Abstract

Neurotransmission is central to neuronal communication, through which information is processed, stored, and retrieved. The vesicular ATPase (V-ATPase) protein is a proton pump that is implicated in neurotransmission. It acidifies synaptic vesicles to be consequently loaded with neurotransmitters prior to release through exocytosis. V100 is a neuron-specific vesicular ATPase subunit a1, and it is a major subunit that determines where the vesicular ATPase functions intracellularly. Previous studies characterized two putative functions for the V100 in neuronal cell biology; intracellular vesicle acidification, and membrane fusion. In this project, we set out to dissect the function of V100 genetically - using immunolabeling and electrophysiology- to understand acidification-dependent and -independent functions. The results cast some light on a potential regulation of the V100 by Ca2+/Calmodulin. This regulatory mechanism may be specifically required for spontaneous vesicle release independent of the proton pump function of the V-ATPase.

Department

Biotechnology Program

Degree Name

MS in Biotechnology

Graduation Date

Fall 11-11-2012

Submission Date

11-11-2012

First Advisor

Hiesinger, Peter Robin

Committee Member 1

Siam, Rania

Committee Member 2

Amleh, Asma

Extent

49 p.

Document Type

Master's Thesis

Library of Congress Subject Heading 1

Neurochemistry.

Rights

The author retains all rights with regard to copyright. The author certifies that written permission from the owner(s) of third-party copyrighted matter included in the thesis, dissertation, paper, or record of study has been obtained. The author further certifies that IRB approval has been obtained for this thesis, or that IRB approval is not necessary for this thesis. Insofar as this thesis, dissertation, paper, or record of study is an educational record as defined in the Family Educational Rights and Privacy Act (FERPA) (20 USC 1232g), the author has granted consent to disclosure of it to anyone who requests a copy. The author has granted the American University in Cairo or its agents a non-exclusive license to archive this thesis, dissertation, paper, or record of study, and to make it accessible, in whole or in part, in all forms of media, now or hereafter known.

Institutional Review Board (IRB) Approval

Not necessary for this item

Comments

I would extend my deepest gratitude to my parents for their consistent and dependable support. I really appreciate their persistent encouragement, love, and patience. They alone have made this effort worth the while. I especially thank my mentor, Robin Hiesinger, first for providing me with the opportunity to conduct the practical work of my thesis in his lab, and second for the quality of guidance and advice he used to share with me. I would also like to thank my lab mates; Daniel Epstein, Dong Wang, Ryan Williamson, Chih-Chiang Chan, Smita Cherry, Jennifer Jen, Egemen Agi, Mehmet Neset, and Leah Taylor. I am also grateful for my colleagues in Hilgemann's and Thomas's labs, especially Mike Fine, Suzan, and Andre Schmidt. I also would like to thank the physiology department administrators, especially Sara Dries, and Patricia Tucker for their genuine concern for my success. I would like to acknowledge the funding source that supported me during my stay in Robin's lab: the Welch Foundation (I-1657). I would also like to thank Dr. Rania Siam for the years I spent under her tutelage. These years have impacted my graduate experience most directly, and I am sure it will help me in my future career. Also I would greatly thank Drs. Amr Shaarawi, Ali Hadi, and Hassan Azzazy for their endless support and help during and even before my travel. Also I thank both; Ms. Samah Abdel Geleel, and Manar Zaki for their continuous help and concern. Finally, I extend my highest regards and sincere thanks to my colleagues in the industrial pharmacy lab at the National research center, and my colleagues in the Biotechnology program, and to all the people who have helped or assisted me to reach my goals.

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