Key result
Endophilin A2 interacts with ClC-3 via its SH3 domain, promoting ClC-3 trafficking to the cell membrane and increasing volume-regulated chloride current in vascular smooth muscle cells.
Absolute Event Rate: 19.7% vs 8.4%
p-value: p=<0.05
Endophilin A2 regulates ClC-3 channel activity and trafficking in vascular smooth muscle cells, providing a novel mechanistic insight into vascular function.
May inform vascular ion channel research; leaves open human relevance pending further studies.
BACKGROUND: . METHODS AND RESULTS: . In addition, the SH3 domain of endophilin A2 mediated its interaction with ClC-3 and promotes ClC-3 transportation from the cytoplasm to cell membranes. The regulation of ClC-3 channel activity was also verified in basilar arterial smooth muscle cells (BASMCs) isolated from endophilin A2 transgenic mice. Moreover, endophilin A2 increase VSMCs proliferation induced by endothelin-1 or hypo-osmolarity. CONCLUSIONS: in VSMCs. This study provides a new mechanism by which endophilin A2 regulates ClC-3 channel activity, and sheds light on how ClC-3 is transported to cell membranes to play its critical role as a chloride channel in VSMCs function, which may be involved in cardiovascular diseases. (Circ J 2016; 80: 2397-2406).
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Liu et al. (2016) studied Vascular smooth muscle cell function. Endophilin A2 overexpression vs. Wild-type or control was evaluated on Volume-regulated chloride current (ICl.vol) density at +100 mV (p=<0.05). Endophilin A2 interacts with ClC-3 via its SH3 domain, promoting ClC-3 trafficking to the cell membrane and increasing volume-regulated chloride current in vascular smooth muscle cells.
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