Search Results - (Author, Cooperation:P. M. Deen)
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1Latest Papers from Table of Contents or Articles in PressS. C. Cheng ; J. Quintin ; R. A. Cramer ; K. M. Shepardson ; S. Saeed ; V. Kumar ; E. J. Giamarellos-Bourboulis ; J. H. Martens ; N. A. Rao ; A. Aghajanirefah ; G. R. Manjeri ; Y. Li ; D. C. Ifrim ; R. J. Arts ; B. M. van der Veer ; P. M. Deen ; C. Logie ; L. A. O'Neill ; P. Willems ; F. L. van de Veerdonk ; J. W. van der Meer ; A. Ng ; L. A. Joosten ; C. Wijmenga ; H. G. Stunnenberg ; R. J. Xavier ; M. G. Netea
American Association for the Advancement of Science (AAAS)
Published 2014Staff ViewPublication Date: 2014-09-27Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Aerobiosis/immunology ; Animals ; Candida albicans/immunology ; Candidiasis/immunology/metabolism ; Disease Models, Animal ; *Epigenesis, Genetic ; Female ; Glucose/metabolism ; Glycolysis/*immunology ; Humans ; Hypoxia-Inducible Factor 1, alpha Subunit/genetics/*metabolism ; Immunity, Innate/*genetics ; Immunologic Memory/*genetics ; Male ; Mice ; Mice, Inbred C57BL ; Monocytes/*immunology/metabolism ; Sepsis/genetics/immunology/metabolism ; Staphylococcal Infections/immunology/metabolism ; Staphylococcus aureus ; TOR Serine-Threonine Kinases/genetics/*metabolism ; Transcriptome ; beta-Glucans/immunologyPublished by: -
2Articles: DFG German National LicensesMulders, Sabine M. ; van der Kemp, Annemiete J. ; Terlouw, Sylvie A. ; van Boxtel, Hanneke A. F. ; van Os, Carel H. ; Deen, P. M. T.
Springer
Published 1998Staff ViewISSN: 1432-2013Keywords: Key words Loop exchange ; Oocytes ; Routing ; Structure ; Water channelSource: Springer Online Journal Archives 1860-2000Topics: MedicineNotes: Abstract Aquaporins are transmembrane proteins that contain six bilayer-spanning domains, connected by loops A to E. The hourglass model predicts that the conserved loops B and E are essential for the formation of the water pore. To test the importance of loops B and E in the determination of the transport characteristics, we exchanged loops B and/or E between AQP0, AQP2, and AQP3. Detailed functional, immunoblot and immunocytochemical analyses of expression in Xenopus oocytes revealed that six out of the nine chimeric aquaporin proteins were not functional, because of misrouting. AQP0 with loop E of AQP2 was not impaired in its routing and revealed a low water permeability equal to that of wild-type AQP0. AQP2 with loop B of AQP0 was also routed normally and gave a high water permeability, similar to that of wild-type AQP2. AQP0 with loops B and E of AQP2 (AQP0–2BE) did not result in an increase in water permeability and was partly misrouted. However, the plasma membrane expression was high enough to expect an increase in water permeability, as loops B and E of AQP2 confer AQP2’s water permeability to AQP0. Although it is unclear for the dual chimera (AQP0–2BE), the parental water permeabilities obtained in oocytes expressing AQP0 with loop E of AQP2 or AQP2 with loop B of AQP0 indicate that, besides loops B and E, other parts of the AQP protein are important in the determination of the characteristics of the channel.Type of Medium: Electronic ResourceURL: -
3Articles: DFG German National LicensesStaff View
ISSN: 1432-2013Keywords: Key words Water channel ; Transfection ; Kidney ; Transcellular osmotic transport ; Aquaporin-1 ; Protein routingSource: Springer Online Journal Archives 1860-2000Topics: MedicineNotes: Abstract Aquaporin-1 is present in the apical and basolateral membranes in proximal tubules and descending limbs of Henlé’s loop. In order to be able to study the routing of Aquaporin-1 and the regulation of Aquaporin-1-mediated transcellular water flow, we stably transfected LLC-PK1 and MDCK-HRS cell lines with an Aquaporin-1 expression construct. LLC-PK1 clone 7 and MDCK clone K integrated two and one copies, respectively, which was reflected in the amount of Aquaporin-1 mRNA expressed in both clones. The Aquaporin-1 protein levels, however, were similar. In both clones, immuno-electronmicroscopy showed extensive labelling of Aquaporin-1 on the basolateral plasma membrane, endosomal vesicles and the apical plasma membrane, including the microvilli. To measure transcellular water permeation, a simple method was applied using phenol-red as a cell-impermeant marker of concentration. In contrast to the native cell lines, both clones revealed a high transcellular osmotic water permeability, which could not be influenced by forskolin add/3-isobutyl-1-methylxanthine (IBMX) or the phorbol ester 12-O-tetradecanoyl 13-acetate (TPA). After glutaraldehyde fixation, it was inhibitable by HgCl2. These results indicate that targeting of Aquaporin-1 to the apical and basolateral plasma membrane is independent of cell type and show for the first time that water flow through a cultured epithelium can be blocked by mercurial compounds.Type of Medium: Electronic ResourceURL: