J. Folbergrova, GLYCOGEN-PHOSPHORYLASE ACTIVITY IN THE CEREBRAL-CORTEX OF RATS DURINGDEVELOPMENT - EFFECT OF HOMOCYSTEINE-INDUCED SEIZURES, Brain research, 694(1-2), 1995, pp. 128-132
The aim of the present study was to examine the total, as well as the
active form of glycogen phosphorylase in the rat cerebral cortex durin
g development, and to assess the response of the enzyme to induced sei
zures. Seizures were induced in 7-, 12- and 18-day-old male Wistar rat
s by i.p. administration of DL-homocysteine thiolactone HCl. Total gly
cogen phosphorylase activity increased from 54.76 +/- 2.33 to 181.14 /- 5.79 mu mol/g/h and phosphorylase a from 3.45 +/- 0.45 to 63.73 +/-
1.41 mu mol/g/h, from postnatal day 7 to 18, respectively. In 7-day-o
ld pups phosphorylase a corresponded to only 6% of total activity. At
the onset of seizures a marked rise (34-90%) in active phosphorylase o
ccurred in all age groups. Thus, in the brains of immature animals a r
apid conversion of phosphorylase b to a can occur in response to incre
ased cellular activity. However, in 7-day-old rats, in spite of marked
activation, phosphorylase a remained very low (6.0 +/- 0.42 mu mol/g/
h) and can thus explain the slow onset of glycogenolysis in this age g
roup. Cyclic AMP levels remained unchanged at the onset of seizures in
7- and 12-day-old pups, and only a mild (+25%) rise was observed in 1
8-day-old rats. The marked increase of phosphorylase a in 7- and 12-da
y-old rats thus occurred in the presence of unchanged levels of cAMP,
suggesting the involvement of cAMP-independent mechanism of activation
, in which Ca2+ most probably plays a role.