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  • 1
    Electronic Resource
    Electronic Resource
    Synapsin IIa: expression in insect cells, purification, and characterization (1992)
    s.l. : American Chemical Society
    Biochemistry 31 (1992), S. 4268-4275 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00132a017
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  • 2
    Electronic Resource
    Electronic Resource
    Synapsin IIa Bundles Actin Filaments (1994)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 63 (1994), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Synapsins are neuron-specific phosphoproteins associated with small synaptic vesicles in the presynaptic nerve terminal. Synapsin I, which has been demonstrated to bundle F-actin in vitro, has been postulated to regulate neurotransmitter release by cross-linking synaptic vesicles to the actin cytoskeleton. To investigate the possible interaction of synapsin II with actin filaments, we expressed synapsin II in Spodoptera frugiperda and High Five insect cells using a recombinant baculovirus. Purified recombinant synapsin IIa was incubated with F-actin, and bundle formation was evaluated by light scattering and electron microscopy. Synapsin IIa was found to bundle actin filaments. Dose-response curves indicated that synapsin IIa was more potent than synapsin I in bundling actin filaments. These data suggest that synapsin IIa may cross-link synaptic vesicles and actin filaments in the nerve terminal.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1994.63041568.x
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  • 3
    Electronic Resource
    Electronic Resource
    Role of Extracellular Signal-Regulated Protein Kinases 1 and 2 in Oligodendroglial Process Extension (1997)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 68 (1997), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The relationship between extracellular signal-regulated protein kinase (ERK) activation and process extension in cultured bovine oligodendrocytes (OLGs) was investigated. Process extension was induced through the exposure of cultured OLGs to phorbol 12-myristate 13-acetate (PMA), an activator of protein kinase C (PKC), for various intervals. During the isolation of these OLGs from bovine brain, the original processes were lost. Therefore, any reinitiation of process extension via PMA stimulation was easily discernible through morphological monitoring. It was found that exposure of OLGs to PMA for 10 min was enough to induce OLG process extension 24–72 h later. Furthermore, this extension was still evident at least 1 week after the initial PMA stimulation, indicating that OLGs do not need continuous PKC activation to sustain process extension. Control and PMA-stimulated OLGs were also subjected to immunocytochemistry using an anti-ERK antibody selective for the mitogen-activated protein kinases p42 Erk2 (ERK2) and p44 Erk1 (ERK1) isoforms. ERK immunoreactivity in the nucleus was evident after PMA stimulation of OLGs but not in control OLGs. In parallel experiments, the control and PMA-stimulated OLGs were purified by Mono Q fractionation and subjected to ERK phosphotransferase assays using [γ-32P]ATP and either myelin basic protein (MBP) or a synthetic peptide substrate based on the Thr97 phosphorylation site in MBP. These assays indicated that in PMA-treated OLGs, ERK activation was at least 12-fold higher than in control OLGs. Anti-ERK and anti-phosphotyrosine western blots of the assay fractions verified an enhanced phosphorylation of ERK1 and ERK2 in PMA-treated fractions relative to control fractions. When OLGs were pretreated for 15 min with the ERK kinase (MEK) inhibitor PD 098059 before PMA stimulation, they exhibited a 67% decrease in ERK activation as compared with cells treated with PMA alone. Furthermore, these MEK inhibitor-pretreated cells were still viable but showed no process extensions up to 1 week later. Therefore, we propose that a threshold level of ERK activity is required for the initiation of OLG process extension.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1997.68030945.x
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  • 4
    Electronic Resource
    Electronic Resource
    Cyclosporine A protects against apoptosis in ischaemic/reperfused rat kidneys (2002)
    Oxford, UK : Blackwell Science Pty
    Clinical and experimental pharmacology and physiology 29 (2002), S. 0 
    Details
    ISSN: 1440-1681
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 1. Renal ischaemia followed by reperfusion leads to acute renal failure in both native kidneys and renal allografts. Cyclosporine A (CsA) has been used as an immunosuppressive agent in organ transplantation. In the present study, the effect of CsA on ischaemia/reperfusion-induced apoptosis in the kidney was investigated.2. Ischaemia/reperfusion injury caused widespread apoptosis primarily in the medulla of the kidney. At 1.5 mg/kg per day, CsA significantly reduced the number of apoptotic cells in rat kidney after ischaemia/reperfusion injury.3. Low-dose CsA treatment did not affect the levels of creatinine in the serum of rats after ischaemia/reperfusion injury.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1440-1681.2002.03736.x
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  • 5
    Electronic Resource
    Electronic Resource
    Purification of DOPA decarboxylase from bovine striatum (1990)
    Springer
    Molecular and cellular biochemistry 94 (1990), S. 121-131 
    Details
    ISSN: 1573-4919
    Keywords: aromatic L-amino acid decarboxylase ; purification, bovine striatum ; 3,4-dihydroxyphenylalanine ; 5-hydroxytryptophan
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Pyridoxal phosphate-dependent DOPA decarboxylase has been purified from bovine striatum to a specific activity of 1.6 U/mg protein. After ammonium sulfate precipitation (30–60%) it was purified by DEAE-Sephacel, Sephacryl S-200, and TSK Phenyl 5 PW chromatography. The purified enzyme showed a single silver staining band with polyacrylamide gel electrophoresis under both denaturing and non-denaturing conditions. The bovine striatal DOPA decarboxylase is a dimer (subunit Mr = 56000 by SDS-PAGE) with a native Mr of 106000 as judged by chromatography on Sephacryl S-200 and by sedimentation analysis. Similar to the DOPA decarboxylase purified from non-CNS tissues, the bovine striatal enzyme requires free sulfhydryl groups for activity, is strongly inhibited by heavy metal ions, and can decarboxylate 5-hydroxytryptophan as well. It should be noted, however, that the final enzyme preparation is enriched in DOPA decarboxylase activity. The distribution of the DOPA decarboxylase and 5-HTP decarboxylase activities also varies among several bovine brain regions. In addition, heat treatment of the enzyme preparation inactivated the two decarboxylation activities at different rates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00214119
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  • 6
    Electronic Resource
    Electronic Resource
    Effect of Flos carthami on stress-activated protein kinase activity in the isolated reperfused rat heart (2000)
    Springer
    Molecular and cellular biochemistry 207 (2000), S. 41-47 
    Details
    ISSN: 1573-4919
    Keywords: SAP kinase ; JNK ; Flos carthami ; ischemia ; reperfusion ; heart
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The apoptotic death of cardiomyocytes due to ischemia/reperfusion is one of the major complications of heart disease. Ischemia/reperfusion has been shown to lead to the activation of the stress-activated protein (SAP) kinases and the p38/reactivating kinase (p38/RK). In this study, the direct effect of an aqueous Flos carthami (FC) extract on SAP kinases was investigated. When isolated rat hearts were perfused by Langendorff mode with media containing FC extract prior to the induction of global ischemia and the subsequent reperfusion, SAP kinase activity was inhibited 95%. Untreated ischemic/reperfused hearts showed a 57% elevation in the activity of SAP kinase. The in vitro effect of these FC extracts on SAP kinase was also tested. At a concentration of 10 μg/ml, the aqueous FC extract resulted in 50% inhibition of SAP kinase activity in ischemic heart tissue. Our results showed that FC affected both the interaction of SAP kinase with c-jun as well as the phosphotransferase reaction. These results clearly demonstrate that extracts from Flos carthami exerted inhibitory effects on SAP kinase. The administration of the FC extract may lead to a modulation of the apoptotic effect of SAP kinase activation induced during ischemia/reperfusion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1017266628572
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  • 7
    Electronic Resource
    Electronic Resource
    Effect of Magnesium tanshinoate B on the production of nitric oxide in endothelial cells (2000)
    Springer
    Molecular and cellular biochemistry 207 (2000), S. 35-39 
    Details
    ISSN: 1573-4919
    Keywords: nitric oxide ; endothelial cells ; Salviae miltiorrhizae ; magnesium tanshinoate B
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Nitric oxide (NO) is a potent vasodilator which plays an important role in regulating vascular tones. Danshen, a Chinese herbal medicine has been widely used for the treatment of cardiovascular diseases. The objective of this study was to investigate the effect of magnesium tanshinoate B (MTB), a compound purified from Danshen, on the production of NO in human endothelial cell line (ECV304). After cells were incubated with MTB (1-10 µM) for 1 or 4 h, amounts of NO metabolites released by cells were quantified and cellular NOS activities were determined following the conversion of [3H]arginine to [3H]citrulline. The NOS protein expression was determined by Western immunoblotting analysis. MTB (1-10 µM) stimulated the release of NO and its metabolites from endothelial cells. Following MTB treatment, the cellular NOS activities were significantly enhanced with a concomitant increase in the levels of constitutive NOS (cNOS) protein mass (110-178%). Selective activation of cNOS by MTB may be employed therapeutically in modulating NO production in endothelial cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007081911734
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