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162 results on '"Oberleithner, H."'

13. Migrating transformed MDCK cells are able to structurally polarize a voltage-activated K+ channel

Author

Reinhardt, J., Golenhofen, N., Pongs, O., Oberleithner, H., and Schwab, A.

Subjects
Cell migration -- Research, Potassium channels -- Research, Science and technology
Abstract

Cell migration of transformed renal epithelial cells (MDCK-F) depends - in addition to cytoskeletal mechanisms - on the polarized activity of a [Ca.sup.2+]-sensitive [K.sup.+] channel in the rear part of the cells. However, because of the lack of specific markers for this channel we are not able to determine whether a polarized distribution of the channel protein underlies its functional polarization. To determine whether the migrating MDCK-F cells have retained the ability to target [K.sup.+] channels to distinct membrane areas we stably transfected the cells with the voltage-dependent [K.sup.+] channel Kv1.4. Stable expression and insertion into the plasma membrane could be shown by reverse transcription-PCR, genomic PCR, Western blot, and patch-clamp techniques, respectively. The distribution of Kv1.4 was assessed with indirect immunofluorescence by using conventional and confocal microscopy. These experiments revealed that Kv1.4 is expressed only in transfected cells where it elicits the typical voltage-dependent, rapidly inactivating [K.sup.+] current. The Kv1.4 protein is clustered at the leading edge of protruding lamellipodia of migrating MDCK-F cells. This characteristic distribution of Kv1.4 provides strong evidence that migrating MDCK-F cells are able to insert ion channels into the plasma membrane in an asymmetric way, which reflects the polarization of migrating cells in the plane of movement. These findings suggest that not only epithelial cells and nerve cells, but also migrating cells, can create functionally distinct plasma membrane areas.

Published
1998

14. Structural activity of a cloned potassium channel (ROMK1) monitored with the atomic force microscope: the 'molecular-sandwich' technique

Author

Oberleithner, H., Schneider, S.W., and Henderson, R.M.

Subjects
Potassium channels -- Research, Atomic force microscopy -- Usage, Proteins -- Research, Science and technology
Abstract

The atomic force microscope (AFM) was used to continuously follow height changes of individual protein molecules exposed to physiological stimuli. A AFM tip was coated with ROMK1 (a cloned renal epithelial potassium channel known to be highly pH sensitive) and lowered onto atomically flat mica surface until the protein was sandwiched between AFM tip and mica. Because the AFM tip was an integral part of a highly flexible cantilever, any structural alterations of the sandwiched molecule were transmitted to the cantilever. This resulted in a distortion of the cantilever that was monitored by means of a laser beam. With this system it was possible to resolve vertical height changes in the ROMK1 protein of [greater than or equal to]0.2 nm (approximately 5% of the molecule's height) with a time resolution of [greater than or equal to]1 msec. When bathed in electrolyte solution that contained the catalytic subunit of protein kinase A and 0.1 mM ATP (conditions that activate the native ion channel), we found stochastically occurring height fluctuations in the ROMK1 molecule. These changes in height were pH-dependent, being greatest at pH 7.6, and lowering the pH (either by titration or by the application of C[O.sub.2]) reduced their magnitude. The data show that overall changes in shape of proteins occur stochastically and increase in size and frequency when the proteins are active. This AFM 'molecular-sandwich' technique, called MOST, measures structural activity of proteins in real time and could prove useful for studies on the relationship between structure and function of proteins at the molecular level.

Published
1997

18. Patchy accumulation of apical Na+ transporters allows cross talk between extracellular space and cell nucleus

Author

Oberleithner, H., Wunsch, S., and Schneider, S.

Subjects
Sodium channels -- Physiological aspects, Biological transport -- Physiological aspects, Science and technology
Abstract

The early detection of extracellular Na+ signal in the cell nucleus was caused by the supranuclear accumulation of Na+ transporters in the apical membrane. The existence of nonuniform and patchy accumulation of Na+ transporters surrounding the nucleus was indicated by the spatial distribution of the cation currents. The cell nucleus was believed to function as a permeable intracellular compartment that bridged the apical membrane filled with Na+ transporters to the cell cytoplasm.

Published
1992

19. Extracellular protonation modulates cell-cell interaction mechanics and tissue invasion in human melanoma cells

Author

Hofschroer, V., Koch, K.A., Ludwig, F.T., Friedl, P., Oberleithner, H., Stock, C., Schwab, A., and Universitäts- und Landesbibliothek Münster

Subjects
Sodium-Hydrogen Exchanger 1, Cancer development and immune defence Radboud Institute for Molecular Life Sciences [Radboudumc 2], Cell Communication, Hydrogen-Ion Concentration, Models, Biological, Collagen Type I, Article, Cell Movement, Cell Line, Tumor, Spheroids, Cellular, Medicine and health, Cell Adhesion, Humans, Neoplasm Invasiveness, ddc:610, Protons, Extracellular Space, Acids, Cell Adhesion Molecules, Melanoma, Cell Aggregation
Abstract

Contains fulltext : 174414.pdf (Publisher’s version ) (Open Access) Detachment of cells from the primary tumour precedes metastatic progression by facilitating cell release into the tissue. Solid tumours exhibit altered pH homeostasis with extracellular acidification. In human melanoma, the Na+/H+ exchanger NHE1 is an important modifier of the tumour nanoenvironment. Here we tested the modulation of cell-cell-adhesion by extracellular pH and NHE1. MV3 tumour spheroids embedded in a collagen matrix unravelled the efficacy of cell-cell contact loosening and 3D emigration into an environment mimicking physiological confinement. Adhesive interaction strength between individual MV3 cells was quantified using atomic force microscopy and validated by multicellular aggregation assays. Extracellular acidification from pHe7.4 to 6.4 decreases cell migration and invasion but increases single cell detachment from the spheroids. Acidification and NHE1 overexpression both reduce cell-cell adhesion strength, indicated by reduced maximum pulling forces and adhesion energies. Multicellular aggregation and spheroid formation are strongly impaired under acidification or NHE1 overexpression. We show a clear dependence of melanoma cell-cell adhesion on pHe and NHE1 as a modulator. These effects are opposite to cell-matrix interactions that are strengthened by protons extruded via NHE1. We conclude that these opposite effects of NHE1 act synergistically during the metastatic cascade.

Published
2016

20. Clathrin inhibitor Pitstop-2 disrupts the nuclear pore complex permeability barrier

Author

Liashkovich, I. (Ivan), Pasrednik, D. (Dzmitry), Prystopiuk, V. (Valeria), Rosso, G. (Gonzalo), Oberleithner, H. (Hans), Shahin, V. (Victor), and Universitäts- und Landesbibliothek Münster

Subjects
stomatognathic diseases, Sulfonamides, Cell Membrane Permeability, Medicine and health, otorhinolaryngologic diseases, Nuclear Pore, Thiazolidines, ddc:610, beta Karyopherins, Article, Clathrin, Endocytosis
Abstract

Existence of a selective nucleocytoplasmic permeability barrier is attributed to Phenylalanine-Glycine rich proteins (FG-nups) within the central channel of the nuclear pore complex (NPC). Limited understanding of the FG-nup structural arrangement hinders development of strategies directed at disrupting the NPC permeability barrier. In this report we explore an alternative approach to enhancing the NPC permeability for exogenous macromolecules. We demonstrate that the recently discovered inhibitor of clathrin coat assembly Pitstop-2 compromises the NPC permeability barrier in a rapid and effective manner. Treatment with Pitstop-2 causes a collapse of the NPC permeability barrier and a reduction of Importin β binding accompanied by alteration of the NPC ultrastructure. Interestingly, the effects are induced by the same chemical agent that is capable of inhibiting clathrin-mediated endocytosis. To our knowledge, this is the first functional indication of the previously postulated evolutionary relation between clathrin and NPC scaffold proteins.

Published
2015
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21. Extracellular protonation modulates cell-cell interaction mechanics and tissue invasion in human melanoma cells

Author

Hofschroer, V., Koch, K.A., Ludwig, F.T., Friedl, P., Oberleithner, H., Stock, C., Schwab, A., Hofschroer, V., Koch, K.A., Ludwig, F.T., Friedl, P., Oberleithner, H., Stock, C., and Schwab, A.

Abstract

Contains fulltext : 174414.pdf (publisher's version ) (Open Access), Detachment of cells from the primary tumour precedes metastatic progression by facilitating cell release into the tissue. Solid tumours exhibit altered pH homeostasis with extracellular acidification. In human melanoma, the Na+/H+ exchanger NHE1 is an important modifier of the tumour nanoenvironment. Here we tested the modulation of cell-cell-adhesion by extracellular pH and NHE1. MV3 tumour spheroids embedded in a collagen matrix unravelled the efficacy of cell-cell contact loosening and 3D emigration into an environment mimicking physiological confinement. Adhesive interaction strength between individual MV3 cells was quantified using atomic force microscopy and validated by multicellular aggregation assays. Extracellular acidification from pHe7.4 to 6.4 decreases cell migration and invasion but increases single cell detachment from the spheroids. Acidification and NHE1 overexpression both reduce cell-cell adhesion strength, indicated by reduced maximum pulling forces and adhesion energies. Multicellular aggregation and spheroid formation are strongly impaired under acidification or NHE1 overexpression. We show a clear dependence of melanoma cell-cell adhesion on pHe and NHE1 as a modulator. These effects are opposite to cell-matrix interactions that are strengthened by protons extruded via NHE1. We conclude that these opposite effects of NHE1 act synergistically during the metastatic cascade.

Published
2017

22. Standardized Nanomechanical Atomic Force Microscopy Procedure (SNAP) for Measuring Soft and Biological Samples

Author

UCL - SST/LIBST - Louvain Institute of Biomolecular Science and Technology, Schillers, H., Rianna, C., Schäpe, J., Luque, T., Doschke, H., Wälte, M., Uriarte, J.J., Campillo, N., Michanetzis, G.P.A., Bobrowska, J., Dumitru, A.C., Herruzo, E.T., Bovio, S., Parot, P., Galluzzi, M., Podestà, A., Puricelli, L., Scheuring, S., Missirlis, Y., Garcia, R., Odorico, M., Teulon, J.-M., Lafont, F., Lekka, M., Rico, F., Rigato, A., Pellequer, J.-L., Oberleithner, H., Navajas, D., Radmacher, M., UCL - SST/LIBST - Louvain Institute of Biomolecular Science and Technology, Schillers, H., Rianna, C., Schäpe, J., Luque, T., Doschke, H., Wälte, M., Uriarte, J.J., Campillo, N., Michanetzis, G.P.A., Bobrowska, J., Dumitru, A.C., Herruzo, E.T., Bovio, S., Parot, P., Galluzzi, M., Podestà, A., Puricelli, L., Scheuring, S., Missirlis, Y., Garcia, R., Odorico, M., Teulon, J.-M., Lafont, F., Lekka, M., Rico, F., Rigato, A., Pellequer, J.-L., Oberleithner, H., Navajas, D., and Radmacher, M.

Published
2017

25. An emerging concept of vascular salt sensitivity in man

Author

Oberleithner, H.

Abstract

For millions of years, daily sodium chloride intake in man was about 1g. Then recently, about 10,000 years ago, salt intake increased by about ten-fold because of the practice of using salt as a food preservative. If salt intake exceeds the kidneys’ ability for salt excretion, then salt is deposited in the body which affects heart, blood vessels and kidneys. In this context, the endothelial surface layer facing the blood stream became a focus of interest. This soft layer, termed endothelial glycocalyx, is a negatively charged biopolymer known to preferentially bind sodium. After a salty meal, the translocation of sodium from the blood into the interstitium is delayed by the significant buffering capacity of the endothelial glycocalyx. Excessive sodium intake over long periods damages the glycocalyx and leads to a decrease in its sodium buffering capacity. It has been shown recently that, after mechanical interaction of blood with a damaged endothelial glycocalyx, erythrocyte surfaces also become damaged [1]. This observation led to the conclusion that vascular sodium buffer capacity of an individual could be derived from a blood sample. A test system (Salt-Blood-Test; SBT) was developed based upon the sodium-dependent erythrocyte zeta-potential [2]. Erythrocyte sedimentation velocity was measured in isosmotic, biopolymer-supplemented electrolyte solutions of different sodium concentrations. Erythrocyte sodium sensitivity (ESS), inversely related to erythrocyte sodium buffer capacity, was expressed as the ratio of the erythrocyte sedimentation velocities of 150 over 125 mM Na + solutions (ESS = 150Na +/125Na +). In 61 healthy individuals (mean age: (23.0 ± 0.5) years) ESS ranged between 2 and 8. The mean value was 4.30 ± 0.19. In conclusion, the SBT could serve as an in vitro test system for the evaluation of salt sensitivity allowing follow-up measurements in the prevention and treatment of vascular dysfunctions.

Published
2013

26. Nanomechanics of the endothelial glycocalyx in experimental sepsis

Author

Wiesinger, V. (Véronique), Peters, W. (Wladimir), Chappell, D. (Daniel), Kentrup, D. (Dominik), Reuter, S.J. (Stefan), Pavenstädt, H. (Hermann), Oberleithner, H. (Hans), Kümpers, P. (Philipp), and Universitäts- und Landesbibliothek Münster

Subjects
Male, Time Factors, Cell Survival, lcsh:R, lcsh:Medicine, Glycocalyx, Microscopy, Atomic Force, Endotoxemia, Mice, Inbred C57BL, Sepsis, Medicine and health, Animals, Humans, Nanoparticles, lcsh:Q, ddc:610, Endothelium, lcsh:Science, Aorta, Research Article
Abstract

The endothelial glycocalyx (eGC), a carbohydrate-rich layer lining the luminal side of the endothelium, regulates vascular adhesiveness and permeability. Although central to the pathophysiology of vascular barrier dysfunction in sepsis, glycocalyx damage has been generally understudied, in part because of the aberrancy of in vitro preparations and its degradation during tissue handling. The aim of this study was to analyze inflammation-induced damage of the eGC on living endothelial cells by atomic-force microscopy (AFM) nanoindentation technique. AFM revealed the existence of a mature eGC on the luminal endothelial surface of freshly isolated rodent aorta preparations ex vivo, as well as on cultured human pulmonary microvascular endothelial cells (HPMEC) in vitro. AFM detected a marked reduction in glycocalyx thickness (266 ± 12 vs. 137 ± 17 nm, P

Published
2013

27. Correction

Author

Schillers, H., Walte, M., Urbanova, K., and Oberleithner, H.

Subjects
Biophysics, Correction
Published
2011

28. Small GTPasen beeinflussen die chondrogene Differenzierung von humanen fettgewebe-assoziierten adulten Stammzellen (ASC)

Author

Jungmann, P, Mehlhorn, A, Schillers, H, Oberleithner, H, Schmal, H, and Südkamp, NP

Subjects
ddc: 610, 610 Medical sciences, Medicine
Abstract

Fragestellung: Humane fettgewebe-assoziierte adulte Stammzellen (ASC) exprimieren nach Kultivierung in 3D Alginate Beads in chondrogenem Differenzierungsmedium vermehrt chondrospezifische Marker wie Kollagen Typ II, haben jedoch eine Tendenz zur zellulären Hypertrophie mit Expression des Kollagens[for full text, please go to the a.m. URL], Deutscher Kongress für Orthopädie und Unfallchirurgie; 74. Jahrestagung der Deutschen Gesellschaft für Unfallchirurgie, 96. Tagung der Deutschen Gesellschaft für Orthopädie und Orthopädische Chirurgie, 51. Tagung des Berufsverbandes der Fachärzte für Orthopädie

Published
2010
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30. Experimental pathology

Author

Yi Chun, D. X., primary, Alexandre, H., additional, Edith, B., additional, Nacera, O., additional, Julie, P., additional, Chantal, J., additional, Eric, R., additional, Zhang, X., additional, Jin, Y., additional, Miravete, M., additional, Dissard, R., additional, Klein, J., additional, Gonzalez, J., additional, Caubet, C., additional, Pecher, C., additional, Pipy, B., additional, Bascands, J.-L., additional, Mercier-Bonin, M., additional, Schanstra, J., additional, Buffin-Meyer, B., additional, Claire, R., additional, Rigothier, C., additional, Richard, D., additional, Sebastien, L., additional, Moin, S., additional, Chantal, B., additional, Christian, C., additional, Jean, R., additional, Migliori, M., additional, Cantaluppi, V., additional, Mannari, C., additional, Medica, D., additional, Giovannini, L., additional, Panichi, V., additional, Goldwich, A., additional, Alexander, S., additional, Andre, G., additional, Amann, K., additional, Migliorini, A., additional, Sagrinati, C., additional, Angelotti, M. L., additional, Mulay, S. R., additional, Ronconi, E., additional, Peired, A., additional, Romagnani, P., additional, Anders, H.-J., additional, Chiang, W. C., additional, Lai, C. F., additional, Peng, W.-H., additional, Wu, C. F., additional, Chang, F.-C., additional, Chen, Y.-T., additional, Lin, S.-L., additional, Chen, Y. M., additional, Wu, K. D., additional, Lu, K.-S., additional, Tsai, T. J., additional, Virgine, O., additional, Qing Feng, F., additional, Zhang, S.-Y., additional, Dominique, D., additional, Vincent, A., additional, Marina, C., additional, Philippe, L., additional, Georges, G., additional, Pawlak, A., additional, Sahali, D., additional, Matsumoto, S., additional, Kiyomoto, H., additional, Ichimura, A., additional, Dan, T., additional, Nakamichi, T., additional, Tsujita, T., additional, Akahori, K., additional, Ito, S., additional, Miyata, T., additional, Xie, S., additional, Zhang, B., additional, Shi, W., additional, Yang, Y., additional, Nagasu, H., additional, Satoh, M., additional, Kidokoro, K., additional, Nishi, Y., additional, Ihoriya, C., additional, Kadoya, H., additional, Sasaki, T., additional, Kashihara, N., additional, Wu, C.-F., additional, Chou, Y.-H., additional, Duffield, J., additional, Rocca, C., additional, Gregorini, M., additional, Corradetti, V., additional, Valsania, T., additional, Bedino, G., additional, Bosio, F., additional, Pattonieri, E. F., additional, Esposito, P., additional, Sepe, V., additional, Libetta, C., additional, Rampino, T., additional, Dal Canton, A., additional, Omori, H., additional, Kawada, N., additional, Inoue, K., additional, Ueda, Y., additional, Yamamoto, R., additional, Matsui, I., additional, Kaimori, J., additional, Takabatake, Y., additional, Moriyama, T., additional, Isaka, Y., additional, Rakugi, H., additional, Wasilewska, A., additional, Taranta-Janusz, K., additional, Deebek, W., additional, Kuroczycka-Saniutycz, E., additional, Lee, A. S., additional, Lee, J. E., additional, Jung, Y. J., additional, Kang, K. P., additional, Lee, S., additional, Kim, W., additional, Arfian, N., additional, Emoto, N., additional, Yagi, K., additional, Nakayama, K., additional, Hartopo, A. B., additional, Nugrahaningsih, D. A., additional, Yanagisawa, M., additional, Hirata, K.-I., additional, Munoz-Felix, J. M., additional, Lopez-Novoa, J. M., additional, Martinez-Salgado, C., additional, Oujo, B., additional, Arevalo, M., additional, Bernabeu, C., additional, Perez-Barriocanal, F., additional, Jesper, K., additional, Nathalie, V., additional, Pierre, G., additional, Yi Chun, D. X., additional, Iyoda, M., additional, Shibata, T., additional, Matsumoto, K., additional, Shindo-Hirai, Y., additional, Kuno, Y., additional, Wada, Y., additional, Akizawa, T., additional, Schwartz, I., additional, Schwartz, D., additional, Prot Bertoye, C., additional, Terryn, S., additional, Claver, J., additional, Beghdadi, W. B., additional, Monteiro, R., additional, Blank, U., additional, Devuyst, O., additional, Daugas, E., additional, Van Beneden, K., additional, Geers, C., additional, Pauwels, M., additional, Mannaerts, I., additional, Van den Branden, C., additional, Van Grunsven, L. A., additional, Seckin, I., additional, Pekpak, M., additional, Uzunalan, M., additional, Uruluer, B., additional, Kokturk, S., additional, Ozturk, Z., additional, Sonmez, H., additional, Yaprak, E., additional, Furuno, Y., additional, Tsutsui, M., additional, Morishita, T., additional, Shimokawa, H., additional, Otsuji, Y., additional, Yanagihara, N., additional, Kabashima, N., additional, Ryota, S., additional, Kanegae, K., additional, Miyamoto, T., additional, Nakamata, J., additional, Ishimatsu, N., additional, Tamura, M., additional, Nakagawa, T., additional, Ichikawa, K., additional, Miyamoto, M., additional, Takabayashi, D., additional, Yamazaki, H., additional, Kakeshita, K., additional, Koike, T., additional, Kagitani, S., additional, Tomoda, F., additional, Hamashima, T., additional, Ishii, Y., additional, Inoue, H., additional, Sasahara, M., additional, El Machhour, F., additional, Kerroch, M., additional, Mesnard, L., additional, Chatziantoniou, C., additional, Dussaule, J.-C., additional, Inui, K., additional, Sasai, F., additional, Maruta, Y., additional, Nishiwaki, H., additional, Kawashima, E., additional, Inoue, Y., additional, Yoshimura, A., additional, Musacchio, E., additional, Priante, G., additional, Valvason, C., additional, Sartori, L., additional, Baggio, B., additional, Kim, J. H., additional, Gross, O., additional, Diana, R., additional, Gry, D. H., additional, Asimal, B., additional, Johanna, T., additional, Imke, S.-E., additional, Lydia, W., additional, Gerhard-Anton, M., additional, Hassan, D., additional, Cano, J. L., additional, Griera, M., additional, Olmos, G., additional, Martin, P., additional, Cortes, M. A., additional, Lopez-Ongil, S., additional, Rodriguez-Puyol, D., additional, DE Frutos, S., additional, Gonzalez, M., additional, Luengo, A., additional, Rodriguez-Puyol, M., additional, Calleros, L., additional, Lupica, R., additional, Lacquaniti, A., additional, Donato, V., additional, Maggio, R., additional, Mastroeni, C., additional, Lucisano, S., additional, Cernaro, V., additional, Fazio, M. R., additional, Quartarone, A., additional, Buemi, M., additional, Kacik, M., additional, Goedicke, S., additional, Eggert, H., additional, Hoyer, J. D., additional, Wurm, S., additional, Steege, A., additional, Banas, M., additional, Kurtz, A., additional, Banas, B., additional, Lasagni, L., additional, Lazzeri, E., additional, Romoli, S., additional, Schaefer, I., additional, Teng, B., additional, Worthmann, K., additional, Haller, H., additional, Schiffer, M., additional, Prattichizzo, C., additional, Netti, G. S., additional, Rocchetti, M. T., additional, Cormio, L., additional, Carrieri, G., additional, Stallone, G., additional, Grandaliano, G., additional, Ranieri, E., additional, Gesualdo, L., additional, Kucher, A., additional, Smirnov, A., additional, Parastayeva, M., additional, Beresneva, O., additional, Kayukov, I., additional, Zubina, I., additional, Ivanova, G., additional, Abed, A., additional, Schlekenbach, L., additional, Foglia, B., additional, Kwak, B., additional, Chadjichristos, C., additional, Queisser, N., additional, Schupp, N., additional, Brand, S., additional, Himer, L., additional, Szebeni, B., additional, Sziksz, E., additional, Saijo, S., additional, Kis, E., additional, Prokai, A., additional, Banki, N. F., additional, Fekete, A., additional, Tulassay, T., additional, Vannay, A., additional, Hegner, B., additional, Schaub, T., additional, Lange, C., additional, Dragun, D., additional, Klinkhammer, B. M., additional, Rafael, K., additional, Monika, M., additional, Anna, M., additional, Van Roeyen, C., additional, Boor, P., additional, Eva Bettina, B., additional, Simon, O., additional, Esther, S., additional, Floege, J., additional, Kunter, U., additional, Janke, D., additional, Jankowski, J., additional, Hayashi, M., additional, Takamatsu, I., additional, Horimai, C., additional, Yoshida, T., additional, Seno DI Marco, G., additional, Koenig, M., additional, Stock, C., additional, Reiermann, S., additional, Amler, S., additional, Koehler, G., additional, Fobker, M., additional, Buck, F., additional, Pavenstaedt, H., additional, Lang, D., additional, Brand, M., additional, Plotnikov, E., additional, Morosanova, M., additional, Pevzner, I., additional, Zorova, L., additional, Pulkova, N., additional, Zorov, D., additional, Wornle, M., additional, Ribeiro, A., additional, Belling, F., additional, Merkle, M., additional, Nakazawa, D., additional, Nishio, S., additional, Shibasaki, S., additional, Tomaru, U., additional, Akihiro, I., additional, Kobayashi, I., additional, Imanishi, Y., additional, Kurajoh, M., additional, Nagata, Y., additional, Yamagata, M., additional, Emoto, M., additional, Michigami, T., additional, Ishimura, E., additional, Inaba, M., additional, Wu, C.-C., additional, Lu, K.-C., additional, Chen, J.-S., additional, Chu, P., additional, Lin, Y.-F., additional, Eller, K., additional, Schroll, A., additional, Kirsch, A., additional, Huber, J., additional, Weiss, G., additional, Theurl, I., additional, Rosenkranz, A. R., additional, Zawada, A., additional, Rogacev, K., additional, Achenbach, M., additional, Fliser, D., additional, Held, G., additional, Heine, G. H., additional, Miyamoto, Y., additional, Iwao, Y., additional, Watanabe, H., additional, Kadowaki, D., additional, Ishima, Y., additional, Chuang, V. T. G., additional, Sato, K., additional, Otagiri, M., additional, Maruyama, T., additional, Iwatani, H., additional, Honda, D., additional, Noguchi, T., additional, Tanaka, M., additional, Tanaka, H., additional, Fukagawa, M., additional, Pircher, J., additional, Koppel, S., additional, Mannell, H., additional, Krotz, F., additional, Virzi, G. M., additional, Bolin, C., additional, Cruz, D., additional, Scalzotto, E., additional, De Cal, M., additional, Vescovo, G., additional, Ronco, C., additional, Grobmayr, R., additional, Lech, M., additional, Ryu, M., additional, Aoshima, Y., additional, Mizobuchi, M., additional, Ogata, H., additional, Kumata, C., additional, Nakazawa, A., additional, Kondo, F., additional, Ono, N., additional, Koiwa, F., additional, Kinugasa, E., additional, Freisinger, W., additional, Lale, N., additional, Lampert, A., additional, Ditting, T., additional, Heinlein, S., additional, Schmieder, R. E., additional, Veelken, R., additional, Nave, H., additional, Perthel, R., additional, Suntharalingam, M., additional, Bode-Boger, S., additional, Beutel, G., additional, Kielstein, J., additional, Rodrigues-Diez, R., additional, Rayego-Mateos, S., additional, Lavoz, C., additional, Stark Aroeira, L. G., additional, Orejudo, M., additional, Alique, M., additional, Ortiz, A., additional, Egido, J., additional, Ruiz-Ortega, M., additional, Oskar, W., additional, Rusan, C., additional, Padberg, J.-S., additional, Wiesinger, A., additional, Reuter, S., additional, Grabner, A., additional, Kentrup, D., additional, Lukasz, A., additional, Oberleithner, H., additional, Pavenstadt, H., additional, Kumpers, P., additional, Eberhardt, H. U., additional, Skerka, C., additional, Chen, Q., additional, Hallstroem, T., additional, Hartmann, A., additional, Kemper, M. J., additional, Zipfel, P. F., additional, N'gome-Sendeyo, K., additional, Fan, Q.-F., additional, Toblli, J., additional, Cao, G., additional, Giani, J. F., additional, Dominici, F. P., additional, Kim, J. S., additional, Yang, J. W., additional, Kim, M. K., additional, Han, B. G., additional, and Choi, S. O., additional

Published
2012
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31. Correction

Author

Schillers, H., primary, Walte, M., additional, Urbanova, K., additional, and Oberleithner, H., additional

Published
2011
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40. 17β-estradiol increases volume, apical surface and elasticity of human endothelium mediated by Na+/H+ exchange

Author

Hillebrand, U., Hausberg, M., Stock, C., Shahin, V., Nikova, D., Riethmüller, C., Kliche, K., Ludwig, T., Schillers, H., Schneider, S.W., and Oberleithner, H.

Subjects
ESTROGEN, ATOMIC force microscopy, SCANNING probe microscopy, CELL membranes
Abstract

Abstract: Objective: 17β-estradiol is known to delay the onset of atherosclerosis in women but cellular mechanisms are still unclear. Estrogens bind to specific receptors and initiate a signaling cascade that involves the activation of plasma membrane Na+/H+ exchange. We hypothesized that estrogens interfere with ion transport across the plasma membrane and thus control endothelial structure and function. Therefore, we investigated the effects of the sex steroids 17β-estradiol, progesterone, and testosterone on volume, apical surface and elasticity in human endothelium. Methods: The atomic force microscope was used as an imaging tool and as an elasticity sensor. We applied the antiestrogen tamoxifen, the Na+/H+ exchange blocker cariporide and the epithelial Na+channel blocker amiloride to elucidate the role of transmembrane ion transport in hormone-treated human umbilical vein endothelial cells (HUVEC). Results: Incubation with 17β-estradiol for 72 h led to a dose-dependent increase of endothelial cell volume (41%), apical cell surface (22%), and cell elasticity (53%) as compared to non-17β-estradiol treated controls. Block of the 17β-estradiol receptor by tamoxifen and of plasma membrane Na+/H+ exchange by cariporide prevented the hormone-induced changes. Progesterone and testosterone were ineffective. Conclusions: 17β-estradiol increases HUVEC water content and HUVEC elasticity mediated by activated estrogen receptors. The estrogen response depends on the activation of plasma membrane Na+/H+ exchange. The increase in endothelial cell elasticity could be one of the vasoprotective mechanisms postulated for 17β-estradiol. [Copyright &y& Elsevier]

Published
2006
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41. Stimulation of protein kinase C pathway mediates endocytosis of human nongastric H[sup +]-K[sup +]-ATPase, ATP1AL1.

Author

Reinhardt, J., Kosch, M., Lerner, M., Bertram, H., Lemke, D., and Oberleithner, H.

Subjects
PROTEIN kinase C, ENDOCYTOSIS
Abstract

Examines the stimulation of protein kinase C pathways for human endocytosis. Details on the luminal plasma membrane of renal epithelial cells; Regulation of adenosine triphosphate (ATPase) by endocytosis; Influence of protein kinase C on plasma membrane expression of nongastric ATPases.

Published
2002
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42. Relationship between cell volume and ion transport in the early distal tubule of the Amphiuma kidney.

Author

Guggino, W B, Oberleithner, H, and Giebisch, G

Abstract

The roles of apical and basolateral transport mechanisms in the regulation of cell volume and the hydraulic water permeabilities (Lp) of the individual cell membranes of the Amphiuma early distal tubule (diluting segment) were evaluated using video and optical techniques as well as conventional and Cl-sensitive microelectrodes. The Lp of the apical cell membrane calculated per square centimeter of tubule is less than 3% that of the basolateral cell membrane. Calculated per square centimeter of membrane, the Lp of the apical cell membrane is less than 40% that of the basolateral cell membrane. Thus, two factors are responsible for the asymmetry in the Lp of the early distal tubule: an intrinsic difference in the Lp per square centimeter of membrane area, and a difference in the surface areas of the apical and basolateral cell membranes. Early distal tubule cells do not regulate volume after a reduction in bath osmolality. This cell swelling occurs without a change in the intracellular Cl content or the basolateral cell membrane potential. In contrast, reducing the osmolality of the basolateral solution in the presence of luminal furosemide diminishes the magnitude of the increase in cell volume to a value below that predicted from the change in osmolality. This osmotic swelling is associated with a reduction in the intracellular Cl content. Hence, early distal tubule cells can lose solute in response to osmotic swelling, but only after the apical Na/K/Cl transporter is blocked. Inhibition of basolateral Na/K ATPase with ouabain results in severe cell swelling. This swelling in response to ouabain can be inhibited by the prior application of furosemide, which suggests that the swelling is due to the continued entry of solutes, primarily through the apical cotransport pathway.

Published
1985
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43. Aldosterone activates Na+/H+ exchange and raises cytoplasmic pH in target cells of the amphibian kidney.

Author

Oberleithner, H, Weigt, M, Westphale, H J, and Wang, W

Abstract

The hypothesis was tested if the mineralocorticoid hormone aldosterone stimulates Na+/H+ exchange in "giant cells" fused from individual target cells of the distal nephron of the frog kidney. By means of microelectrodes, steady-state intracellular pH (pHi) and pHi recovery from an acid load were recorded continuously while the fused cells were exposed to aldosterone. Twenty minutes after addition of the hormone, pHi started to rise and reached a new steady state after about 60 min (delta pHi = 0.28 +/- 0.01). After hormone treatment, pHi recovered significantly faster in response to an intracellular acid load. The diuretic drug amiloride blocked pHi recovery. Experiments in intact tubules showed that aldosterone induces H+ and K+ secretion. Thus, intracellular alkalosis, mediated by Na+/H+ exchange, could serve as a signal that activates pH-sensitive K+ channels of the luminal cell membrane.

Published
1987
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44. Exocytosis of haemostatic active von Willebrand factor multimers on human endothelial cells measured by using atomic force microscopy.

Author

Schneider, S. W., Ossig, R., Barg, A., and Oberleithner, H.

Subjects
*VON Willebrand factor, *BLOOD coagulation factors, *EXOCYTOSIS, *CELL physiology, *HEMOSTASIS, *ATOMIC force microscopy
Abstract

Von Willebrand factor (vWF) is the major player of the first response of primary haemostasis and inflammation. Immobilized to the subendothelial cell matrix vWF is exposed after endothelial cell (EC) damage to initiate platelet clotting. Our data indicate that vWF is also released at the luminal surface of EC mediating platelet adhesion. By using atomic force microscopy (AFM) we visualized the luminal surface topography of EC. Submembrane Weibel-Palade bodies (WPB; storage vesicles of vWF) can be imaged as humps charact-erized by decreased cell membrane stiffness. After cell stimulation (hyperosmolaric solutions or histamine) these docked WPB fuse with the plasma membrane forming large exocytotic pores (d∼300 nm). Release of vWF from these pores was visualized by using immuno-fluorescence after staining the same cell surface with vWF-specific antibodies. Surprisingly, high molecular weight multimers of vWF were found to form elongated fibre-like structures (>200 μm in length) on the EC cell surface. After adding platelet-poor plasma during a 3 minute stimulation time cell surface attached platelets were found to be almost exclusively sticking to vWF fibres. Moreover, we confirmed that luminal release and surface attachment of high-molecular weight vWF fibres on EC at the intact human vessel wall. In contrast to the exocytotic pores we imaged endocytotic pores with sharp edges and a diameter of ∼200 nm.The study shows that AFM enables to measure and visualize cell surface topography with a nanometer resolution. The data indicate a new concept for a physiological function of vWF to effectively recruite platelets and leucocytes to the intact but stimulated vessel wall surface. [ABSTRACT FROM AUTHOR]

Published
2004
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45. Endothelial cortical nanodynamics under hydrostatic pressure influence

Author

Prystopiuk, V. (Valeria), Oberleithner, H. (Hans), and Universitäts- und Landesbibliothek Münster

Subjects
Druck, Zellkortex, Acto-Myosin Dynamik, Nanodynamik, Endothel Zellen, ddc:570, Biology
Abstract

In dieser Studie konzentrieren wir uns auf die Untersuchung akuter transienter Druckunterschiede sowie eventueller Unterschiede zwischen akuten und chronischen Druckeinflüssen auf Endothelzellen. Abhängig von der Zeitspanne der Druckapplikation konnten wir zwei mögliche zelluläre Mechanismen identifizieren. Eine kurzfristige Druckapplikation (1 Stunde) führt zu einer reversiblen Versteifung des endothelialen Zellkortex aufgrund einer Erhöhung der Expression und Phosphorylierung von nicht-Muskel-Myosin II. Eine chronische Druckapplikation der Endothelzellen führt wiederum zu einer globalen Umlagerung des Aktin-Netzwerkes sowie zu einer Augmentation der Aktin-Filamente im apikalen Zellkortex. Folglich stellt der hydrostatische Druck per se wahrscheinlich einen Stimulus dar, welcher die vaskuläre Endothelzellfunktion moduliert und somit in der kardiovaskulären Forschung Berücksichtigung finden sollte.

Published
2016

46. Akute und postkonditionelle Effekte von Hypoxie, Azidose und Temperatur auf die Endothelzellfunktion

Author

Rogge, P. (Phillip), Oberleithner, H. (Hans), and Universitäts- und Landesbibliothek Münster

Subjects
Medicine and health, ddc:610, Endothel, Hypoxie, Azidose, Temperatur, Exozytose, von-Willebrand-Faktor
Abstract

Endothelzellen sind für Blutgerinnung und Entzündungsmediation insbesondere durch die Exozytose der von-Willebrand-Faktor (vWF) enthaltenden Weibel-Palade-Körperchen essentiell. Anhand von humanen Nabelschnurvenenendothelzellen (HUVEC) konnte mittels vWF-ELISA, Rasterkraftmikroskopie und Immunfluoreszenz gezeigt werden, dass a) die vWF-Freisetzung stark temperaturabhängig (33¡C Ð25%, bei 41¡C +25% gegenüber 37¡C) ist und die Morphologie der entstehenden vWF-Netze auf der Zellmembran sich hin zu feineren, verzweigteren Netzen unter 41¡C bzw. plumperen Netzen unter 33¡C ändert. b) die bereits unter Hypoxie gezeigte Sekretionszunahme durch eine begleitenden Azidose verhindert wird, jedoch mit einer im Nachgang anhaltenden Sekretionssteigerung auf dem Niveau der azidosefreien Hypoxie, wobei sich das unter Azidose erhöhte Zellvolumen sich nach Realkalisierung schnell normalisiert. Darüber hinaus wurden technische Verbesserung zur Temperaturoptimierung bei Experimenten erreicht.

Published
2013

47. Vektorieller HCO3- -Transport in submukösen Drüsenzellen

Author

Waltz, A.C. (Andrea), Oberleithner, H. (Hans), and Universitäts- und Landesbibliothek Münster

Subjects
Medicine and health, HCO3- -Transport, CFTR, Calu-3 Zellen, Atemwegsepithelien, pH -Wert, ddc:610
Abstract

Um die Bedeutung des HCO3- -Transportes in Atemwegen genauer zu verstehen, wurden die dafür verantwortlichen Systeme von Calu-3 Zellen untersucht. Eingesetzt wurden fluoreszenzoptische Messungen des pH -Wertes sowie elektrophysiologische Methoden zur Bestimmung des Membranpotentials. Calu-3 Zellen exprimieren die Isoform 1 der Natriumprotonenaustauscher und die renale Isoform der H+/K+ -ATPase. Die Depolarisation durch Stimulation des cAMP -Weges führte zu einer Verstärkung, Hyperpolarisation durch Kaliumkanalaktivatoren zu einer Hemmung des HCO3- -Importes, was für einen elektrogenen NBC spricht. Außerdem ist ein DIDS insensitiver, aber Glibenclamid empfindlicher Prozess am HCO3- -Export dieser Zellen beteiligt. Unsere Daten lassen vermuten, dass es sich hierbei um einen durch CFTR vermittelten Mechanismus handelt. Eine eingeschränkte Funktion dieses Kanals würde somit die HCO3- -Sekretion in Atemwegsepithelien vermindern.

Published
2006

48. Die Sortierung der menschlichen, nicht gastrischen H + , K + -ATPase, ATP1AL1, in Nierenepithelzellen

Author

Lerner, M. (Markus), Oberleithner, H. (Hans), and Universitäts- und Landesbibliothek Münster

Subjects
Epithel, Proteinsortierung, P-Typ-ATPase, H, K-ATPase, ATP1AL1, GFP, Medicine and health, ddc:610
Abstract

Nierenepithelzellen verfügen über unterschiedliche Plasmamembrandomänen, die mit spezifischen Transmembranproteinen ausgestattet sind. Diese Differenzierung erfordert Sortierungssignale, die in polarisierte Proteine integriert sein können. Die menschliche, nicht gastrische H+,K+-ATPase, ATP1AL1, gehört zu den P-Typ-ATPasen u. wird vorherrschend apikal lokalisiert, wo sie an der K+- u. Na+- Resorption u. Protonensekretion teilnimmt. Ziel der Arbeit war, das Sortierungssignal von ATP1AL1 einzugrenzen u. neue Erkenntnisse über apikale Proteinsortierung zu gewinnen. In MDCK-Zellen wurde die Sortierung mittels Chimären zwischen ATP1AL1 und der basolateralen Na+,K+-ATPase untersucht. In vitro wurde ATP1AL1 über ein gekoppeltes Autofluoreszenzprotein (GFP) erforscht. Es stellte sich heraus, dass v. a. eine Aminosäure in der 2. Ektodomäne für die apikale Sortierung entscheidend ist und die polare Ausrichtung der ATPase vermutlich Mikrotubuli-abhängig ist.

Published
2005

49. Intravascular adhesion and recruitment of neutrophils in response to CXCL1 depends on their TRPC6 channels.

Author

Lindemann O, Rossaint J, Najder K, Schimmelpfennig S, Hofschröer V, Wälte M, Fels B, Oberleithner H, Zarbock A, and Schwab A

Subjects
Animals, Calcium metabolism, Cell Adhesion, Chemotaxis, Kidney immunology, Kidney metabolism, Kidney Diseases metabolism, Mice, Mice, Inbred C57BL, Mice, Knockout, Reperfusion Injury metabolism, Chemokine CXCL1 immunology, Kidney Diseases immunology, Neutrophils physiology, Reperfusion Injury immunology, TRPC6 Cation Channel immunology
Abstract

Here we report a novel role for TRPC6, a member of the transient receptor potential (TRPC) channel family, in the CXCL1-dependent recruitment of murine neutrophil granulocytes. Representing a central element of the innate immune system, neutrophils are recruited from the blood stream to a site of inflammation. The recruitment process follows a well-defined sequence of events including adhesion to the blood vessel walls, migration, and chemotaxis to reach the inflammatory focus. A common feature of the underlying signaling pathways is the utilization of Ca 2+ ions as intracellular second messengers. However, the required Ca 2+ influx channels are not yet fully characterized. We used WT and TRPC6 -/- neutrophils for in vitro and TRPC6 -/- chimeric mice (WT mice with WT or TRPC6 -/- bone marrow cells) for in vivo studies. After renal ischemia and reperfusion injury, TRPC6 -/- chimeric mice had an attenuated TRPC6 -/- neutrophil recruitment and a better outcome as judged from the reduced increase in the plasma creatinine concentration. In the cremaster model CXCL1-induced neutrophil adhesion, arrest and transmigration were also decreased in chimeric mice with TRPC6 -/- neutrophils. Using atomic force microscopy and microfluidics, we could attribute the recruitment defect of TRPC6 -/- neutrophils to the impact of the channel on adhesion to endothelial cells. Mechanistically, TRPC6 -/- neutrophils exhibited lower Ca 2+ transients during the initial adhesion leading to diminished Rap1 and β 2 integrin activation and thereby reduced ICAM-1 binding. In summary, our study reveals that TRPC6 channels in neutrophils are crucial signaling modules in their recruitment from the blood stream in response to CXCL1. KEY POINT: Neutrophil TRPC6 channels are crucial for CXCL1-triggered activation of integrins during the initial steps of neutrophil recruitment.

Published
2020
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50. A two-phase response of endothelial cells to hydrostatic pressure.

Author

Prystopiuk V, Fels B, Simon CS, Liashkovich I, Pasrednik D, Kronlage C, Wedlich-Söldner R, Oberleithner H, and Fels J

Subjects
Humans, Endothelial Cells metabolism, Hydrostatic Pressure
Abstract

The vascular endothelium is exposed to three types of mechanical forces: blood flow-mediated shear stress, vessel diameter-dependent wall tension and hydrostatic pressure. Despite considerable variations of blood pressure during normal and pathological physiology, little is known about the acute molecular and cellular effects of hydrostatic pressure on endothelial cells. Here, we used a combination of quantitative fluorescence microscopy, atomic force microscopy and molecular perturbations to characterize the specific response of endothelial cells to application of pressure. We identified a two-phase response of endothelial cells with an initial response to acute (1 h) application of pressure (100 mmHg) followed by a different response to chronic (24 h) application. While both regimes induce cortical stiffening, the acute response is linked to Ca 2 + -mediated myosin activation, whereas the chronic cell response is dominated by increased cortical actin density and a loss in endothelial barrier function. GsMTx-4 and amiloride inhibit the acute pressure response, which suggests that the ENaC Na + channel is a key player in endothelial pressure sensing. The described two-phase pressure response may participate in the differential effects of transient changes in blood pressure and hypertension., Competing Interests: Competing interestsThe authors declare no competing or financial interests., (© 2018. Published by The Company of Biologists Ltd.)

Published
2018
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