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proteinase/rintasyöpä
Linkki tallennetaan leikepöydälle
Sivu 1 alkaen 264 tuloksia
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
SNPs near the cysteine proteinase cathepsin O gene (CTSO) determine tamoxifen sensitivity in ERα-positive breast cancer through regulation of BRCA1.
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Tamoxifen is one of the most commonly employed endocrine therapies for patients with estrogen receptor α (ERα)-positive breast cancer. Unfortunately the clinical benefit is limited due to intrinsic and acquired drug resistance. We previously reported a genome-wide association study that identified
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
A cysteine proteinase secreted from human breast tumours is immunologically related to cathepsin B.
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The stable cathepsin B-like cysteine (thiol) proteinase secreted from human breast tumours in culture was shown to be destabilized by mercurial compounds. After such treatment the enzyme cross-reacts in a radioimmunoassay with a monospecific antiserum to human liver cathepsin B. It is suggested that
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,
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
Proteinase-like peptidase activities and oestrogen receptor levels in breast cancer tissue.
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The relationship between proteinase-like peptidase activities and oestrogen receptor levels and status in breast cancer tissue homogenates from 61 patients with breast cancer has been evaluated. With Spearman's rank-order correlation analysis, significant positive correlations were observed between
Proteinase activity in malignant human breast cancers and NMU mammary tumours of the rat.
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In subcellular fractions of human mammary tumours and NMU tumours of rats proteinase activity was studied by means of the synthetic substrates Bz-dl-arginin-4-nitroanilid (BAPNA) and Bz-dl-arginin-2-naphthyl-amid (BANA). Using the substrate BAPNA enzymatic activity was found to be highest in low
[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
Characterization of a thiol proteinase secreted by malignant human breast tumours.
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It has previously been demonstrated (Poole, A.R., Tiltman, K.J., Recklies, A.D. and Stoker, T.A.M. (1978) Nature 273, 545-547) that malignant human breast tumours maintained in organ culture secrete elevated amounts of a thiol proteinase. This enzyme has been shown to possess enzymic properties
Proteinases as Biomarkers in Breast Cancer Prognosis and Diagnosis.
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BACKGROUND
Breast cancer is the second leading cause of cancer-related deaths among women in the Western World.
METHODS
Upon diagnosis and treatment in the preinvasive state, the five years survival rate levitate up to 93%, making early detection crucial for dedicative diagnosis and treatment.
Expression of proteinases and inhibitors in human breast cancer progression and survival.
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OBJECTIVE
The expression of proteinases and their inhibitors determines the extracellular matrix (ECM) turnover in normal and pathological processes. In cancer, proteolysis is abnormally regulated, favouring ECM degradation, which aids tumour invasion and metastasis. Previous studies have determined
Proteinases and sialyltransferase in human breast tumors.
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Proteolytic and sialyltransferase activities were determined in extracts of 65 human primary breast tumors, 6 lymph node metastases, 6 fibroadenomas and 27 normal tissues. Using proteins and synthetic selective substrates, we observed the presence of collagen-peptidases, plasminogen activator,
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