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The Journal of Neuroscience, October 15, 2008, 28(42):10587-10598; doi:10.1523/JNEUROSCI.3750-08.2008

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Cellular/Molecular
Role of the Vesicular Chloride Transporter ClC-3 in Neuroendocrine Tissue

Tanja Maritzen,¹ Damien J. Keating,^1,4 Ioana Neagoe,^1,2,3 Anselm A. Zdebik,^1,2,3 and Thomas J. Jentsch^1,2,3

¹Zentrum für Molekulare Neurobiologie (ZMNH), Universität Hamburg, D-20246 Hamburg, Germany, ²Leibniz-Institut für Molekulare Pharmakologie (FMP) and ³Max-Delbrück-Centrum für Molekulare Medizin (MDC), D-13125 Berlin, Germany, and ⁴Department of Human Physiology and Centre for Neuroscience, Flinders University, Adelaide SA 5001, Australia

Correspondence should be addressed to Thomas J. Jentsch, Leibniz-Institut für Molekulare Pharmakologie (FMP) and Max-Delbrück-Centrum für Molekulare Medizin (MDC), Robert-Rössle-Straße 10, D-13125 Berlin, Germany. Email: Jentsch{at}fmp-berlin.de

ClC-3 is an intracellular chloride transport protein known to reside on endosomes and synaptic vesicles. The endogenous protein has been notoriously difficult to detect in immunohistological experiments because of the lack of reliable antibodies. Using newly generated antibodies, we now examine its expression pattern at the cellular and subcellular level. In all tissues examined, immunostaining indicated that ClC-3 is a vesicular protein, with a prominent expression in endocrine cells like adrenal chromaffin cells and pancreatic islet cells. In line with a possible function of ClC-3 in regulating vesicle trafficking or exocytosis in those secretory cells, capacitance measurements and amperometry indicated that exocytosis of large dense-core vesicles (LDCVs) was decreased in chromaffin cells from ClC-3 knock-out mice. However, immunohistochemistry complemented with subcellular fractionation showed that ClC-3 is not detectable on LDCVs of endocrine cells, but localizes to endosomes and synaptic-like microvesicles in both adrenal chromaffin and pancreatic β cells. This observation points to an indirect influence of ClC-3 on LDCV exocytosis in chromaffin cells, possibly by affecting an intracellular trafficking step.

Key words: Clcn3; gene disruption; catecholamine; insulin; channel; exchanger

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Received Aug. 8, 2008; accepted Aug. 28, 2008.

Correspondence should be addressed to Thomas J. Jentsch, Leibniz-Institut für Molekulare Pharmakologie (FMP) and Max-Delbrück-Centrum für Molekulare Medizin (MDC), Robert-Rössle-Straße 10, D-13125 Berlin, Germany. Email: Jentsch{at}fmp-berlin.de

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