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Published on: July 5, 2013
Identification of ClC-2-like chloride currents in pig pancreatic acinar cells
1Department of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QJ, UK.
Insights
Researchers identified a hyperpolarization-activated chloride current in pig pancreatic acinar cells. This chloride channel, similar to ClC-2, may facilitate chloride efflux in these cells.
Area of Science:
- Physiology
- Molecular Biology
- Cell Biology
Background:
- Pancreatic acinar cells secrete digestive enzymes.
- Chloride (Cl-) transport is crucial for pancreatic fluid secretion.
- The specific channels mediating Cl- efflux in these cells are not fully understood.
Purpose of the Study:
- To identify and characterize a hyperpolarization-activated chloride current in pig pancreatic acinar cells.
- To determine the properties and localization of the underlying chloride channel.
- To investigate the potential role of this channel in pancreatic acinar cell function.
Main Methods:
- Whole-cell patch-clamp electrophysiology to record ionic currents.
- Pharmacological and ionic manipulations to characterize current properties.
- Immunohistochemistry using an antiserum against ClC-2 to localize the channel protein.
Main Results:
- A hyperpolarization-activated Cl- current (approx. 50 pA/pF at -60 mV) was identified.
- The current exhibited inward rectification, a Cl- = Br->I- selectivity, and activation by hypotonicity.
- Immunolocalization revealed the ClC-2-like channel in apical secretory granules, not the basolateral membrane.
Conclusions:
- Pig pancreatic acinar cells possess a ClC-2-like chloride channel.
- This channel is localized to secretory granules at the apical pole.
- The ClC-2-like channel likely functions as a chloride efflux pathway in pancreatic acinar cells.
Abstract:
We used the whole-cell patch-clamp technique to identify a hyperpolarization-activated Cl- current (approximately 50 pA/pF at -60 mV) in acutely isolated, voltage-clamped, single, pig pancreatic acinar cells. This current had characteristic properties of inward rectification, a Cl- = Br->I- selectivity sequence and activation by extracellular hypotonicity. These properties are similar to those reported for the ClC-2 Cl- channel recently cloned from rat and expressed in oocytes. An antiserum raised against the C-terminus of ClC-2 localized the channel to secretory granules containing amylase that were situated exclusively at the apical pole of the pig pancreatic acinar cells, but the channel was not localized in the basolateral membrane. Our study combines a functional assessment and immunohistochemical localization of ClC-2-like channels in a native mammalian cell. The data suggest that the ClC-2-like Cl- channel may function as a Cl- efflux pathway in pancreatic acinar cells.
