B. Fernandez-cuartero et al., Delta aminolevulinate dehydratase (ALA-D) activity in human and experimental diabetes mellitus, INT J BIO C, 31(3-4), 1999, pp. 479-488
Citations number
61
Categorie Soggetti
Biochemistry & Biophysics
Journal title
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
The haem pathway is impaired in porphyrias and a frequent coexistence of di
abetes mellitus and porphyria disease has been reported.
We have therefore decided to investigate delta-aminolevulinate dehydratase,
one of the more sensitive enzymes in the haem pathway: in both human diabe
tic patients and diabetic rats. We have studied 131 diabetes mellitus patie
nts, 32 insulin dependent and 99 non-insulin dependent. The latter group wa
s further subdivided according to treatment: diet alone (n = 24), diet plus
oral hypoglycemic agents (n = 28) and diet plus insulin (n = 47). We have
also performed similar studies in the rat model of diabetes mellitus, induc
ed in 11 Wistar rats by streptozotocin. Control groups of both humans and a
nimals were used.
Erythrocytic aminolevulinate dehydratase activity was reduced in both insul
in dependent and non-insulin dependent diabetic patients as compared to the
ir controls (p < 0.001). This activity was only partially restored by addit
ion of zinc and thiols to the incubation media. In insulin-dependent diabet
es mellitus, reduction of enzyme activity was related to the glycosilated h
emoglobin concentration (p < 0.05) and in non-insulin dependent diabetes me
llitus to the glycemia (p < 0.01). In the diabetic rat, aminolevulinate deh
ydratase activity was diminished on both erythrocytes (p < 0.01) and hepati
c tissue (p < 0.01) when compared to the control group.
The decrease in activity of erythrocyte aminolevulinate dehydratase observe
d in diabetic patients, may represent an additional and useful parameter fo
r the assessment of the severity of carbohydrate metabolism impairment. (C)
1999 Elsevier Science Ltd. All rights reserved.