Biomedical subjects

M Seaver

Publications and source records attributed to M Seaver.

6 recordsLinked to original sources

PubMed2005

Detecting nonlinearity in structural systems using the transfer entropy.

The transfer entropy was recently proposed as a means of exploring coupling in dynamical systems. Transfer entropy is an information theoretic that quantifies the degree to which one dynamical process affects the transition probabilities (dynamics) of another. Here we demonstrate how this metric may be utilized to detect the presence of nonlinearity in a system. Using the method of surrogate data, the transfer entropy computed at various lag times are compared to values computed from linearized surrogates. The transfer entropy is shown to be a more sensitive indicator of nonlinearity than is the mutual information for both simulated and experimental data. This technique is particularly applicable to the field of structural health monitoring, where damage is often equated with the presence of a nonlinearity in an otherwise linear system.

Journal Article↗

PubMed2003

Controlling system dimension: a class of real systems that obey the Kaplan-Yorke conjecture.

The Kaplan-Yorke conjecture suggests a simple relationship between the fractal dimension of a system and its Lyapunov spectrum. This relationship has important consequences in the broad field of nonlinear dynamics where dimension and Lyapunov exponents are frequently used descriptors of system dynamics. We develop an experimental system with controllable dimension by making use of the Kaplan-Yorke conjecture. A rectangular steel plate is driven with the output of a chaotic oscillator. We controlled the Lyapunov exponents of the driving and then computed the fractal dimension of the plate's response. The Kaplan-Yorke relationship predicted the system's dimension extremely well. This finding strongly suggests that other driven linear systems will behave similarly. The ability to control the dimension of a structure's vibrational response is important in the field of vibration-based structural health monitoring for the robust extraction of damage-sensitive features.

Models, Theoretical↗

PubMed2003

Use of chaotic excitation and attractor property analysis in structural health monitoring.

This work explores the utility of attractor-based approaches in the field of vibration-based structural health monitoring. The technique utilizes the unique properties of chaotic signals by driving the structure directly with the output of a chaotic oscillator. Using the Kaplan-Yorke conjecture, the Lyapunov exponents of the driving signal may be tuned to the dominant eigenvalues of the structure, thus controlling the dimension of the structural response. Data are collected at various stages of structural degradation and a simple nonlinear model, constructed from the undamaged data, is used to make predictions for the damaged response data. Prediction error is then introduced as a "feature" for classifying the magnitude of the damage. Results are presented for an experimental cantilevered beam instrumented with fiber-optic strain sensors.

Journal Article↗

PubMed2001

First results using automated epifluorescence microscopy to detect Escherichia coli and Staphylococcus epidermidis in WBC-reduced platelet concentrates.

BACKGROUND: Many methods have been tested for the detection of bacterial contamination in platelets. However, only those using molecular biology or cell culturing consistently detect contamination at levels below 10(5) bacteria per mL. This report describes the initial investigation into an alternative method that offers the possibilities of high sensitivity and rapid response while using available laboratory equipment and supplies. This method relies on a fluorescent nucleic acid stain, which preferentially stains bacteria but not platelets, and automated epifluorescence microscopy for rapid analysis. Measurements in WBC-reduced platelet concentrates (PCs) contaminated with bacteria are reported at concentrations between 10(3) and 10(6) bacteria per mL. STUDY DESIGN AND METHODS: Staphylococcus epidermidis or Escherichia coli was inoculated into aliquots of WBC-reduced PCs on Days 2 through 5 of storage. Bacterially inoculated and control PCs were stained, platelets and residual WBCs were lysed, and 200 microL of sample was filtered onto black polycarbonate filters. All preparations were done in triplicate. An automated epifluorescence microscope examined approximately 2 percent of the area of each filter and used image analysis to select the fluorescent particles that should be counted as bacteria. RESULTS: Samples containing 3 to 5 x 10(3) bacteria per mL produced about three times as many fluorescent particles classified as bacteria as the controls. Lower concentrations of S. epidermidis were detected because of higher fluorescence intensity. Simultaneous preparation of six samples requires about 35 minutes. Analysis of each prepared sample takes 10 minutes, for a total preparation and analysis time of about 95 minutes for 6 samples. CONCLUSION: Low concentrations (<5 x 10(3) bacteria/mL) of deliberately inoculated S. epidermidis or E. coli can be measured quickly in WBC-depleted PCs by using a fluorescent nucleic acid stain, differential lysis, and automated microscopy. Continued refinement of the method, studies employing other bacterial strains, and further validations of assay performance are warranted.

Automation↗

PubMed2000

Modification of wild-type and batrachotoxin-resistant muscle mu1 Na+ channels by veratridine.

Biochemical evidence indicates that veratridine (VTD) and batrachotoxin (BTX) share a common binding site in Na+ channels. Under whole-cell voltage-clamp conditions, we examined this single receptor hypothesis by studying the VTD phenotype in BTX-resistant muscle Na+ channels, microl-I433K, N434K, L437K, F1579K, and N1584K. Derived from point mutations at segments D1-S6 and D4-S6, these mutant Na+ channels are resistant to 5 microM BTX when expressed in human embryonic kidney cells. In contrast to the wild-type phenotype, VTD at 200 microM elicits little or no maintained current during a test pulse at +50 mV, and little or no "tail" current after the test pulse in all BTX-resistant mutant channels. Paradoxically, VTD retains its ability to inhibit the peak Na+ current in BTX-resistant mutant Na+ channels. To explain these mutant phenotypes, we propose a two-step binding reaction scheme. An initial VTD-binding interaction with the Na+ channel results in the inhibition of peak current amplitude, and a second binding reaction results in the trapping of VTD within the D1-S6 and D4-S6 domain interface. The failure of BTX-resistant mutant Na+ channels to trap VTD suggests that segments of D1-S6 and D4-S6 form a common receptor for VTD and BTX.

Batrachotoxins↗

PubMed2000

Block of human heart hH1 sodium channels by amitriptyline.

Amitriptyline is a tricyclic antidepressant used to treat major depression and various neuropathic pain syndromes. This drug also causes cardiac toxicity in patients with overdose. We characterized the tonic and use-dependent amitriptyline block of human cardiac (hH1) Na(+) channels expressed in human embryonic kidney cells under voltage-clamp conditions. Our results show that, near the therapeutic plasma concentration of 1 microM, amitriptyline is an effective use-dependent blocker of hH1 Na(+) channels during repetitive pulses (approximately 55% block at 5 Hz). The tonic block for resting and for inactivated hH1 channels by amitriptyline (0.1-100 microM) yielded IC(50) values (50% inhibitory concentration) of 24.8 +/- 2.0 (n = 9) and 0.58 +/- 0.03 microM (n = 7), respectively. Substitution of phenylalanine with lysine at the hH1-F1760 position, a putative binding site for local anesthetics, eliminates the use-dependent block by amitriptyline at 1 microM. The time constants of recovery from the inactivated-state amitriptyline block in hH1 wild-type and hH1-F1760K mutant channels are 8.0 +/- 0. 5 (n = 6) and 0.45 +/- 0.07 s (n = 6), respectively. A substitution at either hH1-F1760K or hH1-Y1767K significantly increases the IC(50) values for resting and inactivated states of amitriptyline, but the increase is much more pronounced with the hH1-F1760K mutation. Because these two residues were proposed to form a part of the local anesthetic binding site, we conclude that amitriptyline and local anesthetics interact with a common binding site. Furthermore, at therapeutic concentrations, the ability of amitriptyline to act as a potent use-dependent blocker of Na(+) channels may, in part, explain its analgesic actions.

Amitriptyline↗