proteinase inhibitor/cancer mamar

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Proteinase inhibitors reduce basement membrane degradation by human breast cancer cell lines.

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The relative importance of different proteinases, and their inhibition, in the breakdown of human endothelial basement membrane (BM) by MDA-MB-231 and MCF7ADR human breast cancer cell lines has been studied using 35S-labelled BM-coated 96-well culture plates. Basement membrane degradation (BMD) was

Demonstration of cysteine proteinase inhibitors ACPI and NCPI in breast cancer and in cell lines MCF-7 and ZR-75-1.

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The samples of breast cancer and cell lines MCF-7 and ZR-75-1 were tested for the occurrence of cysteine proteinase inhibitors ACPI and NCPI. Further, the influence of estradiol on the expression of these inhibitors was examined. Both the tested inhibitors were found in tumor cells and in cell

Cysteine proteinase inhibitor cystatin A in breast cancer.

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Cystatin A (acid cysteine proteinase inhibitor; ACPI) is a natural inhibitor of cysteine proteinases. It has been suggested that an inverse correlation exists between cystatin A and malignant progression. We wanted to assess the biological and clinical significance of cystatin A in infiltrative

Suppression of breast cancer growth and metastasis by a serpin myoepithelium-derived serine proteinase inhibitor expressed in the mammary myoepithelial cells.

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A serpin was identified in normal mammary gland by differential cDNA sequencing. In situ hybridization has detected this serpin exclusively in the myoepithelial cells on the normal and noninvasive mammary epithelial side of the basement membrane and thus was named myoepithelium-derived serine

Low concentrations of the soy phytoestrogen genistein induce proteinase inhibitor 9 and block killing of breast cancer cells by immune cells.

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The risks and benefits of diets and supplements containing the estrogenic soy isoflavone genistein are not well established. We report that 10 nm genistein potently induces the granzyme B inhibitor, proteinase inhibitor 9 (PI-9) in MCF-7 human breast cancer cells. By inducing PI-9, genistein

[alpha 1-proteinase inhibitor in breast cancer].

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Level of alpha 1-proteinase inhibitor (alpha 1-Pi) and antitryptic activity in blood serum were assessed in 167 patients with breast cancer and 30 cases of benign lesions. An increase in blood serum-alpha 1-Pi level was shown to be associated with tumor advancement but could not be regarded as a

Tumor tissue concentrations of the proteinase inhibitors tissue inhibitor of metalloproteinases-1 (TIMP-1) and plasminogen activator inhibitor type 1 (PAI-1) are complementary in determining prognosis in primary breast cancer.

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The purpose of this study was to investigate the association between tumor tissue levels of total tissue inhibitor of metalloproteinases-1 (TIMP-1) and prognosis in patients with primary breast cancer and to analyze whether measurement of TIMP-1 in tumor extracts added prognostic information to that

Demonstration of proteinase inhibitors cystatin A, B and C in breast cancer and in cell lines MCF-7 and ZR-75-1.

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Polyclonal rabbit antibodies to endogenous natural inhibitors of cysteine proteinases (cystatins) were used for their immunohistochemical demonstration in samples of breast cancers and in two breast cancer derived cell lines (MCF-7 and ZR-75-1). The influence of estrogen stimulation on the

The analysis of estrogen receptor-α positive breast cancer stem-like cells unveils a high expression of the serpin proteinase inhibitor PI-9: Possible regulatory mechanisms.

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Breast cancer stem cells seem to play important roles in breast tumor recurrence and endocrine therapy resistance, although the underlying mechanisms have not been well established. Moreover, in some tumor systems the immunosurveillance failure against cancer cells has been related to the presence

Identification, cloning, and characterization of cystatin M, a novel cysteine proteinase inhibitor, down-regulated in breast cancer.

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A novel human cystatin gene was identified in a differential display comparison aimed at the isolation of transcriptionally regulated genes involved in invasion and metastasis of breast cancer. Messenger RNAs from primary and metastatic tumor cells isolated from the same patient were compared. A

[Comparative study of the activity of proteinase inhibitors in mononuclear cells isolated from the blood of healthy women and patients with breast cancer].

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Human breast-cancer cells stimulate the fusion, migration and resorptive activity of osteoclasts in bone explants.

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A central event in bone resorption is the recruitment of osteoclasts to future resorption sites. Breast-cancer cells invariably metastasise to the skeleton and induce extensive bone destruction by osteoclasts. However, our understanding of the mechanisms by which cancer cells interact with

Invasiveness of transformed human breast epithelial cell lines is related to cathepsin B and inhibited by cysteine proteinase inhibitors.

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The activities'of the lysosomal cysteine proteinases cathepsin B and L are regulated by their endogenous inhibitors, stefins A and B, and cystatin C, and their imbalance may be associated with increased invasiveness and development of the malignant cell phenotype. The aim of this study was to

Inhibition of proteinase-like peptidase activities in serum and tissue from breast cancer patients.

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The inhibitory profiles of several proteinase-like peptidases active on synthetic peptide (MCA) substrates, present in sera and 100,000g supernatants of malignant tissue from patients with breast cancer, have been studied using a series of known inhibitors including epoxysuccinyl peptides (E-64,

Pregnancy-Associated Plasma Protein-A, Alpha-2-Macroglobulin, Pregnancy Zone Protein and Their Complexes with IgG in Sera of Healthy Non-Pregnant and Pregnant Woman, and Patients with Breast Cancer.

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The purpose of this study was to measure alpha-2-macroglobulin-IgG (alpha(2)-MG-IgG), pregnancy zone protein-IgG (PZP-IgG) and pregnancy-associated plasma protein-A-IgG (PAPP-A-IgG) complex concentrations in serum in comparison with total alpha(2)-MG, PZP and PAPP-A concentration, and to determine

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