Adenosine transport systems on dissociated brain cells from mouse, guinea-pig, and rat

1990 ◽  
Vol 15 (9) ◽  
pp. 911-915 ◽  
Author(s):  
M. E. Johnston ◽  
J. D. Geiger
Life Sciences ◽  
1996 ◽  
Vol 59 (5-6) ◽  
pp. 435-449 ◽  
Author(s):  
Henrike Hartmann ◽  
Anne Eckert ◽  
Karsten Velbinger ◽  
Michael Rewsin ◽  
Walter E. Müller

1979 ◽  
Vol 46 (1-2) ◽  
pp. 117-121 ◽  
Author(s):  
Z. Janka ◽  
I. Szentistv�nyi ◽  
F. Joo ◽  
A. Juh�sz ◽  
�. Riman�czy

1981 ◽  
Vol 241 (3) ◽  
pp. C106-C112 ◽  
Author(s):  
B. M. Eaton ◽  
D. L. Yudilevich

Unidirectional uptake of eighteen amino acids into the syncytiotrophoblast was measured from both the maternal and fetal circulations of isolated dually perfused guinea pig placentas using a single-circulation, paired-tracer dilution technique. A bolus containing a tritiated amino acid and L-[14C]glucose (extracellular marker) was injected intra-arterially into one circulation, and both venous outflows were sequentially sampled. The maximal cellular uptake (Umax) on the injection side was determined from (1-[3H]/[14C]) values and used to calculate the unidirectional influx. Umax values for neutral and basic amino acids ranged between 15 and 58% and were similar on both sides of the trophoblast. Uptake of the acidic amino acids and taurine was minimal. Amino acid influx from either circulation was followed by rapid tracer backflux and transplacental transfer. Tracer efflux was asymmetric and preferentially directed towards the fetal side. It is suggested that amino acid transport systems are present on both surfaces of the placenta and that net transfer from mother to fetus is the result of asymmetric efflux from the trophoblast.


1957 ◽  
Vol 190 (1) ◽  
pp. 157-162 ◽  
Author(s):  
S. A. Kaplan ◽  
S. N. Stein

Slices of guinea pig brain cortex were suspended in a medium containing inorganic ions (in concentrations similar to those present in plasma), glucose and glutamate. They were shaken for 90 minutes at 37°C in oxygen, the partial pressure of which was varied from 1 to 11 atm. absolute. Raising the pressure above 4 atm. absolute resulted in the slices losing considerable quantities of potassium. At 6 atm. absolute the slices accumulated considerably less glutamic acid than they did at 1 atm. These findings suggest that brain cells are unable to maintain their normal concentrations of these two substances when exposed to oxygen at high pressure and suggest a possible mechanism for the origin of the disturbances of function in the central nervous system of animals exposed to high pressures of oxygen.


1989 ◽  
Vol 263 (3) ◽  
pp. 957-960 ◽  
Author(s):  
W P Gati ◽  
L Dagnino ◽  
A R P Paterson

In mediating the entry of adenosine into mouse erythrocytes and mouse leukaemia L1210 cells, nucleoside transport systems were stereoselective, showing a marked preference for the D-enantiomer of adenosine (D-Ado). Inward zero-trans fluxes of the mirror-image isomer, L-adenosine (L-Ado), in those cells were slow relative to those of D-Ado. Contributing to L-Ado fluxes in both cell types were (i) a transporter-mediated process of high nitrobenzylthioinosine-sensitivity and (ii) simple diffusion.


1971 ◽  
Vol 49 (1) ◽  
pp. 150-158 ◽  
Author(s):  
J. Meldolesi ◽  
J. D. Jamieson ◽  
G. E. Palade

A comparative study of the enzymic activities of membrane fractions derived from guinea pig pancreatic homogenates has yielded the following results: Rough microsomal membranes (derived from the rough ER) have the reductase activities of the two microsomal electron transport systems but lack enzyme activities of Golgi-type (TPPase) and plasmalemmal-type (5'-nucleotidase, ß-leucyl naphthylamidase, Mg-ATPase). Smooth microsomal membranes (derived primarily from the Golgi complex), zymogen granule membranes, and plasmalemmal fractions possess overlapping enzyme activities of plasmalemmal type, in different relative concentrations for each fraction. In addition, the smooth microsomal membranes exhibit TPPase and ADPase activity and share with rough microsomes the reductase activities of the two electron transport chains. Taken together with recent data on the lipid composition of the same fractions (2), these results indicate that the membranes of the pancreatic exocrine cell are chemically and functionally distinct, and hence do not mix with one another during the transport of secretory products.


1980 ◽  
Vol 36 (9) ◽  
pp. 1071-1072 ◽  
Author(s):  
Z. Janka ◽  
I. Szentistványi ◽  
A. Juhász ◽  
A. Rimanóczy

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