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  • 2000-2004  (5)
  • 1955-1959
  • 1880-1889
  • Bioequivalence  (1)
  • Calcium-binding Protein  (1)
  • G2/M arrest  (1)
  • GRGDS  (1)
  • Macrobrachium nipponense  (1)
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Material
Years
Year
Keywords
  • 1
    Electronic Resource
    Electronic Resource
    Pharmacokinetics and bioequivalence evaluation of three commercial tablet formulations of mefloquine when given in combination with dihydroartemisinin in patients with acute uncomplicated falciparum malaria (2000)
    Springer
    European journal of clinical pharmacology 55 (2000), S. 743-748 
    Details
    ISSN: 1432-1041
    Keywords: Key words Pharmacokinetics ; Bioequivalence ; Mefloquine ; Uncomplicated falciparum malaria ; Dihydroartemisinin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Abstract Objective: To assess the pharmacokinetics and relative bioavailability/bioequivalence of three commercial tablet formulations of mefloquine, i.e. Lariam (reference formulation), Mephaquin 100 Lactab and Eloquin-250, when given sequentially after dihydroartemisinin in Thai patients with acute uncomplicated falciparum malaria. Methods: Twenty-nine Thai patients with acute uncomplicated falciparum malaria were randomised to receive an initial dose of 300 mg dihydroartemisinin, followed by 1250 mg mefloquine (at 24 h and 30 h after dihydroartemisinin) given as either Lariam (n=10 cases), Mephaquin (n=9 cases) or Eloquin-250 (n=10 cases). Serial blood samples were obtained up to day 42 after treatment with mefloquine. Mefloquine concentrations were determined in whole blood by means of ultraviolet high-performance liquid chromatography. The pharmacokinetic parameters of mefloquine were estimated using non-compartmental and compartmental analysis. Results: The three combination regimens were well tolerated. Patients in all treatment groups had a rapid initial response. However, nine patients (four and five cases in regimen containing Mephaquin 100 Lactab and Eloquin-250, respectively) had reappearance of parasitaemia during the follow-up period. Mefloquine from the three formulations showed significantly different pharmacokinetic and bioavailability metrics. Significantly lower peak plasma concentrations (Cmax) and areas under the plasma concentration–time curve (AUC; AUC0–48h, AUC0–7days, and total AUC) were observed with Mephaquin 100 Lactab than with the other two formulations. Mean values for relative bioavailability of the test to standard products were 49.1% (Mephaquin 100 Lactab) and 72.4% (Eloquine-250). Based on the criteria set, the bioavailability of the two test products (Mephaquin 100 Lactab and Eloquine-250) was considered non-equivalent to the reference product with respect to the rate (tmax, Cmax) and extent (AUC0–48h, AUC0–7days, total AUC) of mefloquine absorption.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002280050008
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Activation of MAD 2 checkprotein and persistence of cyclin B1/CDC 2 activity associate with paclitaxel-induced apoptosis in human nasopharyngeal carcinoma cells (2000)
    Springer
    Apoptosis 5 (2000), S. 235-241 
    Details
    ISSN: 1573-675X
    Keywords: apoptosis ; cyclin B1/CDC 2 ; G2/M arrest ; MAD 2 ; paclitaxel
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Paclitaxel (Taxol™) is a microtubule-interfering agent that induced persistent and transient G2/M arrest before apoptosis in human nasopharyngeal carcinoma (NPC) cells at high and low concentrations, respectively. In this study, we intended to explore the underlying molecular events and found that cellular cyclin B1/CDC 2 kinase activity was increased and persisted for 〉6 h upon paclitaxel treatment both at high and low concentrations. Furthermore, activation of MAD 2 checkprotein could account for the loss of cyclin B1 ubiquitination and the persistence of cyclin B1/CDC 2 activation in the cases. To investigate the involvement of cyclin B1 and MAD 2 activation in paclitaxel-induced apoptosis, we introduced affinity-purified anti-cyclin B1 and MAD 2 antibodies into NPC cells by electroporation before the further paclitaxel treatment. The antibodies against cyclin B1 and MAD 2 indeed attenuated paclitaxel-induced cytotoxicity and DNA fragmentation. Our study suggests that activation of cyclin B1/CDC 2 and MAD 2 were the M-phase events required for paclitaxel-induced apoptosis in NPC cells. The dys-regulated cyclin B1/CDC 2 activation could enhance the prometaphase progression, but activation of MAD 2 rendered cells inable to exit from the metaphase. Under this circumstance, cells were probably going to “mitotic catastrophe” and ultimately, destined to apoptosis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009652412399
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Effect of pH and Zn2+ on subcultured muscle cells from Macrobrachium nipponense (2000)
    Springer
    Methods in cell science 22 (2000), S. 277-284 
    Details
    ISSN: 1573-0603
    Keywords: Macrobrachium nipponense ; Cell subculture ; pH ; Zn2+
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A cell culture system was devised for muscle cell of Macrobrachium nipponense in the study. The juvenile and adult shrimps were held in laboratory aquaria with penicillin 1000 IU/ml and streptomycin 1000 µg/ml for 12–24 hours. Cell cultures were established in medium 199 supplemented with 20% fetal bovine serum, 1 g/L glucose, 5.2 g/L NaCl, 1.43 g/L CaCl2, 0.05 g/L MgCl2, 100 IU/mL penicillin and 100 µg/ml streptomycin. Fibroblast-like cells were passaged up to three times and survived for 54 days. The results showed the optimum for subculture in vitro was in medium 199 with pH 7.6. Moreover, basal medium supplemented with Zn2+ 60 µg/L could enhance the growth of the muscle cells. It was found that better results for cell culture would be obtained more easily with juvenile shrimps caught in spring than adults in summer or autumn; and shrimps caught within 12 hours after ecdysis could grow much better than the intermoult shrimps.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1017962429862
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Conjugation of Arg-Gly-Asp sequence into thermo-reversible gel as an extracellular matrix for 3T3-L1 fibroblast cell culture (2000)
    Springer
    Biotechnology letters 22 (2000), S. 1553-1556 
    Details
    ISSN: 1573-6776
    Keywords: fibroblast cell ; gel ; GRGDS ; integrin family ; N-isopropylacrylamide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract High molecular weight N-isopropylacrylamide copolymers with small amounts of acrylic acid (typically 2–5 mol% in feed) were synthesized by free radical polymerization in benzene and then conjugated with adhesion molecules of Gly-Arg-Gly-Asp-Ser (GRGDS) peptides. Aqueous polymer solutions (5, 6, 8 and 10% w/v) in culture medium (pH 7.4, ionic strength; 0.15 M) with 3T3-L1 fibroblast cells were mixed and poured in Millicells, which supported the gel formation without a significant gel induction time at 36 °C (gelation temperature). The initially formed gel was translucent and became more opaque as the temperature increased. The interaction between fibroblast cells and an artificial matrix of GRGDS containing p(NiPAAm-co-AAc) copolymer gel resulted in effective cell attachment, proliferation and growth. This study supported that specific attachment is the result of the interaction between the integrin families on the fibroblast and the RGD sequence on the p(NiPAAm-co-AAc) copolymer gel.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005680800420
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Calcium-binding Proteins Calbindin D28K, Calretinin, and Parvalbumin Immunoreactivity in the Rabbit Visual Cortex (2000)
    Springer
    Molecules and cells 10 (2000), S. 206-212 
    Details
    ISSN: 0219-1032
    Keywords: Calcium-binding Protein ; Immunocytochemistry ; Localization ; Visual Cortex
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The distribution and morphology of neurons containing three calcium-binding proteins, calbindin D28K, calretinin, and parvalbumin in the adult rabbit visual cortex were studied. The calcium-binding proteins were identified using antibody immunocytochemistry. Calbindin D28K-immunoreactive (IR) neurons were located throughout the cortical layers with the highest density in layer V. However, calbindin D28K-IR neurons were rarely encountered in layer I. Calretinin-IR neurons were mainly located in layers II and III. Considerably lower densities of calretinin-IR neurons were observed in the other layers. Parvalbumin-IR neurons were predominantly located in layers III, IV, V, and VI. In layers I and II, parvalbumin-IR neurons were only rarely seen. The majority of the calbindin D28K-IR neurons were stellate, round or oval cells with multipolar dendrites. The majority of calretinin-IR neurons were vertical fusiform cells with long processes traveling perpendicularly to the pial surface. The morphology of the majority of parvalbumin-IR neurons was similar to that of calbindin D28K: stellate, round or oval with multipolar dendrites. These results indicate that these three different calcium-binding proteins are contained in specific layers and cells in the rabbit visual cortex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s10059-000-0206-2
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    Paper (German National Licenses)
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