Slc26a11 is prominently expressed in the brain and functions as a chloride channel: expression in Purkinje cells and stimulation of V H+-ATPase
| Autor: | Sharon Barone, Karl Kunzelmann, Jie Xu, Chris I. De Zeeuw, Manoocher Soleimani, Negah Rahmati, Lalida Sirianant |
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| Přispěvatelé: | Neurosciences, Cardiology, Netherlands Institute for Neuroscience (NIN) |
| Rok vydání: | 2013 |
| Předmět: |
medicine.medical_specialty
Cerebellum Physiology Anion Transport Proteins Clinical Biochemistry Central nervous system Cystic Fibrosis Transmembrane Conductance Regulator Biology Hippocampus Mice Purkinje Cells 03 medical and health sciences 0302 clinical medicine Physiology (medical) Internal medicine medicine Animals Humans RNA Messenger Patch clamp 030304 developmental biology Cerebral Cortex 0303 health sciences Cell Membrane Colforsin HEK 293 cells Transfection Olfactory Bulb Olfactory bulb Cell biology Mice Inbred C57BL Protein Transport Proton-Translocating ATPases HEK293 Cells medicine.anatomical_structure Endocrinology Organ Specificity Sulfate Transporters Cerebral cortex Chloride channel Calcium 030217 neurology & neurosurgery |
| Zdroj: | Pflugers Archiv-European Journal of Physiology, 465(11), 1583-1597. Springer-Verlag Pflugers Archiv: European Journal of Physiology, 465, 1583-1597. Springer Verlag GmbH Pflügers Archiv-European Journal of Physiology |
| ISSN: | 0031-6768 |
| Popis: | SLC26A11 (human)/Slc26a11 (mouse), also known as kidney brain anion transporter (KBAT), is a member of the SLC26 anion transporter family and shows abundant mRNA expression in the brain. However, its exact cellular distribution and subcellular localization in the brain and its functional identity and possible physiological roles remain unknown. Expression and immunostaining studies demonstrated that Slc26a11 is abundantly expressed in the cerebellum, with a predominant expression in Purkinje cells. Lower expression levels were detected in hippocampus, olfactory bulb, cerebral cortex, and subcortical structures. Patch clamp studies in HEK293 cells transfected with mouse cDNA demonstrated that Slc26a11 can function as a chloride channel that is active under basal conditions and is not regulated by calcium, forskolin, or co-expression with cystic fibrosis transmembrane regulator. Single and double immunofluorescent labeling studies demonstrated the localization of vacuolar (V) H⁺-ATPase and Slc26a11 (KBAT) in the plasma membrane in Purkinje cells. Functional studies in HEK293 cells indicated that transfection with Slc26a11 stimulated acid transport via endogenous V H⁺-ATPase. We conclude that Slc26a11 (KBAT) is prominently distributed in output neurons of various subcortical and cortical structures in the central nervous system, with specific expression in Purkinje cells and that it may operate as a chloride channel regulating acid translocation by H⁺-ATPase across the plasma membrane and in intracellular compartments. |
| Databáze: | OpenAIRE |
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