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PubMedDate not supplied

Single-leg jump-landing stabilization times in subjects with functionally unstable ankles.

CONTEXT: Factors contributing to functional ankle instability may cause individuals with the condition to land from a jump differently than those with stable ankles. OBJECTIVE: To determine stabilization time differences during single-leg jump landings between stable and unstable ankle groups and to report the reliability and precision of time-to-stabilization measures. DESIGN: A mixed design with 1 between factor (ankle group) and 1 within factor (direction) was used to analyze the comparison between our 10 subjects with functional ankle instability and 10 subjects with stable ankles. Time to stabilization (seconds) was the dependent measure. Reliability for time-to-stabilization measures of our 12 additional subjects with stable ankles were assessed using intraclass correlation coefficients (ICC 2,7). Standard errors of measurements were also calculated for time-to-stabilization measures. SETTING: Sports medicine research laboratory. PATIENTS OR OTHER PARTICIPANT(S): Ten subjects with functional ankle instability who reported at least 2 sprains and "giving way'' sensations at their ankles constituted the functional ankle instability group. Ten subjects without a history of ankle sprain injury served as healthy subjects. Twelve additional healthy subjects participated in the reliability study. INTERVENTION(S): Subjects performed a jump-landing test, which required them to jump 50% to 55% of their maximum vertical jump height and then land on a single leg on a force plate. After landing, they stabilized quickly and remained as motionless as possible in a single-leg stance for 20 s. MAIN OUTCOME MEASURE(S): Anterior-posterior and medial/ lateral vibration magnitude curve fit time-to-stabilization. RESULTS: Time to stabilization was longer for the functional ankle instability group (1.98 +/- 0.81 s) than for the stable ankle group (1.45 +/- 0.30 s) (P < .05). Reliability (standard error of the measurement) values for anterior/posterior and medial/lateral time-to-stabilization were 0.79 (0.15 s) and 0.65 (0.26 s), respectively. CONCLUSIONS: Time to stabilization was longer for subjects with functional ankle instability than subjects with stable ankles. The ankle instability may have impaired the subjects' ability to stabilize after a single-leg jump landing. Reliabilities and standard errors of the measurements of time-to-stabilization measures were moderate and low, respectively.

Journal Article↗

PubMed1993

The effect of stabilization on isokinetic knee extension and flexion torque production.

The purpose of this study was to examine the effect of four methods of stabilization on maximal reciprocal isokinetic knee extension and flexion. Left knee extension/flexion was tested at 60 degrees /s in 20 subjects. Warm-up consisted of five submaximal and one maximal effort followed by three maximal efforts in each of four randomized stabilization conditions: 1) Hands and back stabilization; the trunk was strapped to the back rest and the hands grasped the seat. 2) Back stabilization; the trunk was strapped to the back rest and the hands were folded across the chest. 3) Hand stabilization; the hands grasped the seat and the back rest was removed. 4) No stabilization; the hands were folded across the chest and the back rest was removed. One-way repeated measures ANOVA showed a significant effect of stabilization for knee extension (F(3,57)=17.44, p=.0001) and knee flexion (F(3,57)= 5.37, p=.002). Paired, two-tailed student's t-tests with Bonferroni correction showed that, in knee extension, no stabilization was significantly less than all others, p<.001. In addition, back stabilization was less than hands and back stabilization, p<.005. In knee flexion, no stabilization was significantly less than all others, p<.01. In conclusion, the method of trunk stabilization significantly affected maximal reciprocal isokinetic knee extension/flexion strength measurements. Maximal knee extension/flexion torque production was achieved when the trunk was strapped to the back support and when the hands grasped the seat.

Journal Article↗

PubMedDate not supplied

[Complications of a transpedicular stabilization of thoraco-lumbar burst fractures].

Complications of transpedicular stabilizations of thoraco-lumbar burst fractures are presented on the basis of literature review and own experiences. Unstable thoraco-lumbar burst fractures create the most difficult biomechanical conditions for a stabilizer. A literature review was done to estimate the effectiveness of vertebral body height restoration and its maintenance, the effectiveness of transpedicular grafting, the fusion rate and the implant-related complications rate. Transpedicular stabilization systems demonstrate a marked stiffness in all directions which is greater than in the case of other posterior stabilization systems. During the postero-lateral spondylodesis the transpedicular stabilizer is gradually unburdened but it is still loaded even after the completion of the bone fusion. A support of the anterior spinal column markedly diminishes the loads of the stabilizer and improves the segmental stability. Long-term follow-up studies of transpedicularly stabilized burst fractures reveal a deterioration of primarily good corrections. In some cases the correction returns to the level from before the operation in spite of transpedicular bone grafting. The implant-related complications rate (screw or rod breakages and a loss of interconnections) reaches up to 28 % of cases. In order to improve the anterior column stability and limit late kyphotization, as well as avoid implant-related complications, some authors additionally recommend performing a posterior interbody fusion (PLIF) or an anterior corpectomy with stabilization. Posterior transpedicular stabilization of thoraco-lumbar burst fractures does not provide a complete stabilization of the anterior spinal column, which results in a recurrence of spine kyphotization and implant-related complications. In selected cases, the application of an additional anterior column support markedly relieves the transpedicular fixator and reduces the pseudoarthrosis rate, late kyphotization and implant-related complications simultaneously.

Bone Screws↗

PubMed1996

The stability of human beta-globin mRNA is dependent on structural determinants positioned within its 3' untranslated region.

Controls that act at both transcriptional and posttranscriptional levels assure that globin genes are highly expressed in developing erythroid cells. The extraordinary stabilities of alpha- and beta-globin mRNAs permit globin proteins to accumulate to substantial levels in these cells, even in the face of physiologic transcriptional silencing. Structural features that determine alpha-globin mRNA stability have recently been identified within its 3'UTR; in contrast, the structural features that determine beta-globin mRNA stability remain obscure. The current study begins to define the structural basis for beta-globin mRNA stability. Two tandem antitermination mutations are introduced into the wild-type human beta-globin gene that permit ribosomes to read into the 3'UTR of the encoded beta-globin mRNA. The readthrough beta-globin mRNA is destabilized in cultured erythroid cells, indicating that, as in human alpha-globin mRNA, an unperturbed 3'UTR is crucial to maintaining mRNA stability. Additional experiments show that the beta-globin and alpha-globin mRNA 3'UTRs provide equivalent levels of stability to a linked beta-globin mRNA coding region, suggesting a parallel in their functions. However, destabilization of the antiterminated beta-globin mRNA is independent of active translation into the 3'UTR, whereas translation into the alpha-globin mRNA 3'UTR destabilizes a linked beta-globin coding region in a translationally dependent manner. This indicates that the alpha- and beta-globin 3'UTRs may stabilize linked mRNAs through distinct mechanisms. Finally, it is shown that neither of the two mutations that, in combination, destabilize the beta-globin mRNA have any effect on beta-globin mRNA stability when present singly, suggesting potential redundancy of stabilizing elements. In sum, the current study shows that a functionally intact beta-globin mRNA 3'UTR is crucial to maintaining beta-globin mRNA stability and provides a level of stability that is functionally equivalent to, although potentially mechanistically distinct from, the previously characterized alpha-globin mRNA 3'UTR stability element.

Animals↗

PubMed2005

Neural network-based prediction of mutation-induced protein stability changes in Staphylococcal nuclease at 20 residue positions.

Protein-based therapeutics are playing an increasingly important role in the treatment of diseases, including diabetes and cancer. The viability of these treatments, however, are highly dependent on the stability of the therapeutic, since stability affects both the shelf life of the therapeutic as well as its active life in the body. Stability engineering can, therefore, be used to increase the effectiveness of protein-based therapeutics. Computational methods of protein stability prediction have been under development for about a decade, but complex molecular interactions make stability prediction difficult and computationally intensive. A rapid computational method of protein stability prediction is developed using feed-forward neural networks and used to predict mutation-induced stability changes in Staphylococcal nuclease. The input to the neural network consisted of sequences of evolutionarily based amino acid similarity scores that were obtained through the comparison of the amino acids in a mutation containing sequence to their positional counterparts in the baseline wild-type amino acid sequence. A training set was created which consisted of similarity score sequences, for which the stabilities of the corresponding amino acid sequences were known, paired with the relative stabilities of the sequences to that of the baseline. Back-propagation of error was used to train the network to output accurate relative stability scores for the sequences in the training set. Neural network-based relative stability predictions for 55 sequences containing mutation combinations not found in the training set had an accuracy of 92.8%.

Amino Acid Sequence↗

PubMed1998

The structural stability of the HIV-1 protease.

The most common strategy in the development of HIV-1 protease inhibitors has been the design of high affinity transition state analogs that effectively compete with natural substrates for the active site. A second approach has been the development of compounds that inactivate the protease by destabilizing its quaternary or tertiary structure. A successful optimization of these strategies requires an accurate knowledge of the energetics of structural stabilization and binding, and the identification of those regions in the protease molecule that are critical to stability and function. Here the energetics of stabilization of the HIV-1 protease has been measured for the first time by high sensitivity differential scanning calorimetry. These studies have permitted the evaluation of the different components of the Gibbs energy of stabilization (the enthalpy, entropy and heat capacity changes). The stability of the protease is pH-dependent and due to its dimeric nature is also concentration-dependent. At pH 3.4 the Gibbs energy of stabilization is close to 10 kcal/mol at 25 degreesC, consistent with a dissociation constant of 5x10(-8) M. The stability of the protease increases at higher pH values. At pH 5, the Gibbs energy of stabilization is 14.5 kcal/mol at 25 degreesC, consistent with a dissociation constant of 2.3x10(-11) M. The pH dependence of the Gibbs energy of stabilization indicates that between pH 3.4 and pH 5 an average of 3-4 ionizable groups per dimer become protonated upon unfolding. A structure-based thermodynamic analysis of the protease molecule indicates that most of the Gibbs energy of stabilization is provided by the dimerization interface and that the isolated subunits are intrinsically unstable. The Gibbs energy, however, is not uniformly distributed along the dimerization interface. The dimer interface is characterized by the presence of clusters of residues (hot spots) that contribute significantly and other regions that contribute very little to subunit association. At the dimerization interface, residues located at the carboxy and amino termini contribute close to 75% of the total Gibbs energy (Cys95, Thr96, Leu97, Asn98 and Phe99 and Pro1, Ile3, Leu5). Residues Thr26, Gly27 and Asp29 located at the base of the active site are also important, and to a lesser extent Gly49, Ile50, Gly51 located at the tip of the flap region. The structure-based thermodynamic analysis also predicts the existence of regions of the protease with only marginal stability and a high propensity to undergo independent local unfolding. In particular, the flap region occupies a very shallow energy minimum and its conformation can easily be affected by relatively small perturbations. This property of the protease can be related to the ability of some mutations to elicit resistance towards certain inhibitors.

Calorimetry, Differential Scanning↗

PubMed1998

Proteins from hyperthermophiles: stability and enzymatic catalysis close to the boiling point of water.

It has become clear since about a decade ago, that the biosphere contains a variety of microorganisms that can live and grow in extreme environments. Hyperthermophilic microorganisms, present among Archaea and Bacteria, proliferate at temperatures of around 80-100 degrees C. The majority of the genera known to date are of marine origin, however, some of them have been found in continental hot springs and solfataric fields. Metabolic processes and specific biological functions of these organisms are mediated by enzymes and proteins that function optimally under these extreme conditions. We are now only starting to understand the structural, thermodynamic and kinetic basis for function and stability under conditions of high temperature, salt and extremes of pH. Insights gained from the study of such macromolecules help to extend our understanding of protein biochemistry and -biophysics and are becoming increasingly important for the investigation of fundamental problems in structure biology such as protein stability and protein folding. Extreme conditions in the biosphere require either the adaptation of the amino acid sequence of a protein by mutations, the optimization of weak interactions within the protein and at the protein-solvent boundary, the influence of extrinsic factors such as metabolites, cofactors, compatible solutes. Furthermore folding catalysts, known as chaperones, that assist the folding of proteins may be involved or increased protein protein synthesis in order to compensate for destruction by extreme conditions. The comparison of structure and stability of homologous proteins from mesophiles and hyperthermophiles has revealed important determinants of thermal stability of proteins. Rather than being the consequence of one dominant type of interactions or of a general stabilization strategy, it appears that the adaptation to high temperatures reflects a number of subtle interactions, often characteristic for each protein species, that minimize the surface energy and the hydration of apolar surface groups while burying hydrophobic residues and maximizing packing of the core as well as the energy due to charge-charge interactions and hydrogen bonds. In this article, mechanisms of intrinsic stabilization of proteins are reviewed. These mechanisms are found on different levels of structural organization. Among the extrinsic stabilization factors, emphasis is put on archaea chaperonins and their still strongly debated function. It will be shown, that optimization of weak protein-protein and protein-solvent interactions plays a key role in gaining thermostability. The difficulties in correlating suitable optimization criteria with real thermodynamic stability measures are due to experimental difficulties in measuring stabilization energies in large proteins or protein oligomers and will be discussed. Thus small single domain proteins or isolated domains of larger proteins may serve as model systems for large or multidomain proteins which due to the complexity of their thermal unfolding transitions cannot be analyzed by equilibrium thermodynamics. The analysis of the energetics of the thermal unfolding of a small, hyperthermostable DNA binding protein from Sulfolobus has revealed that a high melting temperature is not synonymous with a larger maximum thermodynamic stability. Finally, it is now well documented, that many thermophilic and hyperthermophilic proteins show a statistically increased number of salt bridges and salt bridge networks. However their contribution to thermodynamic and functional stability is still obscure.

Amino Acid Sequence↗

PubMed2006

Stabilization of interface-binding chloroperoxidase for interfacial biotransformation.

The stability of an interface-binding chloroperoxidase (CPO) against the deactivation effect of H(2)O(2) was examined. Native CPO was conjugated with polystyrene and thus self-assembled at the water-oil interface. Although the interface-assembled CPO showed improved stability as compared to native CPO, enzyme deactivation as a result of the side effect of H(2)O(2), still limits the overall productivity of the enzyme. Two approaches to further improve the stability of CPO were examined in this work. In one approach, several stabilizers including poly(ethylene glycol) (PEG), PEI, glycerol, sugars and sucrose monododecanoate were used; while in a second approach, in situ generation of hydrogen peroxide (H(2)O(2)) by using glucose oxidase (GOx) was applied. PEG was found exceptional in that it increased both the operational and storage stability of CPO. The best improvement of enzyme productivity was obtained with addition of PEG which led to an increase of 57% for interface-bound CPO and 33% for native CPO. One interesting observation with PEI is that it enhanced the storage stability against H(2)O(2) deactivation, but did not affect the enzyme's operational stability. On the other hand, glucose enhanced the operational stability by two folds, but exhibited no significant effect on storage stability. It was also found that the extended operational lifetime of CPO with in situ generation of H(2)O(2) by GOx was a result that combines the stabilizing effect of glucose and lowered concentration of H(2)O(2). Interestingly, the addition of stabilizers could improve the enantioselectivity of CPO by as much as 10%.

Biotransformation↗

PubMed1997

Significant role of electrostatic interactions for stabilization of protein assemblies.

Contribution of electrostatic interactions to stability of BPTI orthorhombic, pig-insulin cubic crystals, and horse L ferritin crystals was evaluated with numerical calculation of Poisson-Boltzmann equation based on a dielectric model. The stability of a ferritin molecule (24-mer) composed of 24 subunits was also evaluated. It was found that the surface charge-charge interactions at separation distances (< 5 A) were insensitive to variations in the ionic strength, and thus stabilized assembled states of the proteins (i.e., crystalline state and oligomeric state). It was also revealed that the charge density and the packing of the protein crystals were largely responsible for the ionic strength dependence of the crystal stability. The stability of the 5PTI crystalline state with a high charge density drastically increased as the concentration of the solvent ions increased. In contrast, that of the insulin crystal with a low charge density and large solvent region was insensitive to changes in the ionic concentration. The electrostatic interaction between ferritin 24-mers was attributed to two salt bridges mediated by Cd ion. For the stability of the ferritin 24-mer, which is evolutionally designed, the electrostatic stabilization between the subunits was attributed to polar bonds such as buried salt bridges or hydrogen bonds, which occasionally yielded more than 5 kcal/mol and were numerous and very strong compared with the bonds between molecules in the 5PTI and 9INS crystals. By analyzing the atomic charge-charge interactions in detail, it was found that charge pairs separated by less than 3 A, such as hydrogen bonds, dominantly stabilize the assembled states, and that pairs 3 to 5 A apart were also important. The stability of the assembled states evaluated by the total EET was determined by the fine balance between the two competing contributions arising from the stabilizing atoms and the destabilizing atoms. Changes of the ASA and hydration free energy were also evaluated in accordance with the process of the subunit assembly. The change of hydration free energy, which was very large (i.e., approximately +100 kcal/mol/subunit) and unfavorable for the assembly, was proportional to the electrostatic hydration energy (i.e., Born energy change in the hydration process). Hydrophobic groups were likely to appear more frequently than hydrophilic groups at the interfaces. This study offers a method which can improve the stability of protein crystals by introducing polar or charged residues that are properly designed to form specific hydrogen bonds or salt bridges between neighboring protein molecules. This method is also applicable to crystallography, because it improves refinement of protein structures in crystals by taking the inter-protein interactions into account.

Algorithms↗

PubMed2003

Lipid oxidation in corn oil-in-water emulsions stabilized by casein, whey protein isolate, and soy protein isolate.

Proteins can be used to produce cationic oil-in-water emulsion droplets at pH 3.0 that have high oxidative stability. This research investigated differences in the physical properties and oxidative stability of corn oil-in-water emulsions stabilized by casein, whey protein isolate (WPI), or soy protein isolate (SPI) at pH 3.0. Emulsions were prepared with 5% corn oil and 0.2-1.5% protein. Physically stable, monomodal emulsions were prepared with 1.5% casein, 1.0 or 1.5% SPI, and > or =0.5% WPI. The oxidative stability of the different protein-stabilized emulsions was in the order of casein > WPI > SPI as determined by monitoring both lipid hydroperoxide and headspace hexanal formation. The degree of positive charge on the protein-stabilized emulsion droplets was not the only factor involved in the inhibition of lipid oxidation because the charge of the emulsion droplets (WPI > casein > or = SPI) did not parallel oxidative stability. Other potential reasons for differences in oxidative stability of the protein-stabilized emulsions include differences in interfacial film thickness, protein chelating properties, and differences in free radical scavenging amino acids. This research shows that differences can be seen in the oxidative stability of protein-stabilized emulsions; however, further research is needed to determine the mechanisms for these differences.

Chemical Phenomena↗

PubMed2005

Kinetic analysis about the effects of neutral salts on the thermal stability of yeast alcohol dehydrogenase.

The effects of salts on the rate constants of inactivation by heat of yeast alcohol dehydrogenase (YADH) at 60.0 degrees C were measured. Different effects were observed at low and high salt concentrations. At high concentrations, some salts had stabilizing effects, while others were destabilizing. The effects of salts in the high concentration range examined can be described as follows: (decreased thermal stability) NaClO(4) < NaI = (C(2)H(5))(4)NBr < NH(4)Br < NaBr = KBr = CsBr = (no addition) < (CH(3))(4)NBr < KCl < KF < Na(2)SO(4) (increased thermal stability). The decreasing effect of NaClO(4) on YADH controlled the thermal stability of the enzyme absolutely and was not compensated by the addition of Na(2)SO(4), a salt which stabilized the enzyme. However, Na(2)SO(4) compensation did occur in response to the decrease in thermal stability caused by (C(2)H(5))(4)NBr. The rate constants of inactivation by heat (k (in)) of the enzyme were measured at various temperatures. Effective values of the thermodynamic activation parameters of thermal inactivation, activation of free energy (DeltaG (double dagger)), activation enthalpy (DeltaH (double dagger)), and activation entropy (DeltaS (double dagger)), were determined. The thermal stability of YADH in 0.8 M Na(2)SO(4) increased more than that of pyruvate kinase from Bacillus stearothermophilus, a moderate thermophile. The changes in the values of DeltaH (double dagger) and DeltaS (double dagger) were great and showed a general compensatory tendency, with the exception of in the case of NaClO(4). The temperature for the general compensation effect (T (c)) was approximately 123 degrees C. With Na(2)SO(4), the thermal stability of YADH at a temperature below T (c) was greater than that in the absence of salt due to the higher values of DeltaH (double dagger) and DeltaS (double dagger), respectively, and thus was an example of low-temperature enzymatic stabilization. With (C(2)H(5))(4)NBr, the thermal stability of YADH at a temperature below T (c) was lower than that in the absence of salt due to the lower values of DeltaH (double dagger) and DeltaS (double dagger), respectively, and thus was an example of low-temperature enzymatic destabilization. But with NaClO(4), the changes in the values of DeltaH (double dagger) and DeltaS (double dagger) were small and the thermal stability of YADH was thus an example of high-temperature enzymatic destabilization.

Alcohol Dehydrogenase↗

PubMed2005

Low-magnesium, trans-cleavage activity by type III, tertiary stabilized hammerhead ribozymes with stem 1 discontinuities.

BACKGROUND: Low concentrations of free magnesium in the intracellular environment can present critical limitations for hammerhead ribozymes, especially for those that are designed for intermolecular (trans) cleavage of a host or pathogen RNA. Tertiary stabilizing motifs (TSM's) from natural and artificial ribozymes with a "type I" topology have been exploited to stabilize trans-cleaving hammerheads. Ribozymes with "type II" or "type III" topologies might seem incompatible with conversion to trans-cleavage designs, because opening the loop at the end of stem 1 or stem 2 to accommodate substrate binding is expected to disrupt the TSM and eliminate tertiary stabilization. RESULTS: Stem 1, together with single-stranded segments capping or internal to this stem, contains both the substrate-binding and tertiary stabilization functions. This stem was made discontinuous within the sTRSV hammerhead ribozyme, thereby separating the two functions into discrete structural segments. The resulting ribozyme, designated "RzC," cleaved its 13 nucleotide target substrate at MgCl2 concentrations as low as 0.2 mM at 25 degrees C and 0.5 mM at 37 degrees C. Under multiple-turnover conditions, nearly thirty turnovers were observed at the highest substrate:RzC ribozyme ratios. Similar stabilization was observed for several derivatives of RzC. Catalytic activity was diminished or eliminated at sub-millimolar MgCl2 concentrations for ribozymes with weakened or deleted tertiary interactions. Eadie-Hofstee analysis revealed that the stabilized and non-stabilized ribozymes bind their substrates with equivalent affinities, suggesting that differences in observed activity are not the result of diminished binding. Some of the stabilized and non-stabilized ribozymes appear to fold into a heterogeneous collection of conformers, only a subset of which are catalytically active. CONCLUSION: Hammerhead ribozymes with the "type III" topology can be converted to a tertiary, trans-cleavage design. Separating the stabilization and substrate recognition functions of stem 1 increases cleavage activity at physiological concentrations of divalent magnesium while retaining recognition of exogenous targets. Trans-cleaving ribozymes that exploit the tertiary stabilizing motifs of all natural hammerhead topologies can therefore be used in intracellular applications.

Enzyme Activation↗

PubMed2026

Effects of an actuated ankle exoskeleton on walking stability in healthy adults: a controlled laboratory study.

BACKGROUND: Ankle exoskeletons are widely used to reduce the metabolic cost of walking, yet their effects on walking stability during unperturbed gait remain insufficiently understood. Walking stability can be characterized using complementary measures that capture stride-to-stride variability, global temporal organization, and local dynamic stability. Understanding how walking with an actuated ankle exoskeleton system influences these different aspects of gait stability is essential for the safe design and control of wearable robotic devices. METHODS: Eighteen healthy adults walked on a treadmill at a constant speed (1.1 m/s) with and without an actuated bilateral ankle exoskeleton in a randomized crossover design. Spatiotemporal variability was quantified using coefficients of variation (CoV) of stride length, step width, and stance ratio. Global gait stability was assessed using detrended fluctuation analysis of stride time. Local dynamic stability was evaluated using maximum Lyapunov exponent calculated for the trunk, hip, upper leg, lower leg, and foot. Paired-samples two-sided t-tests were used to compare conditions. RESULTS: Walking with the ankle exoskeleton resulted in increased stride-to-stride spatiotemporal variability, reflected by higher CoV values for stride length (p < 0.001) and stance ratio (p = 0.005), while mean stride length and step width remained unchanged. Mean stance ratio was reduced in the exoskeleton condition (p < 0.001). Global gait stability did not differ between conditions, indicating preserved long-range temporal gait organization. Local dynamic stability increased at the lower leg (p < 0.001) and foot (p = 0.019) when walking with the exoskeleton. CONCLUSIONS: Walking with the actuated ankle exoskeleton alters gait control across multiple levels during steady walking. While stride-to-stride variability in stride length and stance ratio increased, global gait stability remained unchanged. Local dynamic stability was increased at the lower leg and foot, suggesting segment-specific effects of ankle-level assistance close to the assisted joint. However, these findings should be interpreted as the combined effect of wearing the exoskeleton and receiving active assistance, rather than the isolated effect of plantarflexion assistance. These results provide insight for the design and control of ankle exoskeletons with respect to stability-related effects during walking.

Humans↗

PubMed1998

Use of stabilized technetium-99m-exametazime for radiolabeling leukocytes.

UNLABELLED: With a stabilizing agent (i.e., methylene blue and sodium phosphate buffer mixture), the in vitro stability of 99mTc-exametazime has been increased to 4-6 hr postreconstitution. However, it is not feasible to use the stabilized 99mTc-exametazime for leukocyte radiolabeling. This is due to the deep blue appearance of the mixture of stabilized 99mTc-exametazime and blood components, which makes it impossible to separate properly the supernatant from the leukocyte button. In our study, we have developed a practical methodology for overcoming this difficulty in order to use stabilized 99mTc-exametazime in leukocyte labeling. METHODS: The stabilized 99mTc-exametazime preparation used in our method consisted of 2 ml 7.4-8.0 GBq (200-215 mCi) 99mTc and 2 ml methylene blue/phosphate buffer solution. The separated leukocytes from 80-ml fresh venous blood were incubated with three different ages (i.e., 0-, 4-, or 6-hr postreconstitution) of stabilized 99mTc-exametazime (approximately 925 MBq, approximately 25 mCi; 0.5-1 ml) at room temperature for 15 min. After incubation, 3 ml of 12.6% ACD/NS solution (anticoagulant citrate dextrose, solution A, USP mixed with 0.9% NaCl, v/v) was added to the tube and centrifuged at 160 g for 5 min. Three milliliters of the dark blue supernatant were carefully removed, and the bottom 1 ml portion was resuspended with 9 ml of 12.6% ACD/NS solution. After centrifugation (160 g for 5 min), the supernatant was clear enough to be drawn off without disturbing the radiolabeled leukocyte button. The white cell button was then resuspended in 4 ml of platelet-poor plasma. RESULTS: The overall labeling efficiency (LE) of our new technique was 67.8%-91.9%, with the higher LE associated with fresher stabilized 99mTc-exametazime. During a 6-hr in vitro stability evaluation, radiolabeled leukocytes lost 1.2% +/- 0.3% (n = 24), 1.3% +/- 0.1% (n = 16) and 1.8% +/- 0.1% (n = 16) each hour of the cell-bound 0-, 4-, and 6-hr-old 99mTc-exametazime, respectively. The 99mTc-exametazime-labeled leukocytes examined by the trypan blue staining technique at 6-hr postradiolabeling yielded nonstained cells indicating viable leukocytes. CONCLUSION: We concluded that with a small volume of 99mTc-exametazime and double dilution steps with 12.6% ACD/NS solution, stabilized 99mTc-exametazime can be used effectively for leukocyte radiolabeling with a high LE and long in vitro stability.

Drug Stability↗

PubMed1998

Time to clinical stability in patients hospitalized with community-acquired pneumonia: implications for practice guidelines.

CONTEXT: Many groups have developed guidelines to shorten hospital length of stay in pneumonia in order to decrease costs, but the length of time until a patient hospitalized with pneumonia becomes clinically stable has not been established. OBJECTIVE: To describe the time to resolution of abnormalities in vital signs, ability to eat, and mental status in patients with community-acquired pneumonia and assess clinical outcomes after achieving stability. DESIGN: Prospective, multicenter, observational cohort study. SETTING: Three university and 1 community teaching hospital in Boston, Mass, Pittsburgh, Pa, and Halifax, Nova Scotia. PATIENTS: Six hundred eighty-six adults hospitalized with community-acquired pneumonia. MAIN OUTCOME MEASURES: Time to resolution of vital signs, ability to eat, mental status, hospital length of stay, and admission to an intensive care, coronary care, or telemetry unit. RESULTS: The median time to stability was 2 days for heart rate (< or =100 beats/min) and systolic blood pressure (> or =90 mm Hg), and 3 days for respiratory rate (< or =24 breaths/min), oxygen saturation (> or =90%), and temperature (< or =37.2 degrees C [99 degrees F]). The median time to overall clinical stability was 3 days for the most lenient definition of stability and 7 days for the most conservative definition. Patients with more severe cases of pneumonia at presentation took longer to reach stability. Once stability was achieved, clinical deterioration requiring intensive care, coronary care, or telemetry monitoring occurred in 1% of cases or fewer. Between 65% to 86% of patients stayed in the hospital more than 1 day after reaching stability, and fewer than 29% to 46% were converted to oral antibiotics within 1 day of stability, depending on the definition of stability. CONCLUSIONS: Our estimates of time to stability in pneumonia and explicit criteria for defining stability can provide an evidence-based estimate of optimal length of stay, and outline a clinically sensible approach to improving the efficiency of inpatient management.

Adult↗

PubMed2001

[Biomechanical stability with a new artificial vertebral body implant. 3-dimensional movement analysis of instrumented human vertebral segments].

UNLABELLED: The authors present a new implant for vertebral body replacement in the thoracic and lumbar spine. The titanium implant is designated for reconstruction of the anterior column in injury, posttraumatic kyphosis or tumor of the thoracolumbar spine. The instrumentation has to be supplemented by a stabilizing implant. After positioning, the implant is distracted in situ, through which best contact to adjacent end-plates and 3-dimensional stability should be provided. The possibility of secondary dislocation or loss of correction should thereby be minimized. OBJECTIVES: We investigated the biomechanical 3-dimensional stability in vitro, using Synex in combination with an anteriorly (Ventrofix) or a posteriorly (USS) stabilizing implant. The differences between both stabilizing implants were to be determined. Synex was compared with the "Harms titanium mesh cage" (MOSS) as vertebral body replacement. METHODS: In a 3-dimensional spinal loading simulator, we determined the bisegmental (T12-L2) neutral zone (NZ), elastic zone (EZ), and range of motion (ROM) of 12 human cadaveric spines. After corpectomy of L1 we tested 4 groups of implant combinations: USS/Synex, USS/MOSS, Ventrofix/Synex, Ventrofix/MOSS. We analyzed the differences between each of the instrumentations as well as differences compared to the intact spine. RESULTS: In most directions, significantly higher stability was achieved with USS, compared with Ventrofix and the intact specimen. For axial rotation, with no instrumentation the stability of the intact spine was restored. With Synex a significantly higher stability was noted for extension, lateral bending, and axial rotation in comparison with the Harms cage. A tendency towards more stability for flexion was additionally observed with Synex. When using MOSS in combination with USS, it was necessary to perform a third operative step for induction of intervertebral compression via the posterior fixator. CONCLUSIONS: The posterior fixation was found to offer superior stability compared to the anterior one. Synex was at least comparable to MOSS for suspensory replacement of the vertebral body in the thoracolumbar spine. The evidence of higher biomechanical stability with Synex leads to the probability of a higher rigidity in vivo. Due to the distractability of Synex, a better intervertebral compression was achieved. Therefore, an additional tightening of the posterior fixator after insertion of Synex was not necessary, in contrast to the Harms cage.

Biomechanical Phenomena↗

PubMed2005

The stability of axis I diagnoses in youth across multiple psychiatric hospitalizations.

The literature has yet to reach a consensus as to the stability of severe psychiatric diagnoses in youth. Previous studies among youngsters tracked over set follow-up periods have reported diagnostic stability estimates that are similar to or slightly lower than those of adults. Less is known, however, about the stability of youth psychiatric diagnoses across multiple episodes of psychopathology, such as recurrent inpatient hospitalizations. The present study investigated diagnostic stability among inpatient youth with multiple hospitalizations through longitudinal and cross-sequential designs. Results indicate that diagnostic stability, as measured by positive concordance rates and the kappa coefficient, is highest for mood disorders, especially bipolar disorder. Externalizing disorders and schizophrenia displayed moderate to low stability, with oppositional-defiant disorder displaying the lowest stability. Substance use disorders were found to have moderate stability. Overall, across-episode diagnostic stability among hospitalized youngsters appears to be lower than that of adults. This finding appears to be due to lower stability among certain externalizing disorders and substance use disorders, whereas mood disorders display stability rates resembling those of adults. Potential explanations for and implications of these findings are discussed.

Adolescent↗

PubMed1989

The role of protein-linked oligosaccharide in the bilayer stabilization activity of glycophorin A for dioleoylphosphatidylethanolamine liposomes.

The importance of the protein-linked carbohydrates for the stabilization of dioleoylphosphatidylethanolamine (DOPE) bilayers has been investigated using glycophorin A, the major sialoglycoprotein of the human erythrocyte membrane, as a stabilizer. Two major types of glycophorin, differing in the sialic acid content, were used in the study. Type MM contains 19.2 +/- 2.5 sialic residues per molecule of glycophorin, and type NN contains 10.8 +/- 1.2. Type MM could stabilize DOPE bilayers at 0.5 mol%, whereas type NN was unable to do so even at 1 mol%. The importance of the sialic acid content to the stabilization activity of glycophorin was further confirmed by the observation that the neuraminidase-treated type MM showed a lower stabilization activity than the untreated type. Since type NN had no stabilizing activity, we attempted to couple a trisaccharide, NeuNAc----Gal----Glc, to type NN by reductive amination. 2.5 +/- 0.8 saccharide chains were added per molecule of type NN. The trisaccharide-attached type NN showed a greater stabilization activity than the parent type NN molecule, indicating again that the sialic acid content of the stabilizer molecule determines the stabilization activity. Addition of wheat-germ agglutinin (WGA), which binds to the sialic acid residues of a glycoprotein, to type MM-stabilized liposomes caused rapid aggregation and destabilization of liposomes, resulting in leakage of an entrapped marker, calcein. The aggregation increased with increasing amount of the lectin; however, the leakage rate was maximum at an optimum concentration of WGA. These results are discussed in terms of the role of sialic acid in the interfacial hydration and charge repulsion which determines the DOPE bilayer stability.

Carbohydrate Sequence↗