Tissue inhibitor of metalloproteinases-3 interacts with angiotensin II type 2 receptor and additively inhibits angiogenesis.

Aim: The tissue inhibitors of metalloproteinases (TIMPs) are complex molecules with both pro- and anti-tumour effects. Thus, their diverse expression could be because of their multifunctional properties with respect to tumour growth, angiogenesis, apoptosis, and other biological functions. Previous data have shown that TIMPs bind tightly to most matrix metalloproteinases, although the pathway that mediates angiostatic activity has not been fully established.

TIMP-1 regulates cell proliferation by interacting with the ninth zinc finger domain of PLZF.

The tissue inhibitors of metalloproteinases (TIMPs) are multifunctional proteins that specifically inhibit matrix metalloproteinases (MMPs) and regulate extracellular matrix (ECM) turnover and tissue remodeling. This is directed by forming tightly bound inhibitory complexes with MMPs. Recent years have revealed important differences of various biological activities between TIMP families but molecular mechanisms are not clear.

A novel cervical cancer suppressor 3 (CCS-3) interacts with the BTB domain of PLZF and inhibits the cell growth by inducing apoptosis.

Promyelocytic leukemia zinc finger protein (PLZF) is a sequence-specific, DNA binding, transcriptional repressor differentially expressed during embryogenesis and in adult tissues. PLZF is known to be a negative regulator of cell cycle progression. We used PLZF as bait in a yeast two-hybrid screen with a cDNA library from the human ovary tissue.

The identification of apoptosis-related residues in human thymosin beta-10 by mutational analysis and computational modeling.

Thymosin beta-10 (TB10) is an actin monomer-sequestering peptide that consists of 43 amino acid residues and that tends to form alpha-helical structures. Previously, we showed that the overexpression of TB10 dramatically increases the frequency of apoptosis in human ovarian cancer cells. To identify the critical residues responsible for TB10-mediated apoptosis, we used a series of computational methods.

IFN-gamma/IRF-1-induced p27kip1 down-regulates telomerase activity and human telomerase reverse transcriptase expression in human cervical cancer.

Telomerase activation is regulated by the expression of human telomerase reverse transcriptase (hTERT) and is a key step in the development of human cancers. Interferon-gamma (IFN-gamma) signaling induces growth arrest in many tumors through multiple regulatory mechanisms. The p27 tumor suppressor protein inhibits the formation of tumors through the induction of cell cycle arrest and/or apoptosis.

Homeobox Msx1 interacts with p53 tumor suppressor and inhibits tumor growth by inducing apoptosis.

The stability of wild-type p53 is critical for its apoptotic function. In some cancers, wild-type p53 is inactivated by interaction with viral and cellular proteins, and restoration of its activity has therapeutic potential. Here, we identify homeobox Msx1 as a p53-interacting protein and show its novel function as a p53 regulator.

The interaction between E-tropomodulin and thymosin beta-10 rescues tumor cells from thymosin beta-10 mediated apoptosis by restoring actin architecture.

Thymosin beta-10 (TB10) is a small G-actin binding protein that induces depolymerization of intracellular F-actin pools by sequestering actin monomers. Previously, we demonstrated that overexpression of TB10 in ovarian tumor cells increased the rate of cell death. As an initial step to define molecular mechanism of TB10-dependent apoptotic process in ovarian tumor cells, we searched a human ovary cDNA library for a novel TB10 binding protein using a yeast two-hybrid system.

Interferon regulatory factor-1 (IRF-1) is a mediator for interferon-gamma induced attenuation of telomerase activity and human telomerase reverse transcriptase (hTERT) expression.

Constitutive activation of the telomerase is a key step in the development of human cancers. Interferon-gamma (IFN-gamma) signaling induces growth arrest in many tumors through multiple regulatory mechanisms. In this study, we show that IFN-gamma signaling represses telomerase activity and human telomerase reverse transcriptase (hTERT) transcription, and suggest that this signaling is mediated by IRF-1.