Document Detail


The effect of residual Ca2+ on the stochastic gating of Ca2+-regulated Ca2+ channel models.
MedLine Citation:
PMID:  15833318     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Single-channel models of intracellular Ca(2+) channels such as the inositol 1,4,5-trisphosphate receptor and ryanodine receptor often assume that Ca(2+)-dependent transitions are mediated by a constant background [Ca(2+)] as opposed to a dynamic [Ca(2+)] representing the formation and collapse of a localized Ca(2+) domain. This assumption neglects the fact that Ca(2+) released by open intracellular Ca(2+) channels may influence subsequent gating through the processes of Ca(2+)-activation or -inactivation. We study the effect of such "residual Ca(2+)" from previous channel opening on the stochastic gating of minimal and realistic single-channel models coupled to a restricted cytoplasmic compartment. Using Monte Carlo simulation as well as analytical and numerical solution of a system of advection-reaction equations for the probability density of the domain [Ca(2+)] conditioned on the state of the channel, we determine how the steady-state open probability (p(open)) of single-channel models of Ca(2+)-regulated Ca(2+) channels depends on the time constant for Ca(2+) domain formation and collapse. As expected, p(open) for a minimal model including Ca(2+) activation increases as the domain time constant becomes large compared to the open and closed dwell times of the channel, that is, on average the channel is activated by residual Ca(2+) from previous openings. Interestingly, p(open) for a channel model that is inactivated by Ca(2+) also increases as a function of the domain time constant when the maximum domain [Ca(2+)] is fixed, because slow formation of the Ca(2+) domain attenuates Ca(2+)-mediated inactivation. Conversely, when the source amplitude of the channel is fixed, increasing the domain time constant leads to elevated domain [Ca(2+)] and decreased open probability. Consistent with these observations, a realistic De Young-Keizer-like IP(3)R model responds to residual Ca(2+) with a steady-state open probability that is a monotonic function of the domain time constant, though minimal models that include both Ca(2+)-activation and -inactivation show more complex behavior. We show how the probability density approach described here can be generalized for arbitrarily complex channel models and for any value of the domain time constant. In addition, we present a comparatively simple numerical procedure for estimating p(open) for models of Ca(2+)-regulated Ca(2+) channels in the limit of a very fast or very slow Ca(2+) domain. When the ordinary differential equation for the [Ca(2+)] in a restricted cytoplasmic compartment is replaced by a partial differential equation for the buffered diffusion of intracellular Ca(2+) in a homogeneous isotropic cytosol, we find the dependence of p(open) on the buffer time constant is qualitatively similar to the above-mentioned results.
Authors:
Borbala Mazzag; Christopher J Tignanelli; Gregory D Smith
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Journal of theoretical biology     Volume:  235     ISSN:  0022-5193     ISO Abbreviation:  J. Theor. Biol.     Publication Date:  2005 Jul 
Date Detail:
Created Date:  2005-04-18     Completed Date:  2005-07-18     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0376342     Medline TA:  J Theor Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  121-50     Citation Subset:  IM    
Affiliation:
Department of Applied Science, College of William and Mary, Williamsburg, VA 23187, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Calcium / metabolism*
Calcium Channels / physiology*
Calcium Signaling
Cytosol / metabolism*
Ion Channel Gating / physiology*
Models, Biological
Monte Carlo Method
Time Factors
Chemical
Reg. No./Substance:
0/Calcium Channels; 7440-70-2/Calcium

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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