The detection and characterization of buried resonant targets by iterative, single‐channel time reversal

2008 ◽  
Vol 123 (5) ◽  
pp. 3185-3185
Author(s):  
Ronald A. Roy ◽  
Zachary J. Waters ◽  
Benjamin R. Dzikowicz ◽  
R. Glynn Holt
Keyword(s):  
Time Reversal ◽  
Single Channel

Laboratory investigations of the detection and characterization of buried targets by iterative, single‐channel time reversal

2008 ◽  
Vol 123 (5) ◽  
pp. 3599-3599
Author(s):  
Zachary J. Waters ◽  
Benjamin R. Dzikowicz ◽  
R. Glynn Holt ◽  
Ronald A. Roy
Keyword(s):  
Time Reversal ◽  
Single Channel ◽  
Laboratory Investigations

SIMULATION OF SINGLE CHANNEL BIOLOGICAL TISSUE SPECTROSCOPY USING COMSOL MULTIPHYSICS

2015 ◽  
Vol 77 (28) ◽  
Author(s):  
Azmi Abou Basaif ◽  
Nashrul Fazli Mohd Nasir ◽  
Zulkarnay Zakaria ◽  
Ibrahim Balkhis ◽  
Shazwani Sarkawi ◽  
...  
Keyword(s):  
Magnetic Induction ◽  
Biological Tissue ◽  
Single Channel ◽  
Medical Condition ◽  
Biological Tissues ◽  
Comsol Multiphysics ◽  
Accurate Information ◽  
Tissue Properties ◽  
Biological Soft Tissue

The enhanced ability to detect accurate location and measure the depth of a   metal inside a biological tissue is very useful in the assessment of medical condition and treatment. This manuscript proposed a solution via the measurement of the tissue properties using magnetic induction spectroscopy (MIS) method to describe the characterization of biological soft tissue. The objective of this study is to explore the viability of locating embedded metal inside a biological tissue by measuring the differences the biological tissue electrical properties using principle of Magnetic Induction Spectroscopy (MIS). Simulation is done using COMSOL Multiphysics software for accurate information on the involved parameters for both metal and biological tissues. Simulation has confirmed that MIS capable of detecting and locate embedded metal inside a biological tissue.

ATP-activated chloride channel inhibited by an antibody to P glycoprotein

1994 ◽  
Vol 267 (4) ◽  
pp. C1095-C1102 ◽  
Author(s):  
J. J. Zhang ◽  
T. J. Jacob
Keyword(s):  
Single Channel ◽  
Disulfonic Acid ◽  
Fiber Cells ◽  
Cl Channel ◽  
P Glycoprotein ◽  
Voltage Curve ◽  
Current Voltage ◽  
Single Channel Activity ◽  
Current Voltage Curve

In this report, we present the characteristics of a Cl- channel found in lens fiber cells. The single channel has a conductance of 17 pS, a linear current-voltage curve, is activated by ATP or strong depolarization and is blocked by verapamil, quinidine, 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid, 5-nitro-2-(3- phenylpropylamino)benzoate, dideoxyforskolin, and tamoxifen. These properties are similar to those reported for a volume-activated Cl- channel associated with the multidrug resistance (MDR) gene product, P glycoprotein (24). Confirming this connection, we demonstrate that our lens Cl- channel is inhibited by an antibody to P glycoprotein. The data we present here may, therefore, be the first characterization of the single channel activity of the Cl- channel associated with P glycoprotein.

Characterization of a newly found stretch-activated KCa,ATP channel in cultured chick ventricular myocytes

1999 ◽  
Vol 276 (6) ◽  
pp. H1827-H1838 ◽  
Author(s):  
Takashi Kawakubo ◽  
Keiji Naruse ◽  
Tatsuaki Matsubara ◽  
Nigishi Hotta ◽  
Masahiro Sokabe
Keyword(s):  
Single Channel ◽  
Ventricular Myocytes ◽  
Heart Cells ◽  
Patch Clamp Technique ◽  
Selective Channel ◽  
New Type ◽  
Inside Out ◽  
Ion Selectivities ◽  
Channel Type

With the use of the patch-clamp technique, five kinds of stretch-activated (SA) ion channels were identified on the basis of their single-channel conductances and ion selectivities in cultured chick ventricular myocytes. Because a high-conductance K+-selective channel predominated among these channels, we concentrated on characterizing its properties mostly using excised inside-out patches. With 145 mM KCl solution in the pipette and the bath, the channel had a conductance of 199.8 ± 8.2 pS ( n = 22). The ion selectivities among K+, Na+, Ca2+, and Cl− as estimated from their permeability ratios were P Na/ P K= 0.03, P Ca/ P K= 0.025, and P Cl/ P K= 0.026. The probability of the channel being open (Po) increased with the Ca2+concentration in the bath ([Ca2+]b; dissociation constant K d = 0.51 μM at +30 mV) and membrane potential (voltage at half-maximal Po= 39.4 mV at 0.35 μM [Ca2+]b). The channel was blocked by gadolinium, tetraethylammonium, and charybdotoxin from the extracellular surface and, consequently, was identified as a Ca2+-activated K+(KCa) channel type. The channel was also reversibly activated by ATP applied to the intracellular surface ( K d = 0.74 mM at 0.10 μM [Ca2+]bat +30 mV). From these data taken together, we concluded that the channel is a new type of KCachannel that could be designated as an “SA KCa,ATP channel.” To our knowledge, this is the first report of KCa channel in heart cells.

Characterization of the ryanodine receptor/channel of invertebrate muscle

1998 ◽  
Vol 274 (2) ◽  
pp. R494-R502 ◽  
Author(s):  
Kerry E. Quinn ◽  
Loriana Castellani ◽  
Karol Ondrias ◽  
Barbara E. Ehrlich
Keyword(s):  
Ryanodine Receptor ◽  
Single Channel ◽  
Microscopic Analysis ◽  
Ruthenium Red ◽  
Electron Microscopic ◽  
Release Channel ◽  
Single Channel Currents ◽  
Channel Currents ◽  
Bell Shaped Curve

Electron-microscopic analysis was used to show that invertebrate muscle has feetlike structures on the sarcoplasmic reticulum (SR) displaying the typical four-subunit appearance of the calcium (Ca2+) release channel/ryanodine receptor (RyR) observed in vertebrate skeletal muscle (K. E. Loesser, L. Castellani, and C. Franzini-Armstrong. J. Muscle Res. Cell Motil. 13: 161–173, 1992). SR vesicles from invertebrate muscle exhibited specific ryanodine binding and single channel currents that were activated by Ca2+, caffeine, and ATP and inhibited by ruthenium red. The single channel conductance of this invertebrate RyR was lower than that of the vertebrate RyR (49 and 102 pS, respectively). Activation of lobster and scallop SR Ca2+ release channel, in response to cytoplasmic Ca2+ (1 nM–10 mM), reflected a bell-shaped curve, as is found with the mammalian RyR. In contrast to a previous report (J.-H. Seok, L. Xu, N. R. Kramarcy, R. Sealock, and G. Meissner. J. Biol. Chem. 267: 15893–15901, 1992), our results show that regulation of the invertebrate and vertebrate RyRs is quite similar and suggest remarkably similar paths in these diverse organisms.

CFTR in K562 human leukemic cells

2003 ◽  
Vol 285 (2) ◽  
pp. C480-C488 ◽  
Author(s):  
Yanina A. Assef ◽  
Alicia E. Damiano ◽  
Elsa Zotta ◽  
Cristina Ibarra ◽  
Basilio A. Kotsias
Keyword(s):  
Single Channel ◽  
Functional Characterization ◽  
Leukemic Cells ◽  
Cftr Gene ◽  
Human Leukemia ◽  
Selectivity Ratio ◽  
Open Probability ◽  
Selective Channel ◽  
Human Leukemic Cells

In this study, the expression and functional characterization of CFTR (cystic fibrosis transmembrane regulator) was determined in K562 chronic human leukemia cells. Expression of the CFTR gene product was determined by RT-PCR and confirmed by immunohistochemistry and Western blot analysis. Functional characterization of CFTR Cl- channel activity was conducted with patch-clamp techniques. Forskolin, an adenylyl cyclase activator, induced an anion-selective channel with a linear current-voltage relationship and a single-channel conductance of 11 pS. This cAMP-activated channel had a Pgluconate/PCl or PF/PCl perm-selectivity ratio of 0.35 and 0.30, respectively, and was inhibited by the CFTR blocker glibenclamide and the anti-CFTR antibody MAb 13-1, when added to the cytoplasmatic side of the patch. Glibenclamide decreased the open probability increasing the frequency of open-to-closed transitions. Addition of 200 μM DIDS caused an irreversible block of the channels when added to the cytosolic side of inside-out patches. These and other observations indicate a widespread distribution of CFTR gene expression and suggest that this channel protein may function in most human cells to help maintain cellular homeostasis.

Identification of a resonant target buried in sediment using iterative, single channel, time reversal

2007 ◽  
Vol 122 (5) ◽  
pp. 3023
Author(s):  
Zachary J. Waters ◽  
R. Glynn Holt ◽  
Ronald A. Roy ◽  
Benjamin R. Dzikowicz
Keyword(s):  
Time Reversal ◽  
Single Channel
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