C. Patrini et al., THIAMINE PYROPHOSPHATE-DEPENDENT AND THIAMINE METABOLIZING ENZYMES INTHE DEAFFERENTED CEREBELLUM AND IN THE INTACT CEREBRAL-CORTEX OF RAT, Metabolic brain disease, 13(1), 1998, pp. 21-27
The effects of chemical (CD) and surgical (SD) deafferentation of the
cerebellum on thiamine pyrophosphate (ThPP)-dependent enzymes (transke
tolase, TK; pyruvate-, PDH, and alpha-ketoglutarate, alpha KGDH, dehyd
rogenases) and thiamine (Th) metabolizing enzymes (thiamine pyrophosph
okinase, ThPK; thiamine mono-, ThMPase, and pyrophosphatases, ThPPase)
were evaluated in vitro in rats in steady state conditions. The enzym
es were also determined in the intact cerebral cortex of the same anim
als. CD was carried out by i.p. injection of 3-acetylpyridine, followe
d by harmaline and niacinamide. SD was carried out by complete dissect
ion of the peduncles of the left cerebellar hemisphere. Chemical and s
urgical cerebellar deafferentations significantly lowered the contents
of both Th-metabolizing and ThPP-dependent enzymes in the cerebellum
without modifying those of the cerebral cortex. ThPK and TK, which are
particularly concentrated in neurons, were the most affected enzymes.
The decrease in ThPP-dependent enzymes shown here is associated with
the slowing down of the Th phosphorylation-dephosphorylation cycle and
with no modification in the ThPP content in the cerebellum, both of w
hich were found in a previous study. Cerebellar deafferentation seems
to only affect the apoenzyme moiety of the enzymes.