muramidase and Glioma

This study has developed a chitosan-based delivery system to locally administer ellagic acid for brain cancer treatment. We fabricated chitosan/ellagic acid composite films with various concentrations of ellagic acid. In vitro release study was performed by using a UV spectrophotometer, and enzymatic degradation rate was determined by analyzing the increased free amino groups. Viability of brain cancer cells (human U87 glioblastomas and rat C6 glioma cells) was measured via direct and indirect cell culture on the films by MTS assay. Caspase-3 activation, Western blot for p53, and anti-angiogenesis assays were also examined. In the in vivo study, GFP-tagged rat C6 glioma cells were implanted subcutaneously at the right flank region of nude mice and treatments were initiated by implanting the films subcutaneously. Tumor growth was evaluated by measuring tumor volume using a caliper, an ultrasound machine, and an optical imaging system. The chitosan/ellagic acid composite films were enzymatically degradable and exhibited a sustained slow release of ellagic acid. These materials could inhibit the cancer cell growth in an ellagic acid concentration-dependent manner by inducing apoptosis of cancer cells as well as suppressing angiogenesis. These materials also significantly suppressed tumor tissue growth in vivo.

Topics: Animals; Biocompatible Materials; Blotting, Western; Caspase 3; Cell Line, Tumor; Cell Proliferation; Cell Survival; Chitosan; Drug Screening Assays, Antitumor; Ellagic Acid; Enzyme Activation; Female; Glioma; Humans; Mice; Mice, Nude; Muramidase; Neovascularization, Physiologic; Rats; Tumor Suppressor Protein p53

The chicken lysozyme (cLys) locus has been shown to contain all of the cis-elements necessary for position-independent and tissue-specific expression entirely within a 24-kb region defined by general DNase I sensitivity and flanked by matrix attachment regions. As such, it has been viewed as an example of a functional chromatin domain, which is structurally and functionally isolated from neighbouring chromatin. We report here the identification and characterisation of the chicken glioma-amplified sequence (cGas41) locus, which though widely expressed, is contained entirely within the lysozyme chromatin domain. The cGas41 transcript encodes a putative transcription factor, starts 207 bp downstream of the cLys polyadenylation site and is preceded by a CpG island with proposed dual promoter/origin function. The location and differential expression of cGas41 compels re-evaluation of the accumulated literature on the lysozyme domain, and represents an example of two unrelated, differentially expressed vertebrate genes coexisting in the same functional chromatin domain.

Topics: Amino Acid Sequence; Animals; Avian Proteins; Base Sequence; Cell Line; Chickens; Chromatin; CpG Islands; Gene Expression Profiling; Gene Order; Genetic Linkage; Glioma; Humans; Molecular Sequence Data; Muramidase; Organ Specificity; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger; Transcription Factors

Antisera to alpha 1-antichymotrypsin, alpha 1-antitrypsin and lysozyme were reacted with 20 cases of glioblastoma multiforme, seven anaplastic astrocytomas, eight astrocytomas, six oligodendrogliomas, four ependymomas and the cerebral cortex from six normal autopsy brains. In addition, two pleomorphic xantho-astrocytomas and two heavily lipidized malignant gliomas were similarly examined. All astrocytic lesions were confirmed with anti-GFAP antisera. Thirty astrocytic tumours (77%), four oligodendrogliomas (67%) and three ependymomas (75%) reacted positively with anti-alpha 1-antichymotrypsin; 25 astrocytic tumours (64%), three oligodendrogliomas (50%) and three ependymomas (75%) showed positive staining for alpha 1-antitrypsin. The pattern of staining with either of these two markers did not correlate with tumour grading. None of the gliomas examined stained positively with anti-lysozyme. Non-neoplastic glial elements did not react with any of the three antisera. The results of this study suggest that staining for alpha 1-antichymotrypsin and alpha 1-antitrypsin is of little value in the differential diagnosis of neuroepithelial or mesenchymal lesions in the brain.

Topics: Adolescent; Adult; Aged; Aged, 80 and over; alpha 1-Antichymotrypsin; alpha 1-Antitrypsin; Biomarkers, Tumor; Brain Neoplasms; Child; Female; Glioma; Humans; Immunohistochemistry; Male; Middle Aged; Muramidase

The expression of glial fibrillary acidic protein, fibronectin (FN), factor VIII-related antigen (FVIII/RAG), and of three monohistiocytic markers, lysozyme, alpha-1-antitrypsin and alpha-1-antichymotrypsin was examined in five gliosarcomas (GS) by peroxidase-antiperoxidase immunostaining of formalin-fixed and paraffin-embedded specimens, and compared with vascular changes in 16 glioblastomas (GB). In contrast to GB, endothelial proliferations of GS were sheathed by sarcomatous tissue (perivascular sarcoma), which was contiguous with fibrosarcomatous areas. Cells with conspicuous intracytoplasmic FN content (FN+ cells) were seen in the vascular stroma of GB and dominated in the sarcomatous parts of GS. Most FN+ cells of GS were of varying size and shape and clearly neoplastic. Monohistiocytic markers were demonstrable in small infiltrating mononuclear cells as well as in many sarcomatous cells including FN+ cells. FVIII/RAG was restricted to lumen-lining endothelium and was not found in sarcomatous cells. These results suggest that a major part of sarcoma in GS is less likely to develop from proliferated endothelial cells than from histiocytic cells in the perivascular spaces of GB. By FN mediation, histiocytic cells might also guide and promote sarcomatous proliferations of other mesenchymal cells, leading to fibrosarcomatous development. Prominent monstrous giant cells of one GS seemed to be degenerating glioma cells.

Topics: Adult; Antigens; Brain Neoplasms; Cell Division; Chymotrypsin; Factor VIII; Fibronectins; Glial Fibrillary Acidic Protein; Glioma; Histiocytes; Humans; Male; Middle Aged; Muramidase; Neoplasm Proteins; Trypsin; von Willebrand Factor

Topics: Astrocytoma; Brain Neoplasms; Ependymoma; Glioma; Humans; Muramidase; Neoplasm Metastasis; Pituitary Neoplasms

The presence of lysozyme in the CSF is considered with regard to its value in the early diagnosis of primary or secondary CNS Tumours. Since the appearance of this enzyme in the CSF is secondary to the increase of protein in the fluid, the search for lysozyme in the CSF is of no practical help in the diagnosis of CNS tumours.

Topics: Adolescent; Adult; Aged; Brain Neoplasms; Central Nervous System Diseases; Cerebral Ventricles; Child; Child, Preschool; Craniopharyngioma; Cysts; Female; Glioma; Humans; Hydrocephalus; Infant; Male; Meningioma; Meningitis; Middle Aged; Muramidase; Neoplasm Metastasis; Neurilemmoma; Neuroblastoma; Peripheral Nervous System Neoplasms; Time Factors; Vestibulocochlear Nerve

Topics: Brain Injuries; Brain Neoplasms; Cerebrospinal Fluid; Craniopharyngioma; Glioma; Humans; Meningioma; Muramidase; Neurilemmoma; Neuroblastoma; Vestibulocochlear Nerve

Topics: Blood-Brain Barrier; Brain Neoplasms; Choriocarcinoma; Chorionic Gonadotropin; Desmosterol; Female; Glioma; Humans; Muramidase; Neoplasm Metastasis; Pregnancy

Topics: Brain Neoplasms; Cerebrospinal Fluid; Female; Glioma; Histiocytosis, Langerhans-Cell; Humans; Lymphoma, Large B-Cell, Diffuse; Lymphoma, Non-Hodgkin; Male; Meningitis; Muramidase; Neoplasm Metastasis