Filament Compliance Influences Cooperative Activation of Thin Filaments and the Dynamics of Force Production in Skeletal Muscle 英文参考文献.docVIP

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Filament Compliance Influences Cooperative Activation of Thin Filaments and the Dynamics of Force Production in Skeletal Muscle 英文参考文献.doc

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Filament Compliance Influences Cooperative Activation of Thin Filaments and the Dynamics of Force Production in Skeletal Muscle 英文参考文献

FilamentComplianceInfluencesCooperativeActivation ofThinFilamentsandtheDynamicsofForceProduction inSkeletalMuscle BertrandC.W.Tanner1*,ThomasL.Daniel2,3,MichaelRegnier2 1DepartmentofMolecularPhysiologyandBiophysics,UniversityofVermont,Burlington,Vermont,UnitedStatesofAmerica,2DepartmentofBioengineering,University ofWashington,Seattle,Washington,UnitedStatesofAmerica,3DepartmentofBiology,UniversityofWashington,Seattle,Washington,UnitedStatesofAmerica Abstract StriatedmusclecontractionisahighlycooperativeprocessinitiatedbyCa2+bindingtothetroponincomplex,whichleads totropomyosinmovementandmyosincross-bridge(XB)formationalongthinfilaments.Experimentalandcomputational studiessuggestskeletalmusclefiberactivationisgreatlyaugmentedbycooperativeinteractionsbetweenneighboringthin filamentregulatoryunits(RU-RUcooperativity;1RU=7actinmonomers+1troponincomplex+1tropomyosinmolecule).XB binding can also amplify thin filament activation through interactions with RUs (XB-RU cooperativity). Because these interactions occur with a temporal order, they can be considered kinetic forms of cooperativity. Our previous spatially- explicit models illustrated that mechanical forms of cooperativity also exist, arising from XB-induced XB binding (XB-XB cooperativity).Thesemechanicalandkineticformsofcooperativityarelikelycoordinatedduringmusclecontraction,but the relative contribution from each of these mechanisms is difficult to separate experimentally. To investigate these contributionswebuiltamulti-filamentmodelofthehalfsarcomere,allowingRUactivationkineticstovarywiththestateof neighboringRUsorXBs.SimulationssuggestCa2+bindingtotroponinactivatesathinfilamentdistancespanning9to11 actins and coupled RU-RU interactions dominate the cooperative force response in skeletal muscle, consistent with measurements from rabbit psoas fibers. XB binding was critical for stabilizing thin filament activation, particularly at 2+ submaximalCa levels,eventhoughXB-RUcooperativityamplifiedforcelessthanRU-RUcoo