To evaluate possible roles of matrix metalloproteinase (MMP)-1, -2, tissue inhibitor of metalloproteinase (TIMP)-1, -2 and membrane-type-1 matrix metalloproteinase (MT1-MMP) in invasion of human gliomas, expressions of these proteins were investigated in ten cases of human glioma and two meningioma tissues and eight human glioma cell lines. In gelatin zymography, MMP-2 activities of glioblastomas were higher than astrocytomas. The activated form of MMP-2 was seen in five of six cases of glioblastomas, but not in astrocytomas. MMP-9 activity was detected in all cases of malignant astrocytomas but the reactivity of MMP-9 was weaker than that of MMP-2. MT1-MMP mRNA expression in glioblastomas was higher than that in astrocytomas. Five cases of glioblastomas with activated form of MMP-2 had MT1-MMP expressions. In vitro, human glioma cell lines with high expression of MT1-MMP also showed high MMP-2 activity. TIMP-1 transcripts were constitutively present in almost all glioma tissues and cell lines, whereas TIMP-2 mRNA were weak especially in malignant gliomas. Imbalance of TIMP-2/MMP-2 was observed using immunoprecipitation analysis in a glioma cell line. High expression of MMP-2 and MT1-MMP is possibly involved in invasiveness of malignant glioma.
Animal ; Blotting, Northern/methods ; Brain/pathology ; Brain Neoplasms/pathology ; Brain Neoplasms/enzymology* ; Enzyme Activation ; Gelatinase A/metabolism ; Gelatinase A/genetics* ; Gelatinase B/metabolism ; Gene Expression Regulation, Enzymologic* ; Glioma/pathology ; Glioma/enzymology* ; Human ; Metalloendopeptidases/genetics* ; Papio ; Tissue Inhibitor-of Metalloproteinase-2/genetics ; Tissue-Inhibitor of Metalloproteinase-1/genetics ; Tumor Cells, Cultured

To evaluate possible roles of matrix metalloproteinase (MMP)-1, -2, tissue inhibitor of metalloproteinase (TIMP)-1, -2 and membrane-type-1 matrix metalloproteinase (MT1-MMP) in invasion of human gliomas, expressions of these proteins were investigated in ten cases of human glioma and two meningioma tissues and eight human glioma cell lines. In gelatin zymography, MMP-2 activities of glioblastomas were higher than astrocytomas. The activated form of MMP-2 was seen in five of six cases of glioblastomas, but not in astrocytomas. MMP-9 activity was detected in all cases of malignant astrocytomas but the reactivity of MMP-9 was weaker than that of MMP-2. MT1-MMP mRNA expression in glioblastomas was higher than that in astrocytomas. Five cases of glioblastomas with activated form of MMP-2 had MT1-MMP expressions. In vitro, human glioma cell lines with high expression of MT1-MMP also showed high MMP-2 activity. TIMP-1 transcripts were constitutively present in almost all glioma tissues and cell lines, whereas TIMP-2 mRNA were weak especially in malignant gliomas. Imbalance of TIMP-2/MMP-2 was observed using immunoprecipitation analysis in a glioma cell line. High expression of MMP-2 and MT1-MMP is possibly involved in invasiveness of malignant glioma.
Animal ; Blotting, Northern/methods ; Brain/pathology ; Brain Neoplasms/pathology ; Brain Neoplasms/enzymology* ; Enzyme Activation ; Gelatinase A/metabolism ; Gelatinase A/genetics* ; Gelatinase B/metabolism ; Gene Expression Regulation, Enzymologic* ; Glioma/pathology ; Glioma/enzymology* ; Human ; Metalloendopeptidases/genetics* ; Papio ; Tissue Inhibitor-of Metalloproteinase-2/genetics ; Tissue-Inhibitor of Metalloproteinase-1/genetics ; Tumor Cells, Cultured

OBJECTIVETo study the expression of Aurora-B in human glioma tissue and its significance.

METHODSThe total RNA was extracted from 41 human glioma tissues and 11 normal brain tissues by Trizol reagent. After reverse transcription of the total RNA into cDNAs, Aurora-B mRNA expressions in these samples were detected by quantitative real-time PCR. The protein expression in these samples was detected using immunohistochemical staining.

RESULTSAurora-B mRNA and protein expressions were significantly increased in glioma tissues as compared with those in normal brain tissues.

CONCLUSIONAurora-B mRNA and protein show markedly higher expressions in glioma tissue, suggesting that Aurora-B may be one of the malignant biomarkers in the pathogenesis and progression of human glioma.

Aurora Kinase B ; Aurora Kinases ; Biomarkers, Tumor ; metabolism ; Brain Neoplasms ; enzymology ; pathology ; Female ; Glioma ; metabolism ; pathology ; Humans ; Male ; Protein-Serine-Threonine Kinases ; genetics ; metabolism ; RNA, Messenger ; genetics ; metabolism ; Tumor Cells, Cultured

Telomerase adds telomeric repeats to the ends of telomeres to compensate for their progressive loss. A favorable prognosis is associated with low or no telomerase in some tumors. The authors investigated whether telomerase activity is associated with survival of patients with brain tumors. Sixty-two consecutive patients with brain tumors underwent surgery, and their surgical specimens were investigated. The patients were pathologically categorized as group I (aggressive group) and group II (non-aggressive group). Telomerase activity was examined by the telomeric repeat amplification protocol (TRAP) assay. The median time was calculated in association with overall survival and progression-free survival in each group. The significant difference was noted in telomerase activity between high-grade gliomas and lowgrade gliomas (p=0.022). Telomerase activity was significantly associated with the median overall survival and progression-free survival in all tumors of the aggressive group. On the other hand, the median overall survival in the non-aggressive group was not dependent on telomerase activity, while the median progression-free survival was. Our data suggests that telomerase is an important prognostic indicator of survival in patients with brain tumors.
Adolescent ; Adult ; Aged ; Brain Neoplasms/enzymology/genetics/*pathology ; Child ; Child, Preschool ; Enzyme-Linked Immunosorbent Assay/methods ; Female ; Humans ; Male ; Middle Aged ; Polymerase Chain Reaction/methods ; Prognosis ; Research Support, Non-U.S. Gov't ; Survival Analysis ; Telomerase/genetics/*metabolism