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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 pri...
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2012
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| _version_ | 1867613419135303680 |
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| access_status_str | Open Access |
| author | Khalaf, Ossama Mohamed Salah El-Dien El-Sayed Ibrahim |
| author_browse | Khalaf, Ossama Mohamed Salah El-Dien El-Sayed Ibrahim |
| author_facet | Khalaf, Ossama Mohamed Salah El-Dien El-Sayed Ibrahim |
| author_sort | Khalaf, Ossama Mohamed Salah El-Dien El-Sayed Ibrahim |
| collection | Thesis |
| dc_rights_str_mv | 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. |
| description | 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. |
| format | Thesis |
| id | oai:fount.aucegypt.edu:etds-2583 |
| institution | American University in Cairo (Egypt) |
| last_indexed | 2026-06-10T12:35:50.652Z |
| license_str | Other — see source repository |
| provenance_str_mv | Harvested via OAI-PMH from AUC Knowledge Fountain — bepress |
| publishDate | 2012 |
| publishDateRange | 2012 |
| publishDateSort | 2012 |
| publisher | AUC Knowledge Fountain |
| publisherStr | AUC Knowledge Fountain |
| record_format | dspace |
| source_str | AUC Knowledge Fountain — bepress |
| spelling | oai:fount.aucegypt.edu:etds-2583 Structure-Function Analysis of a Neuron-Specific Vesicular ATPase in Neurotransmission Khalaf, Ossama Mohamed Salah El-Dien El-Sayed Ibrahim 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. 2012-11-11T08:00:00Z thesis application/pdf https://fount.aucegypt.edu/etds/1547 https://fount.aucegypt.edu/context/etds/article/2583/viewcontent/auto_convert.pdf 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. Theses and Dissertations AUC Knowledge Fountain Neurogenetics Neural transmission |
| spellingShingle | Neurogenetics Neural transmission Khalaf, Ossama Mohamed Salah El-Dien El-Sayed Ibrahim Structure-Function Analysis of a Neuron-Specific Vesicular ATPase in Neurotransmission |
| title | Structure-Function Analysis of a Neuron-Specific Vesicular ATPase in Neurotransmission |
| title_full | Structure-Function Analysis of a Neuron-Specific Vesicular ATPase in Neurotransmission |
| title_fullStr | Structure-Function Analysis of a Neuron-Specific Vesicular ATPase in Neurotransmission |
| title_full_unstemmed | Structure-Function Analysis of a Neuron-Specific Vesicular ATPase in Neurotransmission |
| title_short | Structure-Function Analysis of a Neuron-Specific Vesicular ATPase in Neurotransmission |
| title_sort | structure function analysis of a neuron specific vesicular atpase in neurotransmission |
| topic | Neurogenetics Neural transmission |
| url | https://fount.aucegypt.edu/etds/1547 https://fount.aucegypt.edu/context/etds/article/2583/viewcontent/auto_convert.pdf |
| work_keys_str_mv | AT khalafossamamohamedsalaheldienelsayedibrahim structurefunctionanalysisofaneuronspecificvesicularatpaseinneurotransmission |