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  • 1
    Electronic Resource
    Electronic Resource
    Modulation of the .beta.-receptor adenylate cyclase interactions in cultured Chang liver cells by phospholipid enrichment (1979)
    s.l. : American Chemical Society
    Biochemistry 18 (1979), S. 3016-3023 
    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/bi00581a017
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  • 2
    Electronic Resource
    Electronic Resource
    Pyrene-labeled gangliosides: micelle formation in aqueous solution, lateral diffusion, and thermotropic behavior in phosphatidylcholine bilayers (1987)
    s.l. : American Chemical Society
    Biochemistry 26 (1987), S. 5943-5952 
    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/bi00392a055
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  • 3
    Electronic Resource
    Electronic Resource
    Mechanism of lipid-body formation in prokaryotes: how bacteria fatten up (2005)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 55 (2005), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Neutral lipid accumulation is frequently observed in some Gram-negative prokaryotes like Acinetobacter sp. and most actinomycetes, including the pathogenic Mycobacterium tuberculosis and antibiotic producing streptomycetes. We examined the formation  of  wax  ester-  and  triacylglycerol  (TAG)-bodies in Acinetobacter calcoaceticus and Rhodococcus opacus using microscopic, immunological and biophysical methods. A general model for prokaryotic lipid-body formation is proposed, clearly differing from the current models for the formation of lipid inclusions in eukaryotes and of poly(hydroxyalkanoic acid) (PHA) inclusions in prokaryotes. Formation of lipid-bodies starts with the docking of wax ester synthase/acyl-CoA:diacylglycerol acyltransferase (WS/DGAT) to the cytoplasm membrane. Both, analyses of in vivo and in vitro lipid-body synthesis, demonstrated the formation of small lipid droplets (SLDs), which remain bound to the membrane-associated enzyme. SLDs conglomerated subsequently to membrane-bound lipid-prebodies which are then released into the cytoplasm. The formation of matured lipid-bodies in the cytoplasm occurred by means of coalescence of SLDs inside the lipid prebodies, which are surrounded by a half-unit membrane of phospholipids.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2004.04441.x
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  • 4
    Electronic Resource
    Electronic Resource
    Strain-dependent disruption of blood–cerebrospinal fluid barrier by Streptoccocus suis in vitro (2005)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 44 (2005), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Streptococcus suis capsular type 2 is an important agent of diseases including meningitis among pigs worldwide, and is also a zoonotic agent. The barrier function of the choroid plexus epithelium that constitutes the structural basis for the blood-cerebrospinal fluid (CSF) barrier has not been elucidated yet in bacterial meningitis. We investigated the influence of various S. suis isolates on the barrier function of cultured porcine choroid plexus epithelial cells with respect to the transepithelial resistance and paracellular [3H]-mannitol flux. Preferentially apical application of S. suis isolates significantly decreased transepithelial resistance and significantly increased paracellular [3H]-mannitol flux in a time-, dose- and strain-dependent manner. Viable S. suis isolates caused cytotoxicity determined by lactate dehydrogenase assay and electron microscopy, whereas S. suis sonicates and UV-inactivated S. suis did not cause cytotoxicity. The observed effects on porcine choroid plexus epithelial cells barrier function could not exclusively be ascribed to known virulence factors of S. suis such as suilysin. In conclusion, S. suis isolates induce loss of blood–cerebrospinal fluid barrier function in an in vitro model. Thus, S. suis may facilitate trafficking of bacteria and leucocytes across the blood–cerebrospinal fluid barrier. The underlying mechanisms for the barrier breakdown have yet to be determined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/j.femsim.2004.12.006
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  • 5
    Electronic Resource
    Electronic Resource
    The phase behavior of lipid monolayers containing pulmonary surfactant protein C studied by fluorescence light microscopy (1997)
    Springer
    European biophysics journal 26 (1997), S. 359-369 
    Details
    ISSN: 1432-1017
    Keywords: Key words Pulmonary surfactant ; Surfactant protein C ; SP-C ; Fluorescence light microscopy ; Phospholipids ; Monolayer ; Lipid-protein interactions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract Three compounds of the pulmonary surfactant – dipalmitoylphosphatidylcholine (DPPC), dipalmitoylphosphatidylglycerol (DPPG), and the surfactant associated protein C (SP-C) – were spread at the air-water interface of a Langmuir trough as a model system to mimic the properties of natural surfactant. Fluorescence microscopical images of the film formed at the interface were obtained during compression using a fluorescence dye bound covalently either to phosphatidylcholine or to SP-C. The images were quantified using statistical methods in respect to relative areas and relative fluorescence intensities of the domains found. In the early stage of compression, film pressure rose slightly and was accompanied by a phase separation which could be recognized in the images by the formation of bright and dark domains. On further compression, after a steep increase of film pressure, a plateau region of constant film pressure started abruptly. During compression in the plateau region, fluorescence intensity of the bright domain formed in the early stage of compression increased. The increasing fluorescence intensity, the non-Gaussian intensity distribution of the bright domain, and the small mean molecular area of the film in the plateau region gave rise to the assumption that multilayer structures were formed in the late stage of compression. The formation of the multilayer structures was fully reversible in repeated compression-expansion cycles including the plateau region of the phase diagram. The ability of lipid/SP-C mixtures to form reversible multilayer structures during compression may be relevant to stability in lungs during expiration and inhalation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002490050090
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  • 6
    Electronic Resource
    Electronic Resource
    Angiotensin II, vasopressin and GTP[γ-S] inhibit inward-rectifying K+ channels in porcine cerebral capillary endothelial cells (1991)
    Springer
    The journal of membrane biology 123 (1991), S. 55-62 
    Details
    ISSN: 1432-1424
    Keywords: blood-brain barrier ; inward-rectifying K− channels ; angiotensin II ; arginine-vasopressin ; guanosine 5′-[γ-thio]triphosphate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Cerebral capillaries from porcine brain were isolated. and endothelial cells were grown in primary culture. The whole-cell tight seal patch-clamp method was applied to freshly isolated single endothelial cells, and cells which were held in culture up to one week. With high K+ solution in the patch pipette and in the bath we observed inward-rectifying K+ currents, showing a time-dependent decay in part of the experiments. Ba2+ (1–10mm) in the bath blocked this current, whereas outside tetraethylammonium (10mm) decreased the peak current but increased the steady-state current. Addition of 1 μm of angiotensin II or of arginine-vasopressin to the extracellular side caused a time-dependent inhibition of the inward-rectifying K+ current in part of the experiments. Addition of 100 μm GTP[γ-S] to the patch pipette blocked the K+ inward rectifier. In cell-attached membrane patches two types of single inward-rectifying K+ channels were observed, with single channel conductances of 7 and 35 pS. Cell-attached patches were also obtained at the antiluminal membrane of intact isolated cerebral capillaries. Only one type of K+ channel withg=30 pS was recorded. In conclusion, inwardly rectifying K+ channels, which can be inhibited by extracellular angiotensin II and arginine-vasopressin, are present in cerebral capillary endothelial cells. The inhibition of this K+ conductance by GTP[γ-S] indicates that G-proteins are involved in channel regulation. It is suggested that angiotensin II and vasopressin regulate K+ transport across the blood-brain barrier, mediating their effects via G-proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01993963
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  • 7
    Electronic Resource
    Electronic Resource
    Characterization of γ-glutamyl transpeptidase activity of cultured endothelial cells from porcine brain capillaries (1989)
    Springer
    Cell & tissue research 256 (1989), S. 221-226 
    Details
    ISSN: 1432-0878
    Keywords: γ-Glutamyl transpeptidase ; Cerebral capillaries ; Blood-brain barrier ; Cell culture ; Pig
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Endothelial cells were isolated with high viability (〉93%) from porcine brain capillaries by Percoll gradient centrifugation after purely enzymatic digestion. Primary cultures were grown to confluent cell monolayers and quantitated for the activity of γ-glutamyl transpeptidase. The γ-glutamyl transpeptidase activity starts from a high enzymatic level, decreases with time in culture to about 15% of the initial value, and remains constant at this level after day 10 in culture. The activity progression depends on surface conditions. In the presence of collagen, an exponential decrease starts immediately after seeding, with a time constant of 70±10h. In the absence of collagen, γ-glutamyl transpeptidase activity first decreases on day 1 after plating, recovers to the initial value on day 2 and 3 and afterwards declines exponentially to a low and constant activity level. Ethanol added to the cell culture at a time when low constant activity is reached, reactivates the γ-glutamyl transpeptidase to 30% of the initial value.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00224737
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  • 8
    Electronic Resource
    Electronic Resource
    A new astrocytic cell line which is able to induce a blood-brain barrier property in cultured brain capillary endothelial cells (1997)
    Springer
    Cytotechnology 24 (1997), S. 11-17 
    Details
    ISSN: 1573-0778
    Keywords: astrocytes ; blood-brain barrier ; clone ; continuous cell line
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Astrocytes, a member of the glial cell family in the central nervous system, are assumed to play a crucial role in the formation of the blood-brain barrier (BBB) in vertebrates. It was shown that astrocytes induce BBB-properties in brain capillary endothelial cells (BCEC) in vitro. We now established an astroglial cell line of non-tumoral origin. The cloned cell line (A7) shows a highly increased proliferation rate and expresses the astrocytic marker glial fibrillary acidic protein. Furthermore, the clone A7 expresses S-100-protein and vimentin, which are also expressed by primary cultured astrocytes. This cell line therefore shows general astrocytic features. In addition, we were able to show that A7 cells re-induce the BBB-related marker enzyme alkaline phosphatase in BCEC, when these two cell types are co-cultured. Thus we have a cell line which can be readily cultured in large quantities, shows common astrocyte properties and is able to influence BCEC with respect to a BBB-related feature.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007936323956
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  • 9
    Electronic Resource
    Electronic Resource
    Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) of membrane proteins and non-covalent complexes (1995)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 30 (1995), S. 1462-1468 
    Details
    ISSN: 1076-5174
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Matrix-assisted laser desorption/ionization (MALDI) mass spectra and methods to improve their quality are reported for three hydrophobic, membrane-bound proteins: porin from Escherichia coli, bacteriorhodopsin from Halobacterium salinarium and cholesterolesterase from Pseudomonas fluorescens. Several commonly used UV and IR matrices have been tested. In addition, the susceptibility of MALDI mass spectrometry to various neutral and ionic detergents, known usually to degrade the quality of MALDI mass spectra, has been tested systematically. For porin, consisting of three identical non-covalently bound subunits, a new sample preparation is reported, resulting in the desorption of the intact quaternary protein structure. This leads to a better understanding of the way a given analyte is embedded into the host matrix crystals.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jms.1190301012
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  • 10
    Electronic Resource
    Electronic Resource
    Feldeffekttransistoren als Sensoren neuronaler Systeme (1992)
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 104 (1992), S. 47-49 
    Details
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ange.19921040106
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