Publikationsserver der Universitätsbibliothek Marburg

Titel:Proteinkomponenten und Transportwege an der apikalen Membran polarer Epithelzellen
Autor:Greb, Christoph
Weitere Beteiligte: Maier, Uwe G. (Prof. Dr.)
Veröffentlicht:2011
URI:https://archiv.ub.uni-marburg.de/diss/z2011/0103
URN: urn:nbn:de:hebis:04-z2011-01037
DOI: https://doi.org/10.17192/z2011.0103
DDC: Biowissenschaften, Biologie
Titel (trans.):Protein-Components and Transport-Pathways at the Apical Membrane of Polarized Epithelial Cells
Publikationsdatum:2011-06-28
Lizenz:https://rightsstatements.org/vocab/InC-NC/1.0/

Dokument

Schlagwörter:
polarized epithelial cells, Mx1, Mx1, Galectin-3, apikaler Proteintransport, Galectin-3, galectin-3, apikaler Proteintransport, Polare Epithelzellen, Polare Epithelzellen, apical protein transport, Mx1
Referenziert von:

Zusammenfassung:
Polare Epithelzellen stellen einen essentiellen Baustein für die korrekte Funktion eines Organes dar. Sie bilden ein Monolayer an den Organaußengrenzen aus und stellen sowohl eine Barriere gegen, als auch ein Austauschsystem mit der Umwelt dar. Um diese speziellen Aufgaben wahrzunehmen, bedarf es einer geordneten und spezialisierten Aufteilung der Zytoplasmamembran. Die apikale Zytoplasmamembran ist dabei zur Außenwelt orientiert, während die basolaterale Zytoplasmamembran an benachbarte Zellen oder die Basallamina angrenzt. Für die Aufrechterhaltung dieser Polarität ist ein spezielles Protein- und Lipidsortiersystem nötig. Dabei sind bis dato zwei Grundlegende Proteinsortierplattformen bekannt. Zum einen handelt es sich um die Lipid-Raft-assoziierte Sortierung, bei der sich Proteine mit Vorlieben für solche Detergens-resistenten Membranmikrodomänen in diesen sammeln und als hochmolekulare Cluster zur Oberfläche transportiert werden. Zum anderen existiert ein Sortierweg, der auf der Bindung von Galectin-3 an die zu sortierenden Glykoproteine basiert. Auch in diesem Lipid-Raft-unabhängigen Weg bilden die beteiligten Proteine hochmolekulare Cluster. Zunächst wurde die Rolle der Alphakinase ALPK1 im Transport apikaler Proteine im Mäusedarm untersucht und eine Verwicklung in den Transport der Lipid-Raft-Proteine SI und DPP IV festgestellt. Im Hauptteil dieser Dissertation ging es um die Erweiterung des Verständnisses des Lipid-Raft-unabhängigen Proteinsortierweges. Insbesondere wurde festgestellt, dass für das vesikuläre post-TGN-Trafficking im Galectin-3-Sorting vermutlich keine Mantelproteine nötig sind, wohl aber ein Dynamin-ähnliches Protein involviert ist. Dabei handelt es sich um die große GTPase Mx1. Der knock-down dieses Proteins führte zu einer leicht reduzierten Transporteffizienz des von Galectin-3 sortierten Glykoproteins P75-GFP zur apikalen Zytoplasmamembran. Des Weiteren konnte durch Mx1 eine Verbindung zur unkonventionellen Sekretion von Galectin-3 gefunden werden. Durch siRNA-Experimente gegen Mx1 wurde festgestellt, dass dadurch die Sekretion von Galectin-3 abnahm. Interessanterweise scheint sekretiertes Galectin-3 für seine Wiederaufnahme in die Zelle eine Präferenz für Lipid-Rafts zu entwickeln, da gezeigt werden konnte, dass die Galectin-Endozytose in DRMs abläuft und durch einen Inhibitor der Lipid-Raft-abhängigen Endozytose gehemmt werden kann. Unter Zuhilfenahme der TIRF-Mikroskopie konnte die Oberfläche von MDCK-Zellen in bisher nicht gekannter Detailtreue abgebildet werden. Dabei konnten sowohl Mikrovilli, als auch dicht unter der apikalen Oberfläche befindliche Recycling-Endosomen detektiert werden, die möglicherweise als Sortierstation von Galectin-3 und P75-GFP dienen. Neben den Aufgaben von Galectin-3 bei der Epithelzellpolarisierung scheint dieses Lektin außerdem auch bei der Ausbildung von klarzelligen Nierenzellkarzinomen eine Rolle zu spielen. In einem Teilprojekt konnte gezeigt werden, dass Galectin-3 dort ein erhöhtes Expressionslevel aufweist und verstärkt mit β-Catenin interagiert. Zusammengefasst legen die in dieser Dissertation vorgelegten Studien nahe, dass das vielseitige und in der Entwicklung klarzelliger Nierenzellkarzinome beteiligte Protein Galectin-3 während seines Lebenszyklus, zu dem die Sortierung apikaler nicht mit Lipid-Rafts assoziierter Glykoproteine gehört, eine alternierende Präferenz für diese Detergens-resistenten Membranen aufzeigt und seine unkonventionelle Sekretion offensichtlich mit der Dynamin-ähnlichen GTPase Mx1 in Verbindung steht.

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