Slow diffusion of Ca2+ in the rat's hippocampus

1981 ◽  
Vol 59 (9) ◽  
pp. 1022-1025 ◽  
Author(s):  
M. E. Morris ◽  
K. Krnjević

Ca2+-sensitive microelectrodes, attached to CaCl2-containing micropipettes, were inserted into the dorsal hippocampus of rats under urethane. When Ca2+ was released iontophoretically, the amplitude and time course of the resultant increase in extracellular Ca2+ concentration could be fitted to a simple diffusion model, but the apparent diffusion coefficient of Ca2+ was only about 1/100 of its value in water, possibly because of reversible Ca2+ binding to hippocampal tissue. A further anomaly was a very low transport number (<0.01) for the release of Ca2+ from microelectrodes in vivo.

2014 ◽  
Vol 74 (3) ◽  
pp. 622-633 ◽  
Author(s):  
Bertram L. Koelsch ◽  
Galen D. Reed ◽  
Kayvan R. Keshari ◽  
Myriam M. Chaumeil ◽  
Robert Bok ◽  
...  

2012 ◽  
Vol 39 (8) ◽  
pp. 4832-4839 ◽  
Author(s):  
Moti Freiman ◽  
Stephan D. Voss ◽  
Robert V. Mulkern ◽  
Jeannette M. Perez-Rossello ◽  
Michael J. Callahan ◽  
...  

Neurology ◽  
1997 ◽  
Vol 49 (1) ◽  
pp. 113-119 ◽  
Author(s):  
G. Schlaug ◽  
B. Siewert ◽  
A. Benfield ◽  
R. R. Edelman ◽  
S. Warach

1999 ◽  
Vol 181 (1) ◽  
pp. 197-203 ◽  
Author(s):  
Michael B. Elowitz ◽  
Michael G. Surette ◽  
Pierre-Etienne Wolf ◽  
Jeffry B. Stock ◽  
Stanislas Leibler

ABSTRACT The rate of protein diffusion in bacterial cytoplasm may constrain a variety of cellular functions and limit the rates of many biochemical reactions in vivo. In this paper, we report noninvasive measurements of the apparent diffusion coefficient of green fluorescent protein (GFP) in the cytoplasm of Escherichia coli. These measurements were made in two ways: by photobleaching of GFP fluorescence and by photoactivation of a red-emitting fluorescent state of GFP (M. B. Elowitz, M. G. Surette, P. E. Wolf, J. Stock, and S. Leibler, Curr. Biol. 7:809–812, 1997). The apparent diffusion coefficient,Da , of GFP in E. coli DH5α was found to be 7.7 ± 2.5 μm2/s. A 72-kDa fusion protein composed of GFP and a cytoplasmically localized maltose binding protein domain moves more slowly, with Da of 2.5 ± 0.6 μm2/s. In addition, GFP mobility can depend strongly on at least two factors: first,Da is reduced to 3.6 ± 0.7 μm2/s at high levels of GFP expression; second, the addition to GFP of a small tag consisting of six histidine residues reduces Da to 4.0 ± 2.0 μm2/s. Thus, a single effective cytoplasmic viscosity cannot explain all values of Da reported here. These measurements have implications for the understanding of intracellular biochemical networks.


Radiology ◽  
2001 ◽  
Vol 221 (1) ◽  
pp. 27-34 ◽  
Author(s):  
William A. Copen ◽  
Lee H. Schwamm ◽  
R. Gilberto González ◽  
Ona Wu ◽  
Carla B. Harmath ◽  
...  

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