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  • 1
    Electronic Resource
    Electronic Resource
    Fluorometrical Analysis of Guanidino Compounds in Human Cerebrospinal Fluid (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 38 (1982), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Guanidino compounds in CSF of 57 human subjects were determined fluorometrically after reaction with phenanthrenequinone in alkali solution, using HPLC. Creatinine (65.2 ± 13.4 nmol/ml), arginine (24.7 ± 6.4 nmol/ml), and homoarginine (0.7 ± 0.3 nmol/ml) were found in all subjects. Trace amounts of guanidinosuccinic acid and guanidinoacetic acid were detected in some of the subjects. Brain guanidino compounds, taurocyamine, N-acetylarginine, and methylguanidine were not detected in CSF.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1982.tb08649.x
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  • 2
    Electronic Resource
    Electronic Resource
    Matrix metalloproteinase 9 in mucosally invasive gastric cancer (1998)
    Springer
    Gastric cancer 1 (1998), S. 142-145 
    Details
    ISSN: 1436-3305
    Keywords: Key words: extracellular matrix, stomach, neoplasm, metastasis, tumor-stromal cell interaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Background. Matrix metalloproteinase 9 (MMP-9) facilitates tumor invasion and metastasis via basement membrane degradation. Control of MMP-9 production by cancer-stromal cell interactions in these processes has been observed. Methods. We measured plasma MMP-9 concentrations, using a one-step sandwich enzyme immunoassay, and also immunohistochemically localized MMP-9 in patients with small gastric cancers limited to the mucosa. The cancers were classified as intraepithelial tumor (Tis) and T1 disease according to the tumor-node-metastasis (TNM) classification of the International Union Against Cancer. Results. Patients with T1 disease had a higher positivity rate for and mean value of MMP-9 than patients with Tis disease. In T1 tumors, MMP-9 expression determined immunohistochemically, was greater in cells in cancer stroma than in cells in noncancerous stroma, a situation found in only a few Tis tumors. Conclusions. These results suggest that MMP-9 is related to the initial step of gastric cancer invasion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s101200050008
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  • 3
    Electronic Resource
    Electronic Resource
    Matrix metalloproteinase 9 in human plasma has 96% specificity and 56% sensitivity for gastric cancer screening (1996)
    Springer
    International journal of clinical oncology 1 (1996), S. 39-43 
    Details
    ISSN: 1437-7772
    Keywords: matrix metalloproteinase ; gastric cancer ; diagnosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Background Matrix metalloproteinase 9 (MMP-9, 92 kDa gelatinase/type IV collagenase, gelatinase B) is a substance of current interest that can dissolve normal tissue basement membranes consisting of type IV collagen. The release of MMP-9 by tumor cells allows penetration of the stroma. This is an important mechanism for cancer invasion and metastasis. This study measures MMP-9 in the plasma of normal subjects and patients with gastric cancer. The measurement of MMP-9 is found to be a useful tool for gastric cancer screening. Methods Plasma was obtained from 138 healthy individuals and 73 patients with gastric cancer who underwent gastrectomy at Aichi Cancer Center between August 1994 and July 1995. A one-step sandwich enzyme immunoassay using monoclonal antibodies was employed to measure the concentrations of MMP-9 in plasma. Results Seventy-three patients with gastric cancer had higher concentrations of plasma MMP-9 than normal subjects. The sensitivity in these patients was 56%, and the specificity as a cancer screening test for MMP-9 in healthy individuals was 96%. Postoperative plasma MMP-9 concentrations were lower than preoperative concentrations. Patients with advanced gastric cancer and early cancer exhibited higher mean values of plasma MMP-9 than healthy individuals. Preoperative plasma MMP-9 concentrations correlated closely with the many clinicopathologic factors and stages of the Japanese classification of gastric carcinoma. Conclusions The measurement of plasma MMP-9 is helpful for early detection of primary or recurrent gastric cancer, and useful for evaluating the tumors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02347267
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  • 4
    Electronic Resource
    Electronic Resource
    Enhanced production and activation of progelatinase A mediated by membrane-type 1 matrix metalloproteinase in human oral squamous cell carcinomas: Implications for lymph node metastasis (2000)
    Springer
    Clinical & experimental metastasis 18 (2000), S. 179-188 
    Details
    ISSN: 1573-7276
    Keywords: activation of proMMP-2 ; lymph node metastasis ; matrix metalloproteinase ; membrane-type matrix metalloproteinase ; oral squamous cell carcinoma ; tissue inhibitor of metalloproteinases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We measured the production levels of seven different matrix metalloproteinases (MMP-1, 2, 3, 7, 8, 9 and 13) and two tissue inhibitors of metalloproteinases (TIMP-1 and 2) in the homogenates of human oral squamous cell carcinomas and control normal squamous epithelia by the corresponding sandwich enzyme immunoassay systems. The levels of MMP-1, 2, 3, 8, 9, 13 and TIMP-1 were significantly higher in the carcinoma samples than in the control. Among them, only the production level of MMP-2 was significantly higher in the carcinomas with cervical lymph node metastasis than in those without metastasis (P 〈 0.05). Gelatin zymography demonstrated that activation ratio of the zymogen of MMP-2 (proMMP-2) is significantly higher in the carcinomas with lymph node metastasis than in those without metastasis (P 〈 0.05) or normal control (P 〈 0.01). Quantitative RT-PCR for membrane-types 1, 2 and 3 MMPs (MT1, 2 and 3-MMPs), which activate proMMP-2 in vitro, demonstrated that MT1-MMP is predominantly expressed in the carcinoma tissues, and the expression level is significantly higher in the carcinomas with lymph node metastasis than in those without metastasis (P 〈 0.05) or the control samples (P 〈 0.05). Although MT2-MMP and MT3-MMP were detected in approximately 30% of the carcinoma cases, their expression levels were extremely lower compared with that of MT1-MMP. There was a direct correlation between the MT1-MMP expression level and proMMP-2 activation ratio (r = 0.62, P 〈 0.01). In situ hybridization and immunohistochemistry indicated that carcinoma cells and stromal cells adjacent to carcinoma cell nests express MT1-MMP transcripts and protein. MMP-2 and TIMP-2 were also immunolocalized to the carcinoma cells in the carcinoma samples. By in situ zymography, gelatinolytic activity was demonstrated in the carcinoma cell nests and abolished by the treatment with an MMP inhibitor, BB94. These results suggest that among seven different MMPs, the production of proMMP-2 and its activation mediated by MT1-MMP play an important role in the cervical lymph node metastasis of the human oral squamous cell carcinomas.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006749501682
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  • 5
    Electronic Resource
    Electronic Resource
    Secretion of matrix metalloproteinase-2 (72 kD gelatinase/type IV collagenase = gelatinase A) by malignant human glioma cell lines: implications for the growth and cellular invasion of the extracellular matrix (1996)
    Springer
    Journal of neuro-oncology 28 (1996), S. 13-24 
    Details
    ISSN: 1573-7373
    Keywords: smalignant glioma ; matrix metalloproteinases ; extracellular matrix ; invasion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Human glioma cells (T98G and A172 cell lines) were cultured on various extracellular matrix (ECM) components including type 1, IV and V collagens, fibronectin, laminin, and reconstituted basement membrane (Matrigel), and the role of matrix metalloproteinases (MMPs) in their growth and invasion was examined. T98G glioma cells grew well on these ECM components and invaded the reconstituted basement membrane. In contrast, A172 glioma cells showed growth inhibition on collagen types IV and V and Matrigel without invasion of the Matrigel. Gelatin zymography and enzyme immunoassays demonstrated that T98G glioma cells, but not A172 cells, secrete a large amount of matrix metallproteinase-2 (MMP-2, 72 kD gelatinase/type IV collagenase = gelatinase A), and this was confirmed by immunoblotting and immunohistochemistry. Of the two different tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2), T98G cells produced only TIMP-1 during culture on Matrigel, whereas A172 cells secreted both. Although both human recombinant TIMP-1 and TIMP-2 stimulated T98G cell growth slightly on Matrigel, the in vitro invasiveness was significantly reduced by only recombinant TIMP-2. These results suggest that MMP-2 plays an important role in the ECM invasion of T98G human glioma cells in vitro.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00300442
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  • 6
    Electronic Resource
    Electronic Resource
    Catecholamine level in cerebrospinal fluid of epileptics (1982)
    Springer
    Neurochemical research 7 (1982), S. 1299-1305 
    Details
    ISSN: 1573-6903
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We estimated catecholamine levels in CSF of 15 epileptics and 75 non-neurological patients utilizing a high performance liquid chromatograph with a highly sensitive fluorometer and found the following results: The dopamine (DA) levels in males were significantly higher than those in females, while norepinephrine (NE) levels in males were the same as in females. The DA levels were significantly lower and NE levels significantly higher in epileptics than in non-neurological patients. DA and NE in petit mal patients were on the average lower than in grand mal patients, but untreated grand mal patients had higher NE levels. These results suggest that epilepsy may be associated with a disturbance of DA and/or NE metabolism or release in the brain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00965900
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  • 7
    Electronic Resource
    Electronic Resource
    Changes in serum levels of metalloproteinases and their inhibitors by treatment of chronic hepatitis C with interferon (1996)
    Springer
    Digestive diseases and sciences 41 (1996), S. 995-1000 
    Details
    ISSN: 1573-2568
    Keywords: interferon ; chronic hepatitis C ; matrix metalloproteinases ; tissue inhibitors of metalloproteinases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We treated 18 patients with chronic hepatitis C by recombinant interferon-α (6 MIU for 24 weeks). In seven patients, serum aminotransferase levels declined to normal (responders). To evaluate the effect of interferon on matrix metalloproteinases (MMPs) and their inhibitors, namely tissue inhibitors of metalloproteinases (TIMPs), the serum levels of these enzymes were determined by enzyme immunoassay (EIA) using a specific monoclonal antibody. In responders, there was a tendency, but not a significant one, towards either an increase in serum MMP 1 levels or a decrease in serum TIMP 1 levels. In contrast, in nonresponders, both a significant decrease in MMP 1 and MMP 3 and a significant increase in TIMP 1 were observed. The number of cases of either increase in serum MMP levels or decrease in serum TIMP levels was significantly larger in responders than in nonresponders. Furthermore, the ratio of MMP 1 to TIMP 1 significantly increased in responders, suggesting that the balance between matrix formation and degradation in hepatic fibrosis tended to move toward degradation. These data indicate that interferon may exert a beneficial effect on hepatic fibrosis in parallel with improvement of aminotransferase activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02091543
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