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gelatinase/rintasyöpä
Linkki tallennetaan leikepöydälle
Sivu 1 alkaen 153 tuloksia
[Zymography--method for quantitation of activity on gelatinase A (pro-MMP-2, 72 kDa) and gelatinase B (pro-MMP-9, 92 kDa) in serum of patients with breast cancer].
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Zymography is an electrophoretic method for measuring proteolytic activity. The method is based on polyacrylamide gels impregnated with a protein substrate (gelatin, casein), which is degraded by the proteases. It is already widely used for research on extracellular matrix degrading enzymes, in
Gelatinase-a/mmp-2 serum levels and neoplastic progression in breast-cancer patients.
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The metastatic potential of cancer cells has been associated to their ability to elaborate and secrete basement membrane degradative enzymes. In this process a major role appears to be played by a protease known as gelatinase A (72 kDa type IV collagenase, MMP-2). In an effort to assess the
Expression and correlation of Twist and gelatinases in breast cancer.
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Altered expression of Twist, matrix metalloproteinase (MMP)-2 and MMP-9 proteins has been identified in various types of human cancers. However, the correlation between Twist and these gelatinases in breast cancer remains unclear. In this study, immunohistochemical analysis of Twist, MMP-2 and MMP-9
Gelatinase levels in male and female breast cancer.
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Breast cancer is a common disease in females but very rare in males, in whom it shows a more metastatic behavior, and a worse prognosis. Matrix metalloprotease-2 (MMP-2) and MMP-9 are proteolytic enzymes balanced by tissue inhibitor of MMP-2 (TIMP-2), commonly involved in cancer metastasis. This is
Expression of tissue inhibitor of metalloproteinase-1 and type IV collagenase/gelatinase messenger RNAs in human breast cancer.
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The relationship between malignant epithelial cell growth and the formation of tumor stroma is poorly understood. To investigate the roles of type IV collagenases/gelatinases and tissue inhibitor of metalloproteinase-1 (TIMP-1) in human breast cancer, we localized their messenger RNAs (mRNAs) in
Gelatinase A, membrane type 1 matrix metalloproteinase, and extracellular matrix metalloproteinase inducer mRNA expression: correlation with invasive growth of breast cancer.
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Invasive breast cancer varies widely in biologic aggressiveness, from fairly indolent tumors to rapidly disseminating carcinomas. Matrix metalloproteinases have enzymatic activity and assist in tumor invasion by degrading basement membranes and extracellular matrix. The extracellular matrix
Plasma gelatinase levels in patients with primary breast cancer in relation to axillary lymph node status, Her2/neu expression and other clinicopathological variables.
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Matrix metalloproteinases (MMPs), in particular the gelatinases MMP2 and MMP9, are important mediators of tumour invasion and metastasis. We examined whether plasma gelatinase levels could predict lymph node metastasis in breast cancer patients. Further, we investigated the relationship of plasma
Neutrophil gelatinase-associated lipocalin protein as a biomarker in the diagnosis of breast cancer: A meta-analysis.
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Neutrophil gelatinase-associated lipocalin (NGAL) has been thought to play an important role in breast cancer tumorigenesis and progression. Various studies have focused on the association between NGAL and breast cancer. The aim of this meta-analysis was to establish the overall accuracy of the NGAL
Differential influence of antiestrogens on the in vitro release of gelatinases (type IV collagenases) by invasive and non-invasive breast cancer cells.
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Matrix metalloproteinases (MMPs) play an important role in tumor cell invasion and cancer metastasis. Accordingly, a higher level of these enzymes has been associated with the invasive phenotype. In the present study the effect of the antiestrogens, Analog II (AII), ICI-182,780 (ICI), and tamoxifen
Gelatinase A expression and localization in human breast cancers. An in situ hybridization study and immunohistochemical detection using confocal microscopy.
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The gelatinase A (72 kDa type IV collagenase) is a matrix metallo-proteinase which degrades basement membrane collagens. Various studies emphasize its role in stromal invasion of cancers, but there is some controversy about its origin. Gelatinase A was localized by immunohistochemistry using
Prognostic significance of stromelysin 3, gelatinase A, and urokinase expression in breast cancer.
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This study was aimed at testing the hypothesis that the expression of proteases essentially produced by reactive stromal cells (stromelysin-3 [ST3], gelatinase A [GELA], and urokinase [uPA]) is predictive of prognosis in patients with breast cancer. This was a study of patients with node-positive
Circulating levels of matrix metalloproteinase-9 (MMP-9), neutrophil gelatinase-associated lipocalin (NGAL) and their complex MMP-9/NGAL in breast cancer disease.
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BACKGROUND
Recent evidence suggests that neutrophil gelatinase-associated lipocalin (NGAL) expression is induced in many types of human cancer, while detection of its complex with matrix metalloproteinase-9 (MMP-9) is correlated with cancer disease status. We aim to evaluate the serum expression of
Neutrophil gelatinase-associated lipocalin (NGAL) is a predictor of poor prognosis in human primary breast cancer.
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Neutrophil gelatinase-associated lipocalin (NGAL) is a small, secreted glycoprotein with proposed functions in cell proliferation, survival and morphogenesis. NGAL is expressed in a variety of tumor types including breast carcinomas, but it is not known whether NGAL contributes directly to breast
The matrix metalloproteinase-9/neutrophil gelatinase-associated lipocalin complex plays a role in breast tumor growth and is present in the urine of breast cancer patients.
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OBJECTIVE
Having previously shown that the binding of neutrophil gelatinase-associated lipocalin (NGAL) to matrix metalloproteinase-9 (MMP-9) protects this extracellular matrix remodeling enzyme from autodegradation, we hypothesized that the addition of NGAL to breast cancer cells, which do not
Role of DDR1 in the gelatinases secretion induced by native type IV collagen in MDA-MB-231 breast cancer cells.
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Discoidin domain receptors (DDRs) are receptor tyrosine kinases that get activated by collagens in its native triple-helical form. In mammalian cells, DDR family consists of two members, namely DDR1 and DDR2, which mediates migration and proliferation of several cell types. DDR1 is activated by
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