<?xml version="1.0"?>
<!-- FILE : mijailovich_model_2000.xml
CREATED : 3rd August 2004
LAST MODIFIED : 3rd August 2004
AUTHOR : Catherine Lloyd
The Bioengineering Institute
The University of Auckland
MODEL STATUS : This model conforms to the CellML 1.0 Specification released on
10th August 2001, and the 16/01/2002 CellML Metadata 1.0 Specification.
DESCRIPTION : This file contains a CellML description of Mijailovich et al.'s 2000 model of calcium, cross-bridge phosphorylation and contraction.
CHANGES:
--><model xmlns="http://www.cellml.org/cellml/1.0#" xmlns:cmeta="http://www.cellml.org/metadata/1.0#" cmeta:id="mijailovich_2001" name="mijailovich_2001">
<documentation xmlns="http://cellml.org/tmp-documentation">
<article>
<articleinfo>
<title>Modelling Actin-Myosin Binding in Airway Smooth Muscle</title>
<author>
<firstname>Catherine</firstname>
<surname>Lloyd</surname>
<affiliation>
<shortaffil>Auckland Bioengineering Institute, The University of Auckland</shortaffil>
</affiliation>
</author>
</articleinfo>
<section id="sec_status">
<title>Model Status</title>
<para>
This CellML model runs in both OpenCell and COR but to replicate the published results (the first part of figure 3b). The units have been checked and they are consistent.
</para>
</section>
<sect1 id="sec_structure">
<title>Model Structure</title>
<para>
ABSTRACT: We carried out a detailed mathematical analysis of the effects of length fluctuations on the dynamically evolving cross-bridge distributions, simulating those that occur in airway smooth muscle during breathing. We used the latch regulation scheme of Hai and Murphy (Am. J. Physiol. Cell Physiol. 255:C86-C94, 1988) integrated with Huxley's sliding filament theory of muscle contraction. This analysis showed that imposed length fluctuations decrease the mean number of attached bridges, depress muscle force and stiffness, and increase force-length hysteresis. At frequencies >0.1 Hz, the bond-length distribution of slowly cycling latch bridges changed little over the stretch cycle and contributed almost elastically to muscle force, but the rapidly cycling cross-bridge distribution changed substantially and dominated the hysteresis. By contrast, at frequencies greater than 0.033 Hz this behavior was reversed: the rapid cycling cross-bridge distribution changed little, effectively functioning as a constant force generator, while the latch bridge bond distribution changed substantially and dominated the stiffness and hysteresis. The analysis showed the dissociation of force/length hysteresis and cross-bridge cycling rates when strain amplitude exceeds 3%; that is, there is only a weak coupling between net external mechanical work and the ATP consumption required for cycling cross-bridges during the oscillatory steady state. Although these results are specific to airway smooth muscle, the approach generalizes to other smooth muscles subjected to cyclic length fluctuations.
</para>
<para>
The original paper reference is cited below:
</para>
<para>
Perturbed Equilibria of Myosin Binding in Airway Smooth Muscle: Bond-Length Distributions, Mechanics, and ATP Metabolism, Srboljub M. Mijailovich, James P. Butler, and Jeffrey J. Fredberg, 2000, <emphasis>Biophysical Journal</emphasis>, 79, 2667-2681. <ulink url="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11053139&dopt=Abstract">PubMed ID: 11053139</ulink>
</para>
<informalfigure float="0" id="fig_reaction_diagram">
<mediaobject>
<imageobject>
<objectinfo>
<title>reaction diagram</title>
</objectinfo>
<imagedata fileref="mijailovich_2000.png"/>
</imageobject>
</mediaobject>
<caption>Hai and Murphy's four-state model: the latch regulatory scheme for Ca<superscript>2+</superscript>-dependent smooth muscle activation and Huxley's slidin filament model. A represents the actin filament, M represents detached myosin, Mp is detached, phosphorylated myosin, AM is the actin-myosin complex, and AMp is the phosphorylated actin-myosin complex.</caption>
</informalfigure>
</sect1>
</article>
</documentation>
<units name="nanometre">
<unit prefix="nano" units="metre"/>
</units>
<units name="first_order_rate_constant">
<unit exponent="-1" units="second"/>
</units>
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<!--<variable units="nanometre" name="x" initial_value="2200.0"/>
<variable units="nanometre" name="h" initial_value="15.6"/> -->
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<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#">
<rdf:Bag rdf:about="rdf:#80d484a2-8449-4fbd-9110-849f57545217">
<rdf:li>myosin</rdf:li>
<rdf:li>calcium</rdf:li>
<rdf:li>myofilament mechanics</rdf:li>
<rdf:li>atp</rdf:li>
<rdf:li>metabolism</rdf:li>
<rdf:li>smooth muscle</rdf:li>
<rdf:li>contraction</rdf:li>
</rdf:Bag>
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<vCard:FN xmlns:vCard="http://www.w3.org/2001/vcard-rdf/3.0#">Catherine Lloyd</vCard:FN>
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<bqs:subject_type xmlns:bqs="http://www.cellml.org/bqs/1.0#">keyword</bqs:subject_type>
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<dcterms:W3CDTF xmlns:dcterms="http://purl.org/dc/terms/">2004-08-03</dcterms:W3CDTF>
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<dcterms:alternative xmlns:dcterms="http://purl.org/dc/terms/">myosin</dcterms:alternative>
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<vCard:Given xmlns:vCard="http://www.w3.org/2001/vcard-rdf/3.0#">Catherine</vCard:Given>
<vCard:Family xmlns:vCard="http://www.w3.org/2001/vcard-rdf/3.0#">Lloyd</vCard:Family>
<vCard:Other xmlns:vCard="http://www.w3.org/2001/vcard-rdf/3.0#">May</vCard:Other>
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<dc:creator xmlns:dc="http://purl.org/dc/elements/1.1/" rdf:resource="rdf:#90dce5a8-3a50-4611-96f9-d5e43f0526dd"/>
<dc:title xmlns:dc="http://purl.org/dc/elements/1.1/">
Perturbed Equilibria of Myosin Binding in Airway Smooth Muscle: Bond-Length Distributions, Mechanics and ATP Metabolism
</dc:title>
<bqs:volume xmlns:bqs="http://www.cellml.org/bqs/1.0#">79</bqs:volume>
<bqs:first_page xmlns:bqs="http://www.cellml.org/bqs/1.0#">2667</bqs:first_page>
<bqs:Journal xmlns:bqs="http://www.cellml.org/bqs/1.0#" rdf:resource="rdf:#cd2da35f-5fbf-451e-b08c-0b871edbfddc"/>
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<bqs:last_page xmlns:bqs="http://www.cellml.org/bqs/1.0#">2681</bqs:last_page>
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<dc:creator xmlns:dc="http://purl.org/dc/elements/1.1/" rdf:resource="rdf:#84f25898-75da-4a36-b31c-8a94093311b8"/>
<rdf:value>
This is a CellML description of Mijailovich et al.'s 2000 model of calcium, cross-bridge phosphorylation and contraction.
</rdf:value>
</rdf:Description>
<rdf:Description rdf:about="#AM">
<dcterms:alternative xmlns:dcterms="http://purl.org/dc/terms/">actin-myosin complex</dcterms:alternative>
<dc:title xmlns:dc="http://purl.org/dc/elements/1.1/">AM</dc:title>
</rdf:Description>
<rdf:Description rdf:about="#Mp">
<dcterms:alternative xmlns:dcterms="http://purl.org/dc/terms/">phosphorylated myosin</dcterms:alternative>
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The University of Auckland, Auckand Bioengineering Institute
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Mijailovich et al.'s 2000 model of calcium, cross-bridge phosphorylation and contraction.
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