The effect of trauma backboards on computed tomography radiation dose.

AIM: To assess the effect of trauma backboards on the radiation dose at computed tomography (CT) when using automatic tube current modulation (ATCM). MATERIALS AND METHODS: An anthropomorphic phantom was scanned with two commercially available CT systems (GE LightSpeed16 Pro and Siemens Definition AS+) without and with backboards. Tube current-time product (mAs), and CTDIvol (mGy) were recorded for each examination. Thermoluminescent dosimeters were used to measure skin entrance dose in the pelvis and breast. Statistical significance was determined using a two-sample t-test. In addition, an institutional review board-approved retrospective image review was performed to quantify the frequency of backboard use during CT in the emergency department. RESULTS: There was a statistically significant increase in maximum tube current-time product (p<0.05) and CTDIvol (p<0.05) with the presence of a backboard; tube current-time product increased up to 31% and CTDIvol increased up to 27%. There was a significant increase in skin entrance dose in the anterior and posterior pelvis (p<0.05) with the presence of a backboard; skin entrance dose increased up to 25% in the anterior pelvis. Skin entrance dose to the breast increased with a backboard, although this was not statistically significant. The frequency of backboard use during CT markedly decreased (from 77% to 3%) after instituting a multidisciplinary policy to promptly remove patients from backboards upon arrival to the emergency department after a primary clinical survey. CONCLUSIONS: Using backboards during CT with ATCM can significantly increase the radiation dose. Although the decision to maintain patients on backboards is multifactorial, attempts should be made to minimise backboard use during CT when possible.

Role of protein conformation and aggregation in pumping water in and out of a cell.

Dialysis cassettes containing BSA solutions were used to simulate passive in vivo conditions to assess the effect of protein conformation and aggregation on cell water content. The cassettes were suspended in dextran solutions to provide a range of fixed osmotic stress values simulating blood plasma. The system was placed on a shaker for 24 h to attain equilibrium. Four manipulation methods; pH, cosolute salt concentration, e.g. NaCl, temperature annealing and urea concentration denaturant were varied to produce well-known manipulations of BSA conformation. It was observed that the cell water content varied from +14% to about -13% with changes in protein conformation and aggregation. The findings demonstrate that a change in protein conformation and aggregation, pumps water in and out of a cell to maintain equilibrium % water content matching the protein conformational hydration parameter. This concept supplements existing theories on cell volume regulation.

Initial evaluation of a continuous speech recognition program for radiology.

The aims of this work were to measure the accuracy of one continuous speech recognition product and dependence on the speaker's gender and status as a native or nonnative English speaker, and evaluate the product's potential for routine use in transcribing radiology reports. IBM MedSpeak/Radiology software, version 1.1 was evaluated by 6 speakers. Two were nonnative English speakers, and 3 were men. Each speaker dictated a set of 12 reports. The reports included neurologic and body imaging examinations performed with 6 different modalities. The dictated and original report texts were compared, and error rates for overall, significant, and subtle significant errors were computed. Error rate dependence on modality, native English speaker status, and gender were evaluated by performing ttests. The overall error rate was 10.3 +/- 3.3%. No difference in accuracy between men and women was found; however, significant differences were seen for overall and significant errors when comparing native and nonnative English speakers (P = .009 and P = .008, respectively). The speech recognition software is approximately 90% accurate, and while practical implementation issues (rather than accuracy) currently limit routine use of this product throughout a radiology practice, application in niche areas such as the emergency room currently is being pursued. This methodology provides a convenient way to compare the initial accuracy of different speech recognition products, and changes in accuracy over time, in a detailed and sensitive manner.

Experimental determination of section sensitivity profiles and image noise in electron beam computed tomography.

To determine the effect of continuous-volume scanning (CVS) on z-axis resolution, section sensitivity profiles were measured on an electron beam computed tomography (CT) scanner and compared with those obtained using the step-volume scanning (SVS) mode. A steel bead was imaged using different scan parameters, and the mean CT number over the bead was plotted against the z-axis position to determine section sensitivity profiles. From these profiles, full width at half maximum (FWHM), full width at tenth maximum (FWTM), and full width at tenth area (FWTA) were calculated. A uniform water phantom was imaged to measure noise. To determine the visual significance of changes in the section sensitivity profile, a section thickness and contiguity phantom was imaged. All section sensitivity profiles measured had an FWHM value within 0.5 mm of the nominal scan width. The FWTM and FWTA values increased with the CVS mode compared with the SVS mode. This broadening of the section sensitivity profiles was most significant with larger collimator widths. However, use of smaller collimator widths increased image noise. When all other parameters remained constant, increasing the exposure time to reduce image noise did not affect the section sensitivity profile. The CVS mode produced wider section sensitivity profiles than the SVS mode. This effect was minimized when the smallest collimator width was used, but at the expense of increased image noise.

Comparison of four motion correction techniques in SPECT imaging of the heart: a cardiac phantom study.

UNLABELLED: The aim of this study was to evaluate the accuracy of four different motion correction techniques in SPECT imaging of the heart. METHODS: We evaluated three automated techniques: the cross-correlation (CC) method, diverging squares (DS) method and two-dimensional fit method and one manual shift technique (MS) using a cardiac phantom. The phantom was filled with organ concentrations of 99mTc closely matching those seen in patient studies. The phantom was placed on a small sliding platform connected to a computer-controlled stepping motor. Linear, random, sinusoidal and bounce motions of magnitude up to 2 cm in the axial direction were simulated. Both single- and dual-detector 90 degrees acquisitions were acquired using a dual 90 degrees detector system. Data were acquired over 180 degrees with 30 or 15 frames/detector (single-/dual-head) at 30 sec/frame in a 64x64 matrix. RESULTS: The simulated single-detector system, CC method, failed to accurately correct for any of the simulated motions. The DS technique overestimated the magnitude of phantom motion, particularly for images acquired between 45 degrees left anterior oblique and 45 degrees left posterior oblique. The two-dimensional and MS techniques accurately corrected for motion. The simulated dual 90 degrees detector system, CC method, only partially tracked random or bounce cardiac motion and failed to detect sinusoidal motion. The DS technique overestimated motion in the latter half of the study. Both the two-dimensional and MS techniques provided superior tracking, although no technique was able to accurately track the rapid changes in cardiac location simulated in the random motion study. Average absolute differences between true and calculated position of the heart on single- and dual 90 degrees -detectors were 1.7 mm and 1.5 mm for the two-dimensional and MS techniques, respectively. The corresponding values for the DS and CC techniques were 5.7 and 8.9 mm, respectively. CONCLUSION: Of the four techniques evaluated, manual correction by an experienced technologist proved to be the most accurate, although results were not significantly different from those observed with the two-dimensional method. Both techniques accurately determined cardiac location and permitted artifact-free reconstruction of the simulated cardiac studies.

Comparison of selected ultrasound performance tests with varying overall receiver gain and dynamic range, using conventional and magnified field of view.

Most ultrasound (US) scanner vendors currently offer a feature that allows a region of the ultrasound image to be magnified or zoomed. Although the methods of magnification vary among vendors, the ability to "zoom in" on a selected portion of the image has gained clinical acceptance. However, using this feature introduces additional steps in the quality assurance (QA) measurement procedures. No studies exist that demonstrate the advantage of a magnified field of view (FOV) over the conventional FOV for QA purposes. The purpose of this study was to investigate the influence of a magnified versus nonmagnified FOV on various common QA performance tests as a function of the overall receiver gain and dynamic range. Additionally, since the performance tests are subject to variations caused by scanner settings, sets of QC tests were recorded using several different scanner settings to investigate any change in the sensitivity of the QC measurements with respect to the magnified and nonmagnified fields of view. The lateral and axial resolution, slice thickness, and caliper accuracy (vertical and horizontal) as a function of varying overall receiver gain and dynamic range, were obtained using conventional (no zoom) as well as a magnified (zoom) field of view (FOV). Each measurement was performed three times by a single observer using a 4 MHz "vector" format transducer on a single diagnostic medical ultrasound scanner. The results show no statistical significance in the variability of most recorded masurements when using the conventional versus the magnified FOV. However, in some cases, such as lateral resolution, the average value measured using the magnified FOV was typically 0.5 mm lower than when using a conventional FOV.

A mechanistic view of the non-ideal osmotic and motional behavior of intracellular water.

It is commonly assumed that essentially all of the water in cells has the same ideal motional and colligative properties as does water in bulk liquid state. This assumption is used in studies of volume regulation, transmembrane movement of solutes and electrical potentials, solute and solution motion, solute solubility and other phenomena. To get at the extent and the source of non-ideally behaved water (an operational term dependent on the measurement method), we studied the motional and colligative properties of water in cells, in solutions of amino acids and glycine peptides whose surface characteristics are known, and in solution of bovine serum albumin, hemoglobin and some synthetic polypeptides. Solutions of individual amino acids with progressively larger hydrophobic side chains showed one perturbed water molecule (structured-slowed in motion) per nine square angstroms of hydrophobic surface area. Water molecules adjacent to hydrophobic surfaces form pentagonal structural arrays, as shown by X-ray diffraction studies, that are reported to be disrupted by heat, electric field, hydrostatic pressure and phosphorylation state. Hydrophilic amino acids demonstrated water destructuring (increased motion) that was attributed to dielectric realignment of dipolar water molecules in the electric field between charge groups. In solutions of proteins, several methods indicate the equivalent of 2-8 layers of structured water molecules extending beyond the protein surface, and we have recently demonstrated that induced protein conformational change modifies the extent of non-ideally behaved water. Water self-diffusion rate as measured in three different cell types was about half that of bulk water, indicating that most of the water in these cells was slower in motion than bulk water. In different cell types the extent of osmotically perturbed water ranged from less that half to almost all of the intracellular water. The assumption that essentially all intracellular water has ideal osmotic and motional behavior is not supported by the experimental findings. The non-ideally of cell water is an operational term. Therefore, the amount of non-ideally behaving water is dependent on the characteristics of water targeted, i.e. the measurement method, and a large fraction of it is explainable in mechanistic terms at a molecular level based on solute-solvent interactions.

Osmotic pressure method to measure salt induced folding/unfolding of bovine serum albumin.

A new approach has been developed to monitor protein folding by utilizing osmotic pressure and a range of salt concentrations in a well characterized protein, bovine serum albumin (BSA). It is hypothesized that both the 'effective' osmotic molecular weight, Ae, and the solute/solvent interaction parameter, I, in the empirical relation Msolvent/Msolute = (RT rho/Ae)1/pi + I [1] can be used as measures of protein folding. I is a measure of solvent perturbed by the solute and is thought to depend directly upon the solvent accessible surface area (ASA). It is reasoned that larger solvent accessible surface area of an unfolded or denatured protein should perturb more water and produce larger I-values. Thus I-values allow calculation of a unfolded protein fraction, fua, due to changes in relative solvent accessible surface area. It has been observed that Ac decreases for filamentous, denatured proteins due to segmental motion of the molecule [2]. This allows calculation of unfolded protein fraction from the effective molecular weight, fum. Colloid osmotic pressure of BSA was measured in a range of salt concentrations at 25 degrees C, and pH = 7 (above the isoelectric point of BSA at pH = 5.4). Both S and I were used to monitor protein folding as the salt concentration was varied. In general, larger and variable I-values and smaller Ae were observed at salt concentrations less than 50 mmolal NaCl (Imax = 8.9), while constant I = 4.1 and Ae = 66,500 were observed above 50 mmolal NaCl. The two expressions for fractional unfolding (fua and fum) are in general agreement. Small differences in the parameters below 50 mmolal salt concentration are explained with well known shifts in the relative amounts of alpha-helix, beta-sheet and random coil in denatured BSA. The relative amounts of these shifts agree with predictions in the literature attributed to continuous BSA expansion rather than an 'all-or-none' conversion.

A study of the molecular sources of nonideal osmotic pressure of bovine serum albumin solutions as a function of pH.

The nonideal osmotic pressure of bovine serum albumin (BSA) solutions was studied extensively by Scatchard and colleagues. The extent of pH- and salt-dependent nonideality changes are large and unexplained. In 1992, Fullerton et al. derived new empirical expressions to describe solution nonideal colligative properties including osmotic pressure (Fullerton et al. 1992. Biochem. Cell Biol. 70:1325-1331). These expressions are based on the concepts of volume occupancy and hydration force. Nonideality is accurately described by a solute/solvent interaction parameter I and an "effective" osmotic molecular weight Ae. This paper uses the interaction-corrected nonideal expressions for osmotic pressure to calculate the hydration I values and "effective" osmotic molecular weight of BSA, Ae, as a function of pH. Both factors vary in a predictable manner due to denaturing of the BSA molecule. Both contribute to an increase in osmotic pressure for the same protein concentration as the solution pH moves away from the isoelectric point. Increased nonideality is caused by larger hydration resulting from larger solvent-accessible surface areas and by the decrease in "effective" osmotic molecular weight, Ae, due to segmental motion of denatured (filamentous) molecules.

Method to improve the accuracy of membrane osmometry measures of protein molecular weight.

Membrane osmometry provides a simple method to determine protein molecular weight but accuracy is limited by nonideal behavior. Recent studies (Fullerton et al., Biochem. Cell Biol., in press) show that non-ideal osmotic response of protein solutions is described by the empirical equation, Msv/M(s) = RT rho/A(s) x 1/II+I, where M(s) = mass of solute, Msv = mass of solvent, R = the Universal gas constant, T = absolute temperature, rho = solvent density, A(s) = solute molecular mass, II = osmotic pressure, and I = the nonideality parameter. This linear relation is used in this paper to demonstrate that measurement of molecular weight from the slope simplifies such measures and improves the accuracy relative to classical methods. The molecular weight of bovine serum albumin is measured with error less than 0.9%. The single dimensionless non-ideality parameter, I = 4.05 + 0.07, describes non-ideal curvature in the typical IIV = nRT diagram better than the customary second power viral expansion requiring 3 fitting constants. Analysis of eight data sets on four proteins from the literature shows that molecular weight calculated from the slope of the new equation agrees with chemical molecular weight within an RMS error of only 1.9%.