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dc.contributor.advisorMcDonald, Kerry S.eng
dc.contributor.authorKorte, F. Steven, 1975-eng
dc.date.issued2006eng
dc.date.submitted2006 Summereng
dc.descriptionThe entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file.eng
dc.descriptionVita.eng
dc.description"August 2006"eng
dc.descriptionIncludes bibliographical references.eng
dc.descriptionThesis (Ph. D.) University of Missouri-Columbia 2006.eng
dc.descriptionDissertations, Academic -- University of Missouri--Columbia -- Physiology (Medicine).eng
dc.description.abstractThe ability of the heart to function as a pump is governed by mechanisms intrinsic to individual cardiac myocytes. The experiments in this dissertation were designed to examine the effects of sarcomere length and thick filament protein isoform expression on the contractile properties of single skinned cardiac myocytes. Myosin binding protein-C ablation (MyBP-C-\-) increases the rate of force development, loaded shortening velocity, and power output in mouse skinned cardiac myocytes, implying that MyBP-C regulates myocardial contractility by limiting crossbridge cycling. We also examined the effects of SL on mechanical properties in rat skinned cardiac myocytes containing either [alpha]-MyHC or [beta]-MyHC. Peak absolute and normalized loaded shortening velocity and power output was decreased at short SL in both [alpha]-MyHC and [beta]-MyHC myocytes. Matching myocyte force between long and short SL, however, sped loaded shortening velocity and increased power output in [alpha]-MyHC myocytes to values greater than at long SL, but this did not occur in [beta]-MyHC. Matching myocyte width between long and short SL sped loaded shortening velocity and increased power output to values greater than at long SL in both [alpha]-MyHC and [beta]-MyHC myocytes. It is concluded that there is an increase in crossbridge cycling at short SL as compared to long SL, but increased lattice spacing at short SL decreases actomyosin interactions. The data are presented in terms of a model whereby shortening SL induces a conformational change in MyBP-C that removes its constraint on the myosin heads, allowing them to cycle faster.eng
dc.identifier.merlinb58495721eng
dc.identifier.oclc124040717eng
dc.identifier.urihttps://hdl.handle.net/10355/4383
dc.identifier.urihttps://doi.org/10.32469/10355/4383eng
dc.languageEnglisheng
dc.publisherUniversity of Missouri--Columbiaeng
dc.relation.ispartofcollectionUniversity of Missouri--Columbia. Graduate School. Theses and Dissertationseng
dc.subject.meshHeart -- physiologyeng
dc.subject.meshMyocytes, Cardiac -- physiologyeng
dc.subject.meshMuscle Contraction -- physiologyeng
dc.subject.meshMyosins -- physiologyeng
dc.subject.meshSarcoma -- physiologyeng
dc.titleThick filament regulation of myocardial contractioneng
dc.typeThesiseng
thesis.degree.disciplinePhysiology (Medicine) (MU)eng
thesis.degree.grantorUniversity of Missouri--Columbiaeng
thesis.degree.levelDoctoraleng
thesis.degree.namePh. D.eng


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