The large-conductance Ca2+-activated K+ channel interacts with the apolipoprotein ApoA1
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چکیده
منابع مشابه
Overactive bladder and incontinence in the absence of the BK large conductance Ca2+-activated K+ channel.
BK large conductance voltage- and calcium-activated potassium channels respond to elevations in intracellular calcium and membrane potential depolarization, braking excitability of smooth muscle. BK channels are thought to have a particularly prominent role in urinary bladder smooth muscle function and therefore are candidate targets for overactive bladder therapy. To address the role of the BK...
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Large conductance Ca2+-activated K+ (BK) channels belong to the S4 superfamily of K+ channels that include voltage-dependent K+ (Kv) channels characterized by having six (S1-S6) transmembrane domains and a positively charged S4 domain. As Kv channels, BK channels contain a S4 domain, but they have an extra (S0) transmembrane domain that leads to an external NH2-terminus. The BK channel is activ...
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Over the past few years, it has become clear that an important mechanism by which large-conductance Ca(2+)-activated K(+) channel (BK(Ca)) activity is regulated is the tissue-specific expression of auxiliary beta subunits. The first of these to be identified, beta1, is expressed predominately in smooth muscle and causes dramatic effects, increasing the apparent affinity of the channel for Ca(2+...
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The complexity of mammalian physiology requires a diverse array of ion channel proteins. This diversity extends even to a single family of channels. For example, the family of Ca2+-activated K channels contains three structural subfamilies characterized by small, intermediate, and large single channel conductances. Many cells and tissues, including neurons, vascular smooth muscle, endothelial c...
متن کاملFunctional Coupling of the β1 Subunit to the Large Conductance Ca2+-Activated K+ Channel in the Absence of Ca2+
Coexpression of the beta(1) subunit with the alpha subunit (mSlo) of BK channels increases the apparent Ca(2+) sensitivity of the channel. This study investigates whether the mechanism underlying the increased Ca(2+) sensitivity requires Ca(2+), by comparing the gating in 0 Ca(2+)(i) of BK channels composed of alpha subunits to those composed of alpha+beta(1) subunits. The beta(1) subunit incre...
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ژورنال
عنوان ژورنال: Biochemical and Biophysical Research Communications
سال: 2009
ISSN: 0006-291X
DOI: 10.1016/j.bbrc.2009.07.074