In vitro Effects of Short-Chain Aliphatic Alcohols, Benzyl Alcohol and Chlorpromazine on the Transport of Precursors of Monoamines across the Human Erythrocyte Membrane

1987 ◽  
Vol 18 (2) ◽  
pp. 60-67 ◽  
Author(s):  
J. Widmer ◽  
Y. Raffin ◽  
J.-M. Gaillard ◽  
T. Tissot
2017 ◽  
Vol 483 (1) ◽  
pp. 528-533 ◽  
Author(s):  
Pablo Zambrano ◽  
Mario Suwalsky ◽  
Fernando Villena ◽  
Malgorzata Jemiola-Rzeminska ◽  
Kazimierz Strzalka

1990 ◽  
Vol 268 (3) ◽  
pp. 661-667 ◽  
Author(s):  
P J Bilan ◽  
A Klip

Glycation of human erythrocyte membrane proteins was induced by incubation in vitro with high concentrations (80 mM or 200 mM) of D-glucose for 3 or 6 days. The extent of glycation was quantified from the covalent incorporation of 3H by reduction of the glucose glycation products with NaB3H4. For membranes incubated for 3 days with 80 mM-D-glucose, glycation in vitro of Band 4.5 (containing the glucose transporter) was equivalent to 0.11 mol of glucose/mol of glucose transporter, compared with 3H labelling in 3-day-incubated control membranes of 0.055 mol of glucose/mol of glucose transporter. In membranes incubated for 6 days with 200 mM-D-glucose, glycation increased to 0.21 mol of glucose/mol of glucose transporter, whereas the controls without glucose had 0.11 mol of glucose/mol of glucose transporter. Glycation in vitro was accompanied by a fall in the Bmax of binding of [3H]cytochalasin B (a competitive inhibitor of glucose transport), without any change in the binding affinity. The data suggest that glycated glucose transporters have decreased ability to bind cytochalasin B. It is proposed that glycation can alter glucose transporter activity.


1992 ◽  
Vol 205 (1) ◽  
pp. 155-162 ◽  
Author(s):  
Francois BASSE ◽  
Josette SAINTE-MARIE ◽  
Luc MAURIN ◽  
Alain BIENVENUE

Sign in / Sign up

Export Citation Format

Share Document