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Molekularbiologie Und Pharmakologie Neuer G-Protein-Gekoppelter Purin-Rezeptoren

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Molekularbiologie Und Pharmakologie Neuer G-Protein-Gekoppelter Purin-Rezeptoren Molekularbiologie und Pharmakologie neuer G-Protein-gekoppelter Purin-Rezeptoren Dissertation zur Erlangung des Doktorgrades (Dr. rer. nat.) der Mathematisch-Naturwissenschaftlichen Fakultät der Rheinischen Friedrich-Wilhelms-Universität Bonn vorgelegt von Melanie Knospe (geb. Hulbert) aus Bonn Bonn 2012 Angefertigt mit Genehmigung der Mathematisch-Naturwissenschaftlichen Fakultät der Rheinischen Friedrich-Wilhelms-Universität Bonn. 1. Gutachter: Prof. Dr. Christa E. Müller 2. Gutachter: Prof. Dr. Ivar von Kügelgen Tag der Promotion: 28.03.2012 Erscheinungsjahr: 2012 Diese Dissertation ist auf dem Hochschulserver der ULB Bonn (http://hss.ulb. uni-bonn.de/diss_online) elektronisch publiziert. Die vorliegende Arbeit wurde in der Zeit von Juni 2008 bis Dezember 2011 am Pharmazeutischen Institut der Rheinischen Friedrich-Wilhelms-Universität Bonn unter der Leitung von Frau Prof. Dr. Christa E. Müller durchgeführt. Mein besonderer Dank gebührt Frau Prof. Dr. Christa E. Müller für die Über- lassung des interessanten Themas, die fachliche Unterstützung, für die vielen wertvollen Anregungen und Diskussionen sowie die konstruktive Kritik beim Erstellen dieser Arbeit. Herrn Prof. Dr. Ivar von Kügelgen danke ich für die freundliche Übernahme des Koreferats. Für die Mitwirkung in meiner Prüfungskommission bedanke ich mich bei Herrn Prof. Dr. med. Klaus Mohr und Herrn Prof. Dr. Günther Mayer. Ich danke der NRW International Graduate Research School LIMES Chemical Biology für die finanzielle Unterstützung in Form eines Doktorandenstipendiums sowie die Kostenübernahme bei Kongressreisen. meinem Mann Michael und meiner Familie "Wichtig ist, dass man nicht aufhört, zu fragen." Albert Einstein, 1955 Inhaltsverzeichnis 1 Einleitung .................................................................................. 1 1.1 G-Protein-gekoppelte Rezeptoren ........................................................ 1 1.1.1 Struktur .............................................................................................. 1 1.1.2 Klassifizierung der G-Protein-gekoppelten Rezeptoren................... 11 1.1.3 Signaltransduktion ........................................................................... 12 1.1.4 Purinerge Rezeptoren ..................................................................... 16 1.2 Adenin-Rezeptoren .............................................................................. 18 1.2.1 Physiologische Funktionen von Adenin-Rezeptoren ....................... 23 1.2.2 Biosynthese und Metabolisierung von Adenin ................................. 24 2 Ziele der Arbeit ....................................................................... 29 3 Ergebnisse und Diskussion ................................................... 31 3.1 Charakterisierung der Adenin-Ligand-Bindungsstelle des Ratten-Adenin-Rezeptors ............................................................................ 31 3.1.1 Klonierung der Ratten-Adenin-Rezeptor-cDNA ............................... 31 3.1.2 Expressionssystem ......................................................................... 33 3.1.2.1 BaculogoldTM Baculovirus-Expressionssystem ....................... 34 3.1.2.2 Bac-to-Bac-Expressionssystem .............................................. 35 3.1.3 Ko-Expression mit G-Proteinen ....................................................... 38 3.1.4 Radioligand-Bindungsstudien .......................................................... 39 3.1.4.1 Sättigungsexperimente ........................................................... 40 3.1.4.2 Kompetitionsexperimente ....................................................... 41 3.1.5 Entwicklung eines spezifischen gegen den Ratten-Adenin-Rezeptor gerichteten Antikörpers ................................................................... 46 3.1.5.1 Antigen-Design ....................................................................... 47 3.1.5.2 Peptid-Antigensynthese .......................................................... 50 3.1.5.3 Gewinnung des polyklonalen Antikörpers ............................... 50 3.1.6 Western Blotting .............................................................................. 51 II Inhaltsverzeichnis 3.1.6.1 Expressionsuntersuchung mit den Serumproben .................... 51 3.1.6.2 Ko-Expression mit G-Proteinen ............................................... 59 3.1.7 Zusammenfassung und Ausblick ..................................................... 60 3.2 Mutagenese des Ratten-Adenin-Rezeptors ....................................... 61 3.2.1 Klonierung ....................................................................................... 63 3.2.1.1 Klonierung von pUC-myc-rAde-Mutanten ................................ 64 3.2.1.2 Klonierung pFastBac-rAde-Mutanten ...................................... 65 3.2.2 Expressionssystem .......................................................................... 68 3.2.3 Untersuchung des verkürzten N-Terminus des rAdeR .................... 69 3.2.4 Extrazelluläre Disulfidbrücken ......................................................... 75 3.2.5 Radioligand-Bindungsstudien .......................................................... 77 3.2.5.1 Kompetitionsexperimente ........................................................ 78 3.2.5.2 [35S]GTPγS-Bindungsstudien .................................................. 82 3.2.6 Western Blotting .............................................................................. 89 3.2.6.1 Expressionsuntersuchung ....................................................... 89 3.2.7 Zusammenfassung und Ausblick ..................................................... 91 3.3 Charakterisierung des Maus-Adenin-Rezeptors Subtyp 1 ............... 93 3.3.1 Klonierung der Maus-Adenin-Rezeptor Subtyp 1-cDNA .................. 93 3.3.1.1 Klonierung der Gensequenz des Maus-Adenin-Rezeptors Subtyp 1 in die Baculovirus-Transfervektoren pVL1393 und pFastBacTM1 ..................................................................... 94 3.3.1.2 Klonierung in die retroviralen Vektoren pQXCIN und pLXSN ..................................................................................... 96 3.3.2 Expressionssystem .......................................................................... 97 3.3.3 Radioligand-Bindungsstudien .......................................................... 98 3.3.3.1 Sättigungsexperimente ............................................................ 99 3.3.3.2 Kompetitionsexperimente ........................................................ 99 3.3.4 Retrovirale Transfektion ................................................................. 105 3.3.4.1 Transfektion der Verpackungsszellen und Infektion der Zielzelle ................................................................................. 105 3.3.4.2 Selektion einer stabil transfizierten Zelllinie ........................... 107 3.3.4.3 RT-PCR ................................................................................. 107 Inhaltsverzeichnis III 3.3.5 Funktionelle Untersuchungen ........................................................ 108 3.3.5.1 Bestimmung von cAMP......................................................... 108 3.3.5.2 Messung der intrazellulären Calcium-Freisetzung ................ 109 3.3.6 Zusammenfassung und Ausblick .................................................. 110 3.4 Exkurs: Adenin-Transporter ............................................................. 111 3.4.1 Messung der Aufnahme des Radioliganden in die Zelle ............... 112 3.4.2 Zusammenfassung ........................................................................ 118 4 Zusammenfassung ............................................................... 121 5 Experimenteller Teil ............................................................. 125 5.1 Allgemeine Angaben ......................................................................... 125 5.1.1 Geräte und Materialien .................................................................. 125 5.1.2 Chemikalien .................................................................................. 126 5.1.2.1 Kommerziell bezogene Chemikalien ..................................... 126 5.1.2.2 Nicht kommerziell bezogene Chemikalien und Zellkulturbedarf ..................................................................... 128 5.1.2.3 Zellkulturbedarf und Nährmedien .......................................... 128 5.1.3 Radioliganden ............................................................................... 129 5.1.4 Kultivierte Zelllinien ....................................................................... 129 5.1.5 Puffer und Lösungen ..................................................................... 130 5.1.5.1 Lösungen für die Zellkultur .................................................... 130 5.1.5.2 Lösungen für die Molekularbiologie ...................................... 130 5.1.5.3 Lösungen für das Bac-to-Bac-Expressionssystem ............... 131 5.1.5.4 Lösungen für die Proteinbestimmung nach Lowry ................ 131 5.1.5.5 Puffer für Radioligand-Bindungsstudien ............................... 131 5.1.5.6 Lösungen für SDS-PAGE ..................................................... 132 5.1.5.7 Lösungen für Western Blotting .............................................. 132 5.1.5.8 Lösungen für die intrazelluläre Calciummessung ................. 133 5.1.5.9 Lösungen für die „uptake“-Experimente ................................ 133 5.2 Zellkultur ...........................................................................................
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