glioma/protease

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Ubiquitin-specific protease 22 acts as an oncoprotein to maintain glioma malignancy through deubiquitinating B cell-specific Moloney murine leukemia virus integration site 1 for stabilization.

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Ubiquitin-specific protease 22 (USP22) is a member of the "death-from-cancer" signature, which plays a key role in cancer progression. Previous evidence has shown that USP22 is overexpressed and correlates with poor prognosis in glioma. The effect and mechanism of USP22 in glioma malignancy,

The glioma cell-derived neurite promoting activity protein is functionally and immunologically related to human protease nexin-I.

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Protease nexin-I (PN-I, Mr approximately 43,000) is representative of a newly described class of cell-secreted protease inhibitors. PN-I has been purified to apparent homogeneity, partially sequenced, and monospecific antibodies have been raised against it. PN-I is a potent inhibitor of urokinase,

Inhibition of drug-induced DNA fragmentation, but not cell death, of glioma cells by non-caspase protease inhibitors.

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The role of non-caspase protease activation in drug-induced cell death of glioma cells was examined. Neither calpain inhibitors I or II, phenylmethylsulfonyl fluoride (PMSF), Nalpha -p-tosyl-L-lysine chloromethyl ketone (TLCK), N-tosyl-L-phenylalanine chloromethyl ketone (TPCK), E64, leupeptin nor

Expression of cysteine protease inhibitors in human gliomas and meningiomas.

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Increased levels of human cysteine proteases have been implicated in the progression of tumors from the premalignant to the malignant state. The physiological activities of these proteases are regulated by their interactions with specific inhibitors. To our knowledge there have been no previous

Inhibition of tissue factor/protease-activated receptor-2 signaling limits proliferation, migration and invasion of malignant glioma cells.

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Tissue factor (TF) is upregulated in several malignant diseases, including gliomas. Here, we demonstrate pronounced differences in the expression of TF and its interactors factor VII and protease-activated receptor 2 (PAR-2) in nine human glioma cell lines (U87, U251, U343, U373, MZ-18, MZ-54,

Secretion of protease nexin-1 by C6 glioma cells is under the control of a heterotrimeric G protein, Go1.

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Heterotrimeric Go proteins have recently been described as regulators of vesicular traffic. The Goalpha gene encodes, by alternative splicing, two Goalpha polypeptides, Go1alpha and Go2alpha. By immunofluorescence and electron microscopy, we detected Go1alpha on the membrane of small intracellular

Protease inhibitors generate cytotoxic fragments from Alzheimer amyloid protein precursor in cDNA-transfected glioma cells.

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A human glioma cell line (Bu-17) was stably transfected with full-length cDNA encoding beta/A4 amyloid protein precursor (APP). When the transfectants were treated with protease inhibitors (leupeptin, E-64, and antipain) and the lysosomotropic agent chloroquine, aberrantly processed fragments of APP

Proteases and the biology of glioma invasion.

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Despite optimal clinical treatment, the prognosis for malignant gliomas remains poor. One of the primary reasons for treatment failure is not diffuse dissemination, but local invasion. Recently, there has been an increase in information regarding specific molecules that determine the aggressiveness

A protease storm cleaves a cell-cell adhesion molecule in cancer: multiple proteases converge to regulate PTPmu in glioma cells.

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Cleavage of the cell-cell adhesion molecule, PTPµ, occurs in human glioblastoma multiforme brain tumor tissue and glioma cell lines. PTPµ cleavage is linked to increased cell motility and growth factor independent survival of glioma cells in vitro. Previously, PTPµ was shown to be cleaved by furin

Role of Protease-Activated Receptor-1 in Glioma Growth.

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Activation of a thrombin receptor, protease-activated receptor-1 (PAR-1), induces angiogenesis, cell proliferation, and invasion in tumors. The present study examined the effect of host PAR-1 gene deletion on glioma growth in a mouse model. F98 glioma cells were implanted into the right caudate of

Protease activated receptor-1 and brain edema formation in glioma models.

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OBJECTIVE Our previous studies showed that thrombin contributes to brain edema in gliomas. The present study investigated the role of a thrombin receptor, protease activated receptor-1 (PAR-1), in edema formation in glioma models. METHODS These experiments were performed in Fischer 344 rats, PAR-1

Relevance of IGFBP2 proteolysis in glioma and contribution of the extracellular protease ADAMTS1.

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Expression of IGFBP2 (Insulin-like Growth Factor Binding Protein 2) has been positively correlated with glioma progression. Although the proteolysis of IGFBP2 has been widely recognized, with consequences as a major modulator of IGFII signaling, the relevance of this post-translational modification

Ubiquitin-specific protease 22: a novel molecular biomarker in glioma prognosis and therapeutics.

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Ubiquitin-specific protease 22 (USP22) exhibits an important function in tumor progression and oncogenesis. The aim of this study was to investigate the role of USP22 and the association with its potential targets in patients with glioma. To our knowledge, this is the first study that determines the

Targeting the cytotoxicity of fusogenic membrane glycoproteins in gliomas through protease-substrate interaction.

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Fusogenic membrane glycoproteins (FMG) are potent therapeutic transgenes with potential utility in the gene therapy of gliomas. FMG expression constructs caused massive syncytia formation followed by cytotoxic cell death in glioma cell lines, and antitumor activity has been shown in glioma

Anti-miRNA-23a oligonucleotide suppresses glioma cells growth by targeting apoptotic protease activating factor-1.

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BACKGROUND Abnormal expression of microRNAs (miRNAs) is closely related to glioma, which is one of the most common malignant brain tumors. The current study is to identify the key miRNAs involved in the pathogenesis of glioma and to discover novel therapeutic targets for this disease. METHODS Total

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