ABSTRACT
FDG PET/CT has become a valuable tool in the diagnosis of the activity of chronic osteomyelitis. The surgical strategy in the treatment of chronic osteomyelitis is the identification of the bone focus and radical debridement of sequesters. The aim of the current study was the registration and use of the FDG PET/CT imaging datasets on a navigation system to provide diagnostic imaging based feedback during surgical procedures. For the present study, FDG PET/CT scans were acquired from artificial bones and cadaver bones with a local focus of activity. The DICOM data sets were merged using a navigation system. The referenced regions of interest were matched with fluoroscopic pictures to register the PET/CT DICOM datasets to the bone and direct visual control. Navigated targeting led to accurate results when verified with fluoroscopic images by targeting previously inserted reference points in artificial and cadaver bone. FDG PET/CT datasets are suitable for navigation and compatible with conventional planning and navigation software. The combination of diagnostic FDG PET/CT imaging with surgical navigation techniques could be a valuable tool for the accurate treatment of chronic osteomyelitis.
Subject(s)
Femur/diagnostic imaging , Femur/surgery , Image Interpretation, Computer-Assisted/methods , Models, Biological , Positron Emission Tomography Computed Tomography/methods , Surgery, Computer-Assisted/methods , Animals , Cadaver , Computer Simulation , Datasets as Topic , Feasibility Studies , Fluorodeoxyglucose F18 , Humans , Radiopharmaceuticals , Reproducibility of Results , Sensitivity and Specificity , SwineABSTRACT
In studying a magnetic bead's creep response to force pulses in an entangled actin network we have found a novel regime where the bead motion obeys a power law x(t) approximately t(1/2) over two decades in time. It is flanked by a short-time regime with x(t) approximately t(3/4) and a viscous with x(t)approximately t. In the intermediate regime the creep compliance depends on the actin concentration c as c(-beta) with beta approximately 1.1 +/- 0.3. We explain this behavior in terms of osmotic restoring force generated by the piling up of filaments in front of the moving bead. A model based on this concept predicts intermediate x(t) approximately t(1/2) and long-time regimes x(t) approximately t in which the compliance varies as c(-4/3), in agreement with experiment.
Subject(s)
Actins/chemistry , Models, Chemical , Biomechanical Phenomena , Elasticity , Magnetics , Osmotic Pressure , Rheology/methods , ViscosityABSTRACT
We studied the viscoelastic response of entangled actin networks using embedded microbeads driven by force pulses with amplitudes in the range from 3 to 120 pN and durations up to 60 s. We distinguished three regimes in the time dependence of the compliance J(t) of the network. These were characterized by specific power laws J(t) approximately t(alpha)(i) (i=1, 2, 3). In the short-time regime (i=1), we observed the exponent alpha1 approximately 0.75. In the long-time regime (i=3), we find that alpha3 approximately 1. For the intermediate-time interval (i=2), we observed a novel dynamic regime: for all actin concentrations and all applied forces, it was characterized by the exponent alpha3 approximately 0.5. In both regimes i=2 and i=3, the compliance depended upon the actin concentration c, such as J approximately c(-gamma)(i) with gamma2 approximately 1.1 and gamma 3 approximately 1.4. Using these results, we calculated the shear modulus in the frequency domain and found that the intermediate-time regime in the t domain corresponds to its plateau behavior.
Subject(s)
Actin Cytoskeleton/chemistry , Actins/chemistry , Immunomagnetic Separation/methods , Microfluidics/methods , Micromanipulation/methods , Models, Chemical , Models, Molecular , Actin Cytoskeleton/ultrastructure , Actins/ultrastructure , Computer Simulation , Elasticity , Magnetics , Multiprotein Complexes/chemistry , Multiprotein Complexes/ultrastructure , Stress, Mechanical , ViscosityABSTRACT
We present a study on filamentous actin solutions containing heavy meromyosin subfragments of myosin II motor molecules. We focus on the viscoelastic phase behavior and internal dynamics of such networks during adenosine-triphosphate depletion. By combining microrheology and fluorescence microscopy, we observed a sol-gel transition accompanied by a sudden onset of directed filament motion. We interpret the sol-gel transition in terms of myosin II enzymology, and suggest a "zipping" mechanism to explain the filament motion in the vicinity of the sol-gel transition.
