Excitatory amino acids increase glycogen phosphorylase activity in the rat spinal cord

1987 ◽  
Vol 73 (3) ◽  
pp. 209-214 ◽  
Author(s):  
Clifford J. Woolf
1991 ◽  
Vol 547 (2) ◽  
pp. 344-348 ◽  
Author(s):  
Danxia Liu ◽  
Wipawan Thangnipon ◽  
David J. McAdoo

It is possible to distinguish histochemically the relative amounts of the active and inactive forms of glycogen phosphorylase in the spinal cord (Chong & Woolf 1984). Both primary afferent cell bodies in dorsal root ganglia and the cells of the spinal cord normally maintain most of their glycogen phosphorylase in the inactive b form. Noxious mechanical thermal and chemical stimuli result, however, in an increase in the proportion of active glycogen phosphorylase a in the dorsal horn. Innocuous stimuli, in contrast, fail to modify the level of glycogen phosphorylase activity in the spinal cord. Stimulation of the sciatic nerve at a strength that activates unmyelinated afferents produces a pattern of activity change in the spinal cord which closely resembles that found with noxious stimuli while A-fibre stimulation has no demonstrable effect. The increase in glycogen phosphorylase activity can be demonstrated within 5 min of sciatic nerve stimulation and the pattern and level of the activity changes are suppressed by barbiturate anaesthesia.


1996 ◽  
Vol 270 (2) ◽  
pp. E328-E335 ◽  
Author(s):  
A. Chesley ◽  
G. J. Heigenhauser ◽  
L. L. Spriet

The purpose of this study was to examine the regulation (hormonal, substrate, and allosteric) of muscle glycogen phosphorylase (Phos) activity and glycogenolysis after short-term endurance training. Eight untrained males completed 6 days of cycle exercise (2 h/day) at 65% of maximal O2 uptake (Vo2max). Before and after training subjects cycled for 15 min at 80% of Vo2max, and muscle biopsies and blood samples were obtained at 0 and 30 s, 7.5 and 15 min, and 0, 5, 10, and 15 min of exercise. Vo2max was unchanged with training but citrate synthase (CS) activity increased by 20%. Muscle glycogenolysis was reduced by 42% during the 15-min exercise challenge following training (198.8 +/- 36.9 vs. 115.4 +/- 25.1 mmol/kg dry muscle), and plasma epinephrine was blunted at 15 min of exercise. The Phos a mole fraction was unaffected by training. Muscle phosphocreatine utilization and free Pi and AMP accumulations were reduced with training at 7.5 and 15 min of exercise. It is concluded that posttransformational control of Phos, exerted by reductions in substrate (free Pi) and allosteric modulator (free AMP) contents, is responsible for a blunted muscle glycogenolysis after 6 days of endurance training. The increase in CS activity suggests that the reduction of muscle glycogenolysis was due in part to an enhanced mitochondrial potential.


Sign in / Sign up

Export Citation Format

Share Document