocheleau, Hélène; Greenberg, Arnold H.; Edwards, Dylan R.

doi:10.1016/0378-1119(92)90731-4

Cited by 92 publications

(50 citation statements)

References 29 publications

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“…Although some studies indicate that TIMP-2 expression tends to be similar in tumors and matched normal tissues (Stetler-Stevenson et al, 1990), others have found a signi®cant correlation between TIMP-2 expression and the development of distant metastases (Ree et al, 1997). Unlike TIMP-1, TIMP-2 expression is downregulated by TGF-b1 and is una ected by serum and phorbol esters, each of which increase TIMP-1 expression (Leco et al, 1992).…”

Section: Timps May Promote and Suppress Carcinogenesis By Distinct Mementioning

confidence: 99%

The matrix metalloproteinase stromelysin-1 acts as a natural mammary tumor promoter

2000

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Extracellular matrix-degrading matrix metalloproteinases (MMPs) are invariably upregulated in epithelial cancers and are key agonists in angiogenesis, invasion and metastasis. Yet most MMPs are secreted not by the cancer cells themselves, but by stromal cells within and around the tumor mass. Because the stromal environment can in¯uence tumor formation, and because MMPs can alter this environment, MMPs may also contribute to the initial stages of cancer development. Several recent studies in MMP-overexpressing and MMP-de®cient mice support this possibility, but have required carcinogens or pre-existing oncogenic mutations to initiate tumorigenesis. Here we review the spontaneous development of premalignant and malignant lesions in the mammary glands of transgenic mice that express an autoactivating form of MMP-3/stromelysin-1 under the control of the whey acidic protein gene promoter. These changes were absent in nontransgenic littermates and were quenched by co-expression of a human tissue inhibitor of metalloproteinases-1 (TIMP-1) transgene. Thus by altering the cellular microenvironment, stromelysin-1 can act as a natural tumor promoter and enhance cancer susceptibility.

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Section: Timps May Promote and Suppress Carcinogenesis By Distinct Mementioning

confidence: 99%

The matrix metalloproteinase stromelysin-1 acts as a natural mammary tumor promoter

2000

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“…Following transformation, bacteria were grow on LB agar containing 50 μg/ml ampicillin and colonies were transferred to nylon filters (Hybond N, Amersham). Filters were hybridized with a mixture of [ 32 P]dCTP-labelled Timp-1, Timp-2, and Timp-3 cDNA probes [19,21,22] and washed as previously described [19]. Dried filters were exposed to XAR5 X-ray film (Eastman Kodak).…”

Section: Isolation Of Murine Timp-4 Cdnasmentioning

confidence: 99%

“…Comparison of predicted amino acid sequences of mouse TIMPs. The sequences used for comparison include TIMP-1 [21,28] (these sequences are identical and differ at nine positions from another mouse TIMP-1 sequence in [29]); TIMP-2 [30], chosen in preference to [22] as there are two differences (H and E at positions 12 and 195) in which the chosen mouse sequence shows a better match with human TIMP-2; TIMP-3 [19]. The shaded areas represent 75% identity.…”

Section: 1mentioning

confidence: 99%

Murine tissue inhibitor of metalloproteinases—4 (Timp—4): cDNA isolation and expression in adult mouse tissues¹

et al. 1997

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We have isolated cDNA clones corresponding to a new member of the murine tissue inhibitor of metalloproteinase (TIMP) family, designated Timp-4. The nucleotide sequence predicts a protein of 22 609 Da that contains the characteristic 12 cysteine TIMP signature. TIMP-4 is more closely related to TIMP-2 and TIMP-3 than to TIMP-1 (48%, 45% and 38% identity, respectively). Analysis of Timp-4 mRNA expression in adult mouse tissues indicated a 1.2 kb transcript in brain, heart, ovary and skeletal muscle. This pattern of expression distinguishes Timp-4 from other Timps, suggesting that the TIMP-4 protein may be an important tissue-specific regulator of extracellular matrix remodelling.

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“…Changes in the relative levels and molar ratios of TIMPs and the MMPs are implicated in normal and pathological processes such as cancer, which involve connective tissue remodelling or degradation (Leco et al, 1992). Currently, it is thought that differential regulation of these genes might be achieved, in part, by various cytokines and growth factors, which allow responsive elements to either cooperate with or antagonise each other to modulate the expression of these genes (Leco et al, 1992).…”

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confidence: 99%

“…Currently, it is thought that differential regulation of these genes might be achieved, in part, by various cytokines and growth factors, which allow responsive elements to either cooperate with or antagonise each other to modulate the expression of these genes (Leco et al, 1992). For example, there is a multiplicity of agents found to stimulate tissue inhibitor of matrix metalloproteinase1 (TIMP-1) expression in a variety of normal and malignant cell cultures.…”

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confidence: 99%

A novel IL-10 signalling mechanism regulates TIMP-1 expression in human prostate tumour cells

Wang

Stearns

2003

Br J Cancer

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We have previously reported that interleukin 10 (IL-10) signalling stimulated activation of a specific enhancer element, termed HTE-1, to promote tissue inhibitor of matrix metalloproteinase1 (TIMP-1) expression in human bone metastatic PC-3 subclone (PC-3 ML) cells. Recently, we have identified an IL-10 responsive signal molecule, termed IL-10E1, which binds the HTE-1 element and cloned the gene encoding for the 22 kDa protein. In this paper, we have examined the mechanism of IL-10/IL-10 receptor signalling in two distinct human prostate cell lines, a 'normal' prostate epithelial cell line, termed NPTX-1532 and highly metastatic PC-3 ML tumour cells. Signalling cascade studies revealed that IL-10 stimulated tyrosine phosphorylation of JAK1 and TYK2 receptor kinases and tyrosine phosphorylation of IL-10E1. Phosphorylation, triggered IL-10E1's rapid translocation to the nucleus by 10 -30 min. Deletion analysis combined with transient transfection experiments revealed that the n-terminal domain (B74 a.a.) of the IL-10E1 protein, the nt-nls peptide, was stimulated by IL-10 to translocate to the nucleus and induce TIMP-1 expression. Site-directed mutagenesis further showed that phosphorylation of two tyrosine moieties (Y57 and Y62) of the nt-nls peptide was required for IL-10 activation of signalling and TIMP-1 expression. The data demonstrate, for the first time, that IL-10 receptor signalling of TIMP-1 expression is regulated by tyrosine phosphorylation of a novel gene, IL-10E1, in human prostate cells.

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Differential regulation of TIMP-1 and TIMP-2 mRNA expression in normal and Ha-ras-transformed murine fibroblasts

Cited by 92 publications

References 29 publications

The matrix metalloproteinase stromelysin-1 acts as a natural mammary tumor promoter

The matrix metalloproteinase stromelysin-1 acts as a natural mammary tumor promoter

Murine tissue inhibitor of metalloproteinases—4 (Timp—4): cDNA isolation and expression in adult mouse tissues¹

A novel IL-10 signalling mechanism regulates TIMP-1 expression in human prostate tumour cells

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Differential regulation of TIMP-1 and TIMP-2 mRNA expression in normal and Ha-ras-transformed murine fibroblasts

Cited by 92 publications

References 29 publications

The matrix metalloproteinase stromelysin-1 acts as a natural mammary tumor promoter

The matrix metalloproteinase stromelysin-1 acts as a natural mammary tumor promoter

Murine tissue inhibitor of metalloproteinases—4 (Timp—4): cDNA isolation and expression in adult mouse tissues1

A novel IL-10 signalling mechanism regulates TIMP-1 expression in human prostate tumour cells

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Murine tissue inhibitor of metalloproteinases—4 (Timp—4): cDNA isolation and expression in adult mouse tissues¹