Relation of Properties of Isolated Myosin to those of Intact Muscles of the Cat and Sloth

Bárány, Michael; Conover, Thomas E.; Schliselfeld, Louis H.; Gaetjens, Eric; Goffart, M

doi:10.1111/j.1432-1033.1967.tb00120.x

Cited by 58 publications

(11 citation statements)

References 27 publications

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“…[19] found a redistribution of cardiac myosin isoforms in a hamster model of cardiomyopathy. These studies using in vitro motility assays demonstrated that the relative levels of α- and β-cardiac myosin isoform expression could directly regulate the contractility of the muscle, as inferred from the studies of Barany et al [20], who showed that hearts with varying amounts of α and β myosin had different contractile velocities.…”

Section: Single Molecule Techniquesmentioning

confidence: 95%

Insights into Human β-Cardiac Myosin Function from Single Molecule and Single Cell Studies

Sivaramakrishnan

Ashley

Leinwand

et al. 2009

J. of Cardiovasc. Trans. Res.

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β-Cardiac myosin is a mechanoenzyme that converts the energy from ATP hydrolysis into a mechanical force that drives contractility in muscle. Thirty percent of the point mutations that result in hypertrophic cardiomyopathy are localized to MYH7, the gene encoding human β-cardiac myosin heavy chain (β-MyHC). Force generation by myosins requires a tight and highly conserved allosteric coupling between its different protein domains. Hence, the effects of single point mutations on the force generation and kinetics of β-cardiac myosin molecules cannot be predicted directly from their location within the protein structure. Great insight would be gained from understanding the link between the functional defect in the myosin protein and the clinical phenotypes of patients expressing them. Over the last decade, several single molecule techniques have been developed to understand in detail the chemomechanical cycle of different myosins. In this review, we highlight the single molecule techniques that can be used to assess the effect of point mutations on β-cardiac myosin function. Recent bioengineering advances have enabled the micromanipulation of single cardiomyocyte cells to characterize their force–length dynamics. Here, we briefly review single cell micromanipulation as an approach to determine the effect of β-MyHC mutations on cardiomyocyte function. Finally, we examine the technical challenges specific to studying β-cardiac myosin function both using single molecule and single cell approaches.

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Section: Single Molecule Techniquesmentioning

confidence: 95%

Insights into Human β-Cardiac Myosin Function from Single Molecule and Single Cell Studies

Sivaramakrishnan

Ashley

Leinwand

et al. 2009

J. of Cardiovasc. Trans. Res.

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“…; Suzuki, ) and the sloth (Barany et al. ) when compared with similar‐sized species that engage in swifter and more powerful movements. However, our results are in contrast to previous findings for the psoas muscle in orangutans (Kimura, ), which reported less than a third slow fibres compared with about the two‐thirds observed in this study.…”

Section: Discussionmentioning

confidence: 99%

Fibre type composition in the lumbar perivertebral muscles of primates: implications for the evolution of orthogrady in hominoids

et al. 2013

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The axial musculoskeletal system is important for the static and dynamic control of the body during both locomotor and non-locomotor behaviour. As a consequence, major evolutionary changes in the positional habits of a species are reflected by morpho-functional adaptations of the axial system. Because of the remarkable phenotypic plasticity of muscle tissue, a close relationship exists between muscle morphology and function. One way to explore major evolutionary transitions in muscle function is therefore by comparative analysis of fibre type composition. In this study, the three-dimensional distribution of slow and fast muscle fibres was analysed in the lumbar perivertebral muscles of two lemuriform (mouse lemur, brown lemur) and four hominoid primate species (white-handed gibbon, orangutan, bonobo, chimpanzee) in order to develop a plausible scenario for the evolution of the contractile properties of the axial muscles in hominoids and to discern possible changes in muscle physiology that were associated with the evolution of orthogrady. Similar to all previously studied quadrupedal mammals, the lemuriform primates in this study exhibited a morpho-functional dichotomy between deep slow contracting local stabilizer muscles and superficial fast contracting global mobilizers and stabilizers and thus retained the fibre distribution pattern typical for quadrupedal non-primates. In contrast, the hominoid primates showed no regionalization of the fibre types, similar to previous observations in Homo. We suggest that this homogeneous fibre composition is associated with the high functional versatility of the axial musculature that was brought about by the evolution of orthograde behaviours and reflects the broad range of mechanical demands acting on the trunk in orthograde hominoids. Because orthogrady is a derived character of euhominoids, the uniform fibre type distribution is hypothesized to coincide with the evolution of orthograde behaviours.

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“…a tightly "coupled" positive correlation is observed when ATPase activity is plotted against maximum muscle shortening velocity (34). Similarly, vertebrate myosin isoforms have a tightly coupled ATPase to actin sliding velocity ratio (1).…”

Section: Discussionmentioning

confidence: 99%

Variable N-terminal Regions of Muscle Myosin Heavy Chain Modulate ATPase Rate and Actin Sliding Velocity

Swank

Knowles

Kronert

et al. 2003

Journal of Biological Chemistry

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We integratively assessed the function of alternative versions of a region near the N terminus of Drosophila muscle myosin heavy chain (encoded by exon 3a or 3b). We exchanged the alternative exon 3 regions between an embryonic isoform and the indirect flight muscle isoform. Each chimeric myosin was expressed in Drosophila indirect flight muscle, in the absence of other myosin isoforms, allowing for purified protein analysis and whole organism locomotory studies. The flight muscle isoform generates higher in vitro actin sliding velocity and solution ATPase rates than the embryonic isoform. Exchanging the embryonic exon 3 region into the flight muscle isoform decreased ATPase rates to embryonic levels but did not affect actin sliding velocity or flight muscle ultrastructure. Interestingly, this swap only slightly impaired flight ability. Exchanging the flight muscle-specific exon 3 region into the embryonic isoform increased actin sliding velocity 3-fold and improved indirect flight muscle ultrastructure integrity but failed to rescue the flightless phenotype of flies expressing embryonic myosin. These results suggest that the two structural versions of the exon 3 domain independently influence the kinetics of at least two steps of the actomyosin cross-bridge cycle.Myosin powers muscle shortening by converting the chemical energy of ATP into actin movement through conformational changes in the myosin head. Developmental stage and musclespecific myosin isoforms have distinct rates of ATP hydrolysis and propel actin at velocities that strongly correlate with muscle contractile properties (1-3). Differences in myosin isoform function have been well characterized in many species (4). However, the mechanism by which variation in specific structural regions of the myosin heavy chain (MHC) 1 contributes to isoform-specific properties is not well understood, especially in striated muscle isoforms (5, 6).Studies aimed at defining structural regions of MHC that are responsible for setting isoform-specific properties have focused on two flexible surface loops that connect the proteolytic domains of the myosin head (25/50-kDa, loop 1; and 50/20-kDa, loop 2) (for review see Murphy and Spudich (6

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Relation of Properties of Isolated Myosin to those of Intact Muscles of the Cat and Sloth

Cited by 58 publications

References 27 publications

Insights into Human β-Cardiac Myosin Function from Single Molecule and Single Cell Studies

Insights into Human β-Cardiac Myosin Function from Single Molecule and Single Cell Studies

Fibre type composition in the lumbar perivertebral muscles of primates: implications for the evolution of orthogrady in hominoids

Variable N-terminal Regions of Muscle Myosin Heavy Chain Modulate ATPase Rate and Actin Sliding Velocity

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