N- and P/Q-type Ca2+ channels in adrenal chromaffin cells.
N- and P/Q-type Ca2+ channels in adrenal chromaffin cells.
复制标题
肾上腺嗜铬细胞中的 N 型和 P/Q 型 Ca2 通道。
DOI：
10.1111/j.1748-1716.2007.01817.x
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发表时间：
2008
期刊：
影响因子：
--
通讯作者：
Xie,Z
中科院分区：
文献类型：
--
作者：
Fox,AP;Cahill,AL;Currie,KPM;Grabner,C;Harkins,AB;Herring,B;Hurley,JH;Xie,Z
Ca2+is the most ubiquitous second messenger found in all cells. Alterations in [Ca2+]icontribute to a wide variety of cellular responses including neurotransmitter release, muscle contraction, synaptogenesis and gene expression. Voltage‐dependent Ca2+channels, found in all excitable cells (Hille 1992), mediate the entry of Ca2+into cells following depolarization. Ca2+channels are composed of a large pore‐forming subunit, called the α1subunit, and several accessory subunits. Ten different α1subunit genes have been identified and classified into three families, Cav1‐3(Dunlapet al.1995, Catterall 2000). Each α1gene produces a unique Ca2+channel. Although chromaffin cells express several different types of Ca2+channels, this review will focus on the Cav2.1and Cav2.2channels, also known as P/Q‐ and N‐type respectively (Nowyckyet al.1985, Llinaset al.1989b, Wheeleret al.1994). These channels exhibit physiological and pharmacological properties similar to their neuronal counterparts. N‐, P/Q and to a lesser extent R‐type Ca2+channels are known to regulate neurotransmitter release (Hirninget al.1988, Horne & Kemp 1991, Uchitelet al.1992, Luebkeet al.1993, Takahashi & Momiyama 1993, Turneret al.1993, Regehr & Mintz 1994, Wheeleret al.1994, Wu & Saggau 1994, Waterman 1996, Wright & Angus 1996, Reidet al.1997). N‐ and P/Q‐type Ca2+channels are abundant in nerve terminals where they colocalize with synaptic vesicles. Similarly, these channels play a role in neurotransmitter release in chromaffin cells (Garciaet al.2006). N‐ and P/Q‐type channels are subject to many forms of regulation (Ikeda & Dunlap 1999). This review pays particular attention to the regulation of N‐ and P/Q‐type channels by heterotrimeric G‐proteins, interaction with SNARE proteins, and channel inactivation in the context of stimulus‐secretion coupling in adrenal chromaffin cells.
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