Metabolism of biogenetic amines in drosophila nervous tissue

Dewhurst, Susan; Croker, Susan G.; Ikeda, Kenro; McCaman, Richard E.

doi:10.1016/0305-0491(72)90241-6

Cited by 96 publications

(61 citation statements)

References 16 publications

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“…A precise interpretation of which post-transcriptional step or steps participate in regulating gene expression will require knowledge of the cell types in which the various RNA species are located. During postembryonic development, most Ddc enzyme activity is found in the hypoderm, with small but significant amounts also found in nervous tissue (7,18). Though this has not been demonstrated directly for Ddc expression during embryogenesis, we expect a similar situation to prevail.…”

Section: Methodsmentioning

confidence: 83%

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High levels of intron-containing RNAs are associated with expression of the Drosophila DOPA decarboxylase gene.

Beall¹,

Hirsh²

1984

Mol. Cell. Biol.

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We have examined the structure and expression during embryonic development of the Drosophila DOPA decarboxylase gene, Ddc. The Ddc gene is transcribed to make at least five different size classes of RNA. These RNA species first appear late in embryogenesis, coincident with induction of Dde enzyme activity. The most abundant and smallest RNA appears to be Ddc mRNA. The sequences encoding this RNA are split by two intervening sequences. Each of the larger RNA species contains some or all of the intervening sequences. We have noted two unusual features of Ddc expression during embryogenesis. First, the intervening-sequencecontaining RNAs are present as 20% or more of the polyadenylated Dde RNA molecules, an exceptionally high proportion. Second, these RNAs do not disappear as rapidly as Ddc mRNA after Ddc enzyme activity reaches fully induced levels. These observations indicate slow rates of RNA processing relative to mRNA half-life and suggest that post-transcriptional steps participate in regulating Ddc expression. Although four of the five RNA species were detected at multiple developmental stages during which Dde is expressed, one was found uniquely during embryogenesis. This RNA differs from Ddc mRNA in length and in time of expression during embryogenesis but is transcribed in the same orientation and from the same genomic sequences as the Ddc primary transcript.

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Section: Methodsmentioning

confidence: 83%

“…The product of this unique gene, the enzyme DOPA decarboxylase, forms metabolites used in two separate processes: cuticle hardening and pigmentation, and neural function (7,18). The majority of Ddc enzyme activity during development is associated with cuticle formation (16,20).…”

mentioning

confidence: 99%

High levels of intron-containing RNAs are associated with expression of the Drosophila DOPA decarboxylase gene.

Beall¹,

Hirsh²

1984

Mol. Cell. Biol.

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“…Fax (41) (61) 267 22 08. ied e.g. in Drosophila melanogaster by Finocchiario et al [12]), aaNAT plays important roles in the sclerotization of the insect cuticle [13] and the catabolism of neurotransmitters [14][15][16][17]. In the present study, we have purified aaNAT from D. melanogaster, using tryptamine acetylation as functional enzyme assay.…”

Section: Introductionmentioning

confidence: 93%

Isolation and characterization of an arylalkylamine N‐acetyltransferase from Drosophila melanogaster

1995

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The enzyme arylalkylamine N-acetyltransferase (aaNAT) catalyzes the rate-limiting step in melatonin formation in the vertebrate pineal gland. Numerous attempts to purify this highly unstable enzyme from vertebrates have been unsuccessful. Here, we report the purification of an aaNAT enzyme from Drosophila melanogaster, using a radioenzymatic activity assay and column chromatography. The isolated 29.5-kDa protein acetylates tryptamine, dopamine and serotonin with affinities of 0.89 to 0.97 mM, respectively. This suggests that the identified aaNAT may be involved in melatonin synthesis and sclerotization as well as in neurotransmitter catabolism in insects.

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“…However, it is not known if aaNAT activity and melatonin are subject to diurnal variation in Drosophila melanogaster. aaNAT activity has been described in several insect species (14)(15)(16)(17)(18), including D. melanogaster (2,19), but none of these enzymes could be purified to derive antibodies or sufficient internal sequence information for cloning. We have purified an aaNAT from D. melanogaster using tryptamine acetylation as a functional enzyme assay (20).…”

mentioning

confidence: 99%

Cloning of an arylalkylamine N-acetyltransferase (aaNAT1) from Drosophila melanogaster expressed in the nervous system and the gut.

Hintermann

Grieder

Amherd

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

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In insects, neurotransmitter catabolism, melatonin precursor formation, and sclerotization involve arylalkylamine N-acetyltransferase (aaNAT, EC 2.3.1.87) activity. It is not known if one or multiple aaNAT enzymes are responsible for these activities. We recently have purified an aaNAT from Drosophila melanogaster. Here, we report the cloning of the corresponding aaNAT cDNA (aaNAT1) that upon COS cell expression acetylates dopamine, tryptamine, and the immediate melatonin precursor serotonin. aaNAT1 represents a novel gene family unrelated to known acetyltransferases, except in two weakly conserved amino acid motifs. In situ hybridization studies of aaNAT1 mRNA in embryos reveal hybridization signals in the brain, the ventral cord, the gut, and probably in oenocytes, indicating a broad tissue distribution of aaNAT1 transcripts. Moreover, in day/ night studies we demonstrate a diurnal rhythm of melatonin concentration without a clear-cut change in aaNATI mRNA levels. The data suggest that tissue-specific regulation of aaNAT1 may be associated with different enzymatic functions and do not exclude the possibility of additional aaNAT genes.Amine acetylation in insects by the enzyme arylalkylamine N-acetyltransferase (aaNAT, EC 2.3.1.87) is involved in at least three different physiological functions: (i) It appears to be the major route of neurotransmitter catabolism (1-4), inactivating biogenic amines including tryptamine, tyramine, octopamine, serotonin, and norepinephrine. (ii) An acetylated amine, acetyldopamine, is subsequently oxidized to the respective quinone, which cross-links different proteins and/or chitin, resulting in stabilization and hardening (sclerotization) of the insect cuticle (5). (iii) Acetylation of serotonin plays an important role in the regulation of photoperiodically influenced physiological and behavioral processes (6). The major regulatory hormone is melatonin (7, 8), which is synthesized by the methylation of acetylserotonin. In vertebrates, melatonin is secreted periodically with high concentration at night, caused by a 10-to 100-fold nocturnal increase in aaNAT activity (8). The final steps of aaNAT activation are still unclear and presumably involve new RNA and protein synthesis (9-12). All living organisms are influenced by environmental factors such as light and dark and thus need mechanisms to coordinate their physiological processes in response to seasonal changes. Serotonin, aaNAT activity, and melatonin have indeed been found in several organs (eye, optic lobe, and brain) of various invertebrate species in which melatonin concentration also shows a rhythmic behavior (13). However, it is not known if aaNAT activity and melatonin are subject to diurnal variation in Drosophila melanogaster. aaNAT activity has been described in several insect species (14-18), including D. melanogaster (2, 19), but none of these enzymes could be purified to derive antibodies or sufficient internal sequence information for cloning. We have purified an aaNAT from D. melanogaster using tryptam...

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Metabolism of biogenetic amines in drosophila nervous tissue

Cited by 96 publications

References 16 publications

High levels of intron-containing RNAs are associated with expression of the Drosophila DOPA decarboxylase gene.

High levels of intron-containing RNAs are associated with expression of the Drosophila DOPA decarboxylase gene.

Isolation and characterization of an arylalkylamine N‐acetyltransferase from Drosophila melanogaster

Cloning of an arylalkylamine N-acetyltransferase (aaNAT1) from Drosophila melanogaster expressed in the nervous system and the gut.

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