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Stran 1 iz 363 rezultatov
Perturbation of the heparin/heparin-sulfate interactome of human breast cancer cells modulates pro-tumourigenic effects associated with PI3K/Akt and MAPK/ERK signalling.
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Heparansulfate-proteoglycans (HSPGs) interact via their polyanionic heparansulfate (HS) side chains with a variety of proteins on the cell surface or within the extracellular matrix membrane. The large number of heparin/HS binding proteins form a highly interconnected functional network, which has
[Mast cell infiltration of the stroma and free heparin in the blood in breast cancer].
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The study included mast cell content assay in breast cancer stroma, free blood heparin measurement and its variation versus treatment and disease outcome. In clinically unfavorable cases, tumors displayed equal levels of mast cells whatever treatment procedure (surgery, chemotherapy + surgery).
Heparin/heparan sulfate interacting protein expression and functions in human breast cancer cells and normal breast epithelia.
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Heparin/heparan sulfate interacting protein (HIP) is a recently identified protein expressed by many normal epithelia and epithelial cell lines. In the present study, we examined expression and potential functions of this protein in a series of human breast cancer cells and in sections of normal and
Effect of Decapeptyl (a GnRH analogue) and of transforming growth factor-alpha (TGF-alpha), in the presence of heparin, on the sulfatase activity of human breast cancer cells.
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The effects of the polypeptide Decapeptyl (a gonadotropin-releasing hormone (GnRH) agonist analogue) and of transforming growth factor-alpha (TGF-alpha), on estrone sulfate-sulfatase activities in the homogenates of various breast cancer cell lines were studied in the presence of heparin. In
A heparin-binding growth factor secreted from breast cancer cells homologous to a developmentally regulated cytokine.
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We report purification of an 18-kDa heparin-binding growth factor secreted from human cancer cells which is homologous to a developmentally regulated, neurotrophic factor, heparin-binding growth-associated molecule/pleiotrophin (HB-GAM/PTN; Merenmies, J., and Rauvala, H. (1990) J. Biol. Chem. 265,
Delivery of AIB1 siRNA by Ca2+/PEI/heparin composite nanoparticles effectively inhibits the growth of human breast cancer.
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Here, a novel carrier fabricated by the interaction of negatively charged heparin and positively charged PEI and Ca2+ was investigated to deliver AIB1 siRNA into breast cancer cells both in vitro and in vivo. Ca2+/PEI/heparin nanoparticles were prepared by simply mixing
Heparins modulate the IFN-γ-induced production of chemokines in human breast cancer cells.
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Heparins seem to improve survival in patients with advanced malignancies independently of their anticoagulatory function. As the treatment options in advanced and metastatic breast cancer are still very limited, heparins might be an interesting addition to the existing systemic therapies. The
Fatal massive and recurring pulmonary embolism followed by thrombocytopenia developed after heparin and warfarin treatment in a patient with metastatic breast cancer with an incidental large right atrial thrombus.
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A thromboembolic complication such as pulmonary embolism in patients who had cancer and mobile thrombi in the heart is a rare but fatal complication. Surgical thromboembolectomy is considered as the classical treatment of choice. In case of inoperable patient, catheter-directed therapy may be an
Molecular hierarchy of heparin-binding EGF-like growth factor-regulated angiogenesis in triple-negative breast cancer.
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Heparin-binding EGF-like growth factor (HB-EGF) is one of several proangiogenic factors and represents a possible therapeutic target for patients with triple-negative breast cancer (TNBC). However, the role of HB-EGF in promoting tumor aggressiveness in TNBC remains unclear. To investigate specific
Heparin-binding domain, type 1 and type 2 repeats of thrombospondin mediate its interaction with human breast cancer cells.
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Thrombospondin is an adhesive glycoprotein that promotes breast cancer cell adhesion to human vascular endothelial cells (Incardona et al., 1995). In this study, we have identified the molecular domains of thrombospondin that mediate its binding to specific receptors on the human breast
Alteration of integrins by heparin-binding EGF-like growth factor in human breast cancer cells.
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The adhesion of cancer cells to the vascular endothelium is an important step in the hematogenous metastasis of cancer. Human breast cancer cells adhere to human umbilical vein endothelial cells (HUVECs) through the interaction of E selection on HUVECs and the carbohydrate ligand sialyl Lewisx on
Heparin-like polysaccharides reduce osteolytic bone destruction and tumor growth in a mouse model of breast cancer bone metastasis.
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TGF-β regulates several steps in cancer metastasis, including the establishment of bone metastatic lesions. TGF-β is released from bone during osteoclastic bone resorption and it stimulates breast cancer cells to produce osteolytic factors such as interleukin 11 (IL-11). We conducted a cell-based
Heparin-based hydrogel scaffolding alters the transcriptomic profile and increases the chemoresistance of MDA-MB-231 triple-negative breast cancer cells.
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The tumor microenvironment plays a critical role in the proliferation and chemoresistance of cancer cells. Growth factors (GFs) are known to interact with the extracellular matrix (ECM) via heparin binding sites, and these associations influence cell behavior. In the present study, we demonstrate
Low molecular weight heparin-based reduction-sensitive nanoparticles for antitumor and anti-metastasis of orthotopic breast cancer.
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Tumor metastasis has become a major obstacle for the clinical treatment of malignant breast cancer. Thus, a delivery system capable of both antitumor and anti-metastasis efficacy is desired. In this work, a low molecular weight heparin (LMWH)-based reduction-sensitive delivery system was developed,
Heparin-Binding Epidermal Growth Factor-Like Growth Factor as a Potent Target for Breast Cancer Therapy.
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Heparin-binding epidermal growth factor-like growth factor (HB-EGF) belongs to the EGF family and exhibits its activity after binding to its receptors in autocrine, paracrine, and juxtacrine interactions. HB-EGF plays important roles in several biological and pathological processes, such as wound
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