Effect of L-Histidine on Human and Rat Jejunal Pyruvate Kinase Activity

1971 ◽  
Vol 49 (10) ◽  
pp. 1105-1116 ◽  
Author(s):  
Fred B. Stifel ◽  
Robert H. Herman

L-Histidine was found to be an in vitro activator of both human and rat jejunal pyruvate kinase activity and rat hepatic pyruvate kinase activity. Jejunal and hepatic pyruvate kinase activities were higher in rats fed a histidine-complete diet than a histidine-deficient diet. Feeding groups of rats successively larger doses of oral histidine produced a progressive increase in rat jejunal pyruvate kinase activity. An inverse relationship was seen between the pyruvate kinase activity without histidine added and the percent stimulation with histidine added in vitro.The histidine effect appears to be a ubiquitous one in the rat, since stimulation was observed in each of the seven tissues tested. The broad range of the histidine effect suggests that it may play a fundamental role in the regulation of glycolysis in mammalian systems.

2010 ◽  
Vol 24 (3) ◽  
pp. 1045-1051 ◽  
Author(s):  
Tatiana Wannmacher Lepper ◽  
Evandro Oliveira ◽  
Gustavo Duarte Waltereith Koch ◽  
Daiane Bolzan Berlese ◽  
Luciane Rosa Feksa

Blood ◽  
2017 ◽  
Vol 130 (11) ◽  
pp. 1347-1356 ◽  
Author(s):  
Charles Kung ◽  
Jeff Hixon ◽  
Penelope A. Kosinski ◽  
Giovanni Cianchetta ◽  
Gavin Histen ◽  
...  

Key Points AG-348 is a small-molecule allosteric activator of WT red cell pyruvate kinase as well as mutant enzymes associated with hemolytic anemia. Activity in vitro, in mice, and in red blood cells suggests it may address the underlying molecular pathology in PK deficiency patients.


1972 ◽  
Vol 128 (2) ◽  
pp. 415-420 ◽  
Author(s):  
J. Meli ◽  
F. L. Bygrave

1. The modification of pyruvate kinase activity in vitro was examined by altering the environmental [Mg2+]/[Ca2+] ratio with EDTA on the one hand and isolated rat liver mitochondria on the other. 2. Controlled additions of Ca2+ and EDTA caused pyruvate kinase activity to be alternately and rapidly switched on and off. 3. By being able to accumulate Ca2+ in preference to Mg2+ rat liver mitochondria were able to alter the [Mg2+]/[Ca2+] ratio in the vicinity of pyruvate kinase and thereby modify the activity of this enzyme. 4. The possible role of mitochondria in modifying pyruvate kinase and other ion-sensitive cytoplasmic enzyme activities is discussed.


1979 ◽  
Vol 180 (3) ◽  
pp. 523-531 ◽  
Author(s):  
R M Denton ◽  
N J Edgell ◽  
B J Bridges ◽  
G P Poole

1. Evidence is presented that exposure of epididymal fat-pads from fed rats to insulin leads to a marked diminution in the Km for phosphoenolpyruvate of pyruvate kinase. Effects of insulin may be readily demonstrated in experiments both in vivo and in vitro and are not secondary to the activation by the hormone of glucose transport. No effect of insulin is apparent in tissues from 48 h-starved animals. 2. The mechanism of the effect of insulin on pyruvate kinase was not established. The observed changes in Km do not appear to be the result of alterations in the amounts of bound effectors such as fructose 1,6-bisphosphate and alanine. Rather, as the effect persists in incubated extracts, it appears that a change in the degree of phosphorylation or some other covalent modification of the enzyme may be involved.


Diabetes ◽  
1983 ◽  
Vol 32 (11) ◽  
pp. 1017-1022 ◽  
Author(s):  
A. Camagna ◽  
R. De Pirro ◽  
L. Tardella ◽  
L. Rossetti ◽  
R. Lauro ◽  
...  

Diabetes ◽  
1983 ◽  
Vol 32 (11) ◽  
pp. 1017-1022 ◽  
Author(s):  
A. Camagna ◽  
R. D. Pirro ◽  
L. Tardella ◽  
L. Rossetti ◽  
R. Lauro ◽  
...  

2004 ◽  
Vol 3 (3) ◽  
pp. 152-155 ◽  
Author(s):  
Hacer Yapicioglu ◽  
Mehmet Satar ◽  
Nejat Narli ◽  
Levent Kayrin ◽  
Ercan Tutak

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