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astrocytoma/protease
Ο σύνδεσμος αποθηκεύεται στο πρόχειρο
Σελίδα 1 από 99 Αποτελέσματα
General protease and collagenase (IV) activity in C6 astrocytoma cells, C6 spheroids and implanted C6 spheroids.
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Σύνδεση εγγραφή
Tumor growth is dependent on the ability of neoplastic cells to induce angiogenesis. Remodelling of blood vessels requires reconstruction of the collagen (type IV) and non-fibrous protein components of basement membrane. This study assessed the general protease and collagenase (IV) activities of C6
Inhibition of SUMO-specific protease 1 induces apoptosis of astroglioma cells by regulating NF-κB/Akt pathways.
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SUMO-specific protease 1 (SENP1) is an important regulation protease in the protein desumoylation, which was shown to have a prooncogenicrole in many types of cancer. However, the mechanism of action for SENP1 in astrocytoma is not yet clear. Astrocytoma is the most frequent one among various
Guanidinobenzoatase and UPA in high-grade human astrocytomas and after xenografting cell suspensions into the rat cerebral cortex: proteases for metastasis and disease progression.
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BACKGROUND
Invasion and metastasis is aided by the secretion of guanidinobenzoatase, that cleaves the link peptide to fibronectin, and urokinase plasminogen activator (uPA), which initiates a molecular cascade to activate plasmin and collagenases. This process permits malignant cell migration
Experimental validation of deuterium oxide-mediated antitumoral activity as it relates to apoptosis in murine malignant astrocytoma cells.
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OBJECTIVE
Deuterium oxide (D2O), or heavy water, affects a variety of biological activities different from those of water. The authors examined the antitumoral effect of D2O on brain neoplasms and demonstrated D2O-mediated cytotoxicity by using a Rous sarcoma virus-induced murine malignant
Lobar pilocytic astrocytomas of the cerebral hemispheres: II. Pathobiology--morphogenesis of the eosinophilic granular bodies.
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This study provides new immunocytochemical observations on the so-called eosinophilic granular bodies (EGBs), seen predominantly (but not exclusively) in pilocytic astrocytomas. Using combined immunohistochemical and immunoelectron microscopic approaches on formalin-fixed, paraffin-embedded tissues,
Serum proteolytic activity during the growth of C6 astrocytoma.
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Tumor growth is dependent on the ability of neoplastic cells to induce angiogenesis. Blood-vessel remodeling requires the reconstruction of the nonfibrous proteins and type IV collagen components of the basement membrane. This study has assessed the influence of the growth of C6 astrocytoma cells in
Proteolytic activity during the growth of C6 astrocytoma in the murine spheroid implantation model.
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General protease and collagenase IV activity are involved in the remodelling of the vascular basement membrane that occurs during tumor-induced angiogenesis. This study has assessed the level of these enzymes in tumor, peritumoral or contralateral cerebral cortex tissue during the growth of C6
Detection of cathepsin S cysteine protease in human brain tumour microdialysates in vivo.
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Microdialysis enables the chemistry of extracellular fluid in body tissues to be measured. Extracellular proteases such as the cysteine protease, cathepsin S (CatS), are thought to facilitate astrocytoma invasion. Microdialysates obtained from human brain tumours in vivo were subjected to cathepsin
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
Activity of cysteine protease inhibitors in human brain tumors.
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BACKGROUND
Cysteine proteases (mainly cathepsins B and L) are thought to play an important role in the progress of cancer, including brain tumors. Together with other proteases, they hydrolyze the extracellular matrix and basement membrane proteins, thus enabling the tumor to grow and spread.
Low density lipoprotein receptor related protein gene amplification and 766T polymorphism in astrocytomas.
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Low density lipoprotein receptor related protein (LRP) is a receptor for protease complexes, and may function in cell growth and repair, and in tumor invasiveness. LRP expression increases in glioblastomas compared to lower grade astrocytomas. Two potential mechanisms for this increased expression
Epidermal growth factor and pro-inflammatory cytokines regulate the expression of components of plasminogen activation system in U373-MG astrocytoma cells.
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Cytokines and growth factors that influence both secretion of the extracellular matrix (ECM) proteins and migration of the cells decide about the final outcome of tissue remodelling. We have examined expression of the components of the plasminogen activation system in human astrocytoma U373-MG cells
An extracellular proteasome-like structure from C6 astrocytoma cells with serine collagenase IV activity and metallo-dependent activity on alpha-casein and beta-insulin.
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An extracellular proteasome-like (EP) structure has been isolated from serum-free media conditioned by C6 astrocytoma cells. EP has a native molecular mass of 1000 kDa and is composed of three subunits, two isoelectric variants at 70 kDa and one at 65 kDa. The extracellular proteasome degraded
Interferon gamma up-regulates alpha 2 macroglobulin expression in human astrocytoma cells.
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An established human astrocytoma cell line (T67) was shown to constitutively produce the proteinase inhibitor alpha 2 macroglobulin (alpha 2M). Interferon gamma (IFN gamma), a potent immunoregulatory lymphokine, was able to increase the synthesis of alpha 2M by these cells, as measured by ELISA on
Extracellular osmolarity modulates G protein-coupled receptor-dependent ATP release from 1321N1 astrocytoma cells.
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We previously reported that ATP release from 1321N1 human astrocytoma cells could be stimulated either by activation of G protein-coupled receptors (GPCR) or by hypotonic stress. Cheema et al. (Cheema TA, Ward CE, Fisher SK. J Pharmacol Exp Ther 315: 755-763, 2005) have demonstrated that thrombin
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