Jfm. Leal et M. Barbancho, ALDEHYDE DEHYDROGENASE (ALDH) ACTIVITY IN DROSOPHILA-MELANOGASTER ADULTS - EVIDENCE FOR CYTOSOLIC LOCALIZATION, Insect biochemistry and molecular biology, 23(5), 1993, pp. 543-547
The subcellular localization of the aldehyde dehydrogenase activity fr
om the ALDH (EC 1.2.1.3) enzyme has been studied in nutritionally mani
pulated Drosophila melanogaster adults from a wild (LRC) and an ADH-nu
ll (bAdh(n4)) strain. ALDH activities from ALDH or ADH (EC 1.1.1.1) en
zymes were selectively inhibited by prefeeding respectively the flies
sucrose solutions supplemented with either cyanamide or acetone respec
tively. ALDH, ADH (as a cytosolic marker) and succinate dehydrogenase
(EC 1.3.9.1) (as a mitochondrial marker) activities were assayed in bo
th the mitochondrial and cytosolic fractions isolated from flies subje
cted to each treatment. Total ALDH activity in the cytosolic fraction
was found to be between five (ADH strain) and ten (ADH strain) times h
igher than that in the mitochondrial fraction. Prefeeding cyanamide re
sulted in a 64% (ADH strain) and a 90% (ADH strain) reduction of the c
ytosolic ALDH activity, whereas prefeeding acetone resulted in a 38% (
ADH strain) reduction of this activity. Prefeeding both cyanamide and
acetone resulted in a total inhibition of ALDH activity, which was als
o observed after an extended cyanamide treatment. In conclusion, our r
esults support that, contrary to what occurs in larvae, in adults the
ALDH activity from ALDH enzyme is mainly localized in the cytosolic fr
action: about 85% in ADH+ and 90% in ADH- strains. Although larvae and
adults use different ALDH activities to detoxify acetaldehyde (from A
DH and ALDH enzymes, respectively) both of them are cytosolic. Reasons
for these different uses are discussed in relation to the subcellular
localization of ALDH activity.