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Resources » Paper

J Sulcove et al. (1999) International C. elegans Meeting "Development of an Open-ended Muscle Physiology Experiment with C. elegans"

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    Publication type:
    Meeting_abstract
    WormBase ID:
    WBPaper00022936

    J Sulcove, & T Allen (1999). Development of an Open-ended Muscle Physiology Experiment with C. elegans presented in International C. elegans Meeting. Unpublished information; cite only with author permission.

    Given the broad range of mutant strains that have deficits in behaviors relevant to an undergraduate course in physiology, we sought to develop a discovery-based experiment with C. elegans that would both amplify concepts being learned in class and permit students to participate in the experimental design. The created experiment spans two to three laboratory sessions and requires a minimal amount of equipment. The cyclic interaction of myosin with actin is the basis of tension development in muscle cells, as well as eukaryotic cells generally, and the mechanical events are coupled to the hydrolysis of MgATP by myosin. The experiment challenges students to characterize quantitatively the deficits in muscular function arising from selected missense mutations in unc-54 (myosin heavy chain B). The experiment exploits the availability of unc-54 mutations ( e.g. , s74 and s95 alleles) that have salient functional deficits without disruption of muscle structure. Following discussion of Reynold's numbers, students generally develop swimming assays in which tail-beats per minute are examined as a function of bulk solution viscosity. The concepts that the students consider when designing their experiments include the following: osmolarity and its measurement; bulk solution viscosity and its measurement; muscular fatigue and endurance; and force-velocity relations and their interpretation in the context of muscular efficiency. Students have found the experiment engaging, because of the linkage between mutations in human cardiac myosin and familial hypertrophic cardiomyopathy, a lethal heart disease. Moreover, the accessibility of the crystalline structure of the myosin head (containing the catalytic domain and the actin-binding regions) permits students to correlate their results with the emerging structure-function relationship of myosin. The experiment can also be extended to the analysis of other mutations affecting muscular function ( e.g. , unc-27 /Troponin I-2; please see abstract presented at this meeting by Burkeen et al. , In Vivo Analysis of Troponin I Domains in Muscle Function).


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