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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Gabrielaitis, Mantas Pangrsic, Tina Wolf, Fred Strenzke, Nicola Schwaller, Beat Michanski, Susann Moser, Tobias |
| Description | Author Affiliation: Pangrsic T ( Institute for Auditory Neuroscience and InnerEarLab, University Medical Center Göttingen, 37099 Göttingen, Germany); Gabrielaitis M ( Institute for Auditory Neuroscience and InnerEarLab, University Medical Center Göttingen, 37099 Göttingen, Germany); Michanski S ( Institute for Auditory Neuroscience and InnerEarLab, University Medical Center Göttingen, 37099 Göttingen, Germany); Schwaller B ( Unit of Anatomy, Department of Medicine, University of Fribourg, 1700 Fribourg, Switzerland); Wolf F ( Collaborative Research Center 889, University of Göttingen, 37099 Göttingen, Germany); Strenzke N ( Collaborative Research Center 889, University of Göttingen, 37099 Göttingen, Germany); Moser T ( Institute for Auditory Neuroscience and InnerEarLab, University Medical Center Göttingen, 37099 Göttingen, Germany); |
| Abstract | EF-hand $Ca^{2+}-binding$ proteins are thought to shape the spatiotemporal properties of cellular $Ca^{2+}$ signaling and are prominently expressed in sensory hair cells in the ear. Here, we combined genetic disruption of parvalbumin-α, calbindin-D28k, and calretinin in mice with patch-clamp recording, in vivo physiology, and mathematical modeling to study their role in $Ca^{2+}$ signaling, exocytosis, and sound encoding at the synapses of inner hair cells (IHCs). IHCs lacking all three proteins showed excessive exocytosis during prolonged depolarizations, despite enhanced $Ca^{2+}-dependent$ inactivation of their $Ca^{2+}$ current. Exocytosis of readily releasable vesicles remained unchanged, in accordance with the estimated tight spatial coupling of $Ca^{2+}$ channels and release sites (effective “coupling distance” of 17 nm). Substitution experiments with synthetic $Ca^{2+}$ chelators indicated the presence of endogenous $Ca^{2+}$ buffers equivalent to 1 mM synthetic $Ca^{2+}-binding$ sites, approximately half of them with kinetics as fast as 1,2-Bis(2-aminophenoxy)ethane-N,N,N′,N′-tetraacetic acid (BAPTA). Synaptic sound encoding was largely unaltered, suggesting that excess exocytosis occurs extrasynaptically. We conclude that EF-hand $Ca^{2+}$ buffers regulate presynaptic IHC function for metabolically efficient sound coding. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 9 |
| Volume Number | 112 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2015-03-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Calbindin 1 Metabolism Calbindin 2 Calcium Signaling Physiology Exocytosis Hair Cells, Auditory, Inner Parvalbumins Animals Genetics Drug Effects Chelating Agents Pharmacology Egtazic Acid Analogs & Derivatives Cytology Mice Mice, Knockout Synapses Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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