scholarly journals Differential effects of glucose and fructose on hexose metabolism in dog spermatozoa

Reproduction ◽  
2002 ◽  
pp. 579-591 ◽  
Author(s):  
T Rigau ◽  
M Rivera ◽  
MJ Palomo ◽  
JM Fernandez-Novell ◽  
T Mogas ◽  
...  

Incubation of dog spermatozoa with 10 mmol l(-1) glucose or fructose rapidly increased the intracellular content of glucose 6-phosphate and fructose 6-phosphate, although the effect of fructose was greater. These effects were correlated with increases in ATP, ribose 5-phosphate and glycogen contents, and in the rates of formation of L-lactate and CO2. In all cases, except for ATP and glycogen, the effect of fructose was greater than that of glucose. The total hexokinase activity of the crude extracts of dog spermatozoa was more sensitive to fructose than to glucose at lower concentrations (0.1-3.0 mmol l(-1)). Both monosaccharides induced a fast and intense increase in the overall tyrosine phosphorylation of dog spermatozoa, although their specific induced-phosphorylation patterns differed slightly. Glut 3 and Glut 5 hexose transporters were the main hexose transporters in dog spermatozoa; however, other possible SGLT family-related hexose transporters were also localized. These data indicate that, at concentrations from 1 mmol l(-1) to 10 mmol l(-1), fructose has a stronger effect than glucose on hexose metabolism of dog spermatozoa. These differences appear to be related to variations in the sensitivity of hexokinase activity. Moreover, the differential hexose metabolism induced by the two sugars had distinct effects on the function of dog spermatozoa, as revealed by the diverse patterns of tyrosine phosphorylation.

2002 ◽  
Vol 82 (4) ◽  
pp. 848-856 ◽  
Author(s):  
James W. Gurd ◽  
N. Bissoon ◽  
P. W. Beesley ◽  
Takanobu Nakazawa ◽  
Tadashi Yamamoto ◽  
...  

Author(s):  
Krishan K. Arora ◽  
Glenn L. Decker ◽  
Peter L. Pedersen

Hexokinase (ATP: D-hexose 6-phophotransferase EC 2.7.1.1) is the first enzyme of the glycolytic pathway which commits glucose to catabolism by catalyzing the phosphorylation of glucose with ATP. Previous studies have shown diat hexokinase activity is markedly elevated in rapidly growing tumor cells exhibiting high glucose catabolic rates. A large fraction (50-80%) of this enzyme activity is bound to the mitochondrial fraction (1,2) where it has preferred access to ATP (3). In contrast,the hexokinase activity of normal tissues is quite low, with one exception being brain which is a glucose-utilizing tissue (4). Biochemical evidence involving rigorous subfractionation studies have revealed striking differences between the subcellular distribution of hexokinase in normal and tumor cells [See review by Arora et al (4)].In the present report, we have utilized immunogold labeling techniques to evaluate die subcellular localization of hexokinase in highly glycolytic AS-30D hepatoma cells and in the tissue of its origin, i.e., rat liver.


2001 ◽  
Vol 120 (5) ◽  
pp. A215-A215
Author(s):  
P BARDHAN ◽  
S HUQ ◽  
S SARKER ◽  
D MAHALANABIS ◽  
K GYR

2001 ◽  
Vol 120 (5) ◽  
pp. A168-A168
Author(s):  
T KAIHARA ◽  
T KUSAKA ◽  
H KAWAMATA ◽  
Y ODA ◽  
J IMURA ◽  
...  

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