Mechanism of Stimulation of the Hexose Monophosphate Shunt of Erythrocytes by Pyruvate

Enzyme ◽  
1974 ◽  
Vol 18 (1-2) ◽  
pp. 7-18 ◽  
Author(s):  
Ernest Beutler ◽  
Enriqueta Guinto
Blood ◽  
1975 ◽  
Vol 45 (1) ◽  
pp. 49-54 ◽  
Author(s):  
AL Jr Sagone ◽  
SP Balcerzak ◽  
EN Metz

Abstract In this investigation, we studied the importance of cellular glutathione (GSH) in the hexose monophosphate shunt (HMPS) activity of unstimulated human erythrocytes and the mechanism by which pyruvate stimulates the HMPS. The rate of HMPS activity was measured by the production of radioactive CO2 from 14C-1-glucose or 14C-1-ribose using a vibrating reed electrometer and ionization chamber. HMPS activity was not significantly impaired by N-ethylmaleimide (NEM) in concentrations which bound all red cell GSH. Red cells incubated under carbon monoxide (CO), an experimental condition which eliminates peroxide production, still had HMPS activity which was 44% of the value under air. Pyruvate stimulation of the HMPS was unaffected by doses of NEM which bound all cellular GSH or by incubation under CO. These data indicated that pyruvate stimulation of the HMPS occurs by pathways which do not involve peroxide formation, GSH, or oxygen. This study indicates that sulfhydrylblockade of GSH does not necessarily inhibit HMPS activity and that HMPS activity in red cells may respond to reactions not linked directly to glutathione reduction.


1981 ◽  
Vol 178 (3) ◽  
pp. 257-262 ◽  
Author(s):  
Franco Patrone ◽  
Franco Dallegri ◽  
Anna Maria Maggi ◽  
Claudio Rapetto ◽  
Gianfranco Lanzi

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