J. Rasschaert et al., IMPAIRED FAD-GLYCEROPHOSPHATE DEHYDROGENASE-ACTIVITY IN ISLET AND LIVER HOMOGENATES OF FA FA RATS/, Molecular and cellular biochemistry, 135(2), 1994, pp. 137-141
The mitochondrial FAD-linked enzyme glycerophosphate dehydrogenase pla
ys a key role in the pancreatic B-cell glucose sensing device. In the
present study, the activity of this enzyme was examined in islets of f
a/fa rats in which inherited diabetes mellitus is associated with obes
ity, hyperinsulinism and severe insulin resistance. The specific activ
ity of both FAD-linked glycerophosphate dehydrogenase and glutamate de
hydrogenase were decreased in islet and liver homogenates prepared fro
m fa/fa, as compared to Fa/Fa, rats, this coinciding with a low ratio
between glutamate-oxalacetate and glutamate-pyruvate transaminase acti
vity in both islet and liver extracts, islet hyperplasia, hyperinsulin
emia and hepatic steatosis in the hyperglycemic fa/fa rats. It is spec
ulated that a low activity of FAD-linked glycerophosphate dehydrogenas
e in the pancreatic B-cell may participate to the perturbation of gluc
ose homeostasis in fa/fa rats, like in other animal models of non-insu
lin-dependent diabetes mellitus.