A proposed biosynthesis pathway of drosopterins in Drosophila melanogaster

Parisi, G.; Carfagna, M.; D'Amora, D

doi:10.1016/0022-1910(76)90012-3

Cited by 12 publications

(2 citation statements)

References 31 publications

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“…Although studies of the presence of particular pteridines in insects and the biochemical pathways associated with their accumulation continue (e.g. Fan et al, 1976;Parisi et al, 1976;Silva et al, 1991), the link between these processes and the behavioral and ecological factors that modify them unfortunately remains obscure.…”

Section: Discussionmentioning

confidence: 99%

Age determination in individual wild-caughtDrosophila serratausing pteridine concentration

Robson

Vickers

Blows

et al. 2006

Journal of Experimental Biology

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SUMMARY Fluorescence spectrophotometry can reliably detect levels of the pteridine 6-biopterin in the heads of individual Drosophila serrata Malloch 1927. Pteridine content in both laboratory and field captured flies is typically a level of magnitude higher than the minimally detectable level(meanlab=0.54 units, meanfield=0.44 units, minimum detectable level=0.01 units) and can be used to predict individual age in laboratory populations with high certainty (r2=57%). Laboratory studies of individuals of known age (from 1 to 48 days old)indicate that while pteridine level increases linearly with age, they also increase in a linear manner with rearing temperature and ambient light levels,but are independent of sex. As expected, the longevity of laboratory-reared males (at least 48 days) is higher than the range of predicted ages of wild-caught males based on individual pteridine levels (40 days). However, the predictive equation based on pteridine level alone suggested that a number of wild-caught males were less than 0 days old, and the 95% confidence limits for these predictions based on the inverse regression are broad. The age of the oldest wild-caught male is predicted to fall within the range of 2 to 50 days. The significant effects of temperature and light intensity determined in the laboratory study (effect sizes ω2=14.3 and 20.4%,respectively) suggests that the calibration of the age prediction equation for field populations would be significantly improved when combined with fine-scaled studies of habitat temperature and light conditions. The ability to determine relative age in individual wild-caught D. serratapresents great opportunities for a variety of evolutionary studies on the dynamics of natural populations.

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Section: Discussionmentioning

confidence: 99%

Age determination in individual wild-caughtDrosophila serratausing pteridine concentration

Robson

Vickers

Blows

et al. 2006

Journal of Experimental Biology

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“…A mitochondrial process oxidising H 2 ‐xanthommatin with O 2 was proposed to regenerate xanthommatin. Similarly, xanthommatin was proposed to be a cofactor of xanthine dehydrogenase in the biogenesis of pterins in fruit fly eyes (Parisi, Carfagna & D'Amora, , ). Finally, Santoro & Parisi () suggested that H 2 ‐xanthommatin was formed by the action of a specific enzyme, called xanthommatin reductase, that used NADH as a cofactor; in this case, pterins were involved as potent inhibitors of this redox reaction.…”

Section: Ommochrome Biochemistry: From the Indole To The Phenoxazone mentioning

confidence: 99%

Ommochromes in invertebrates: biochemistry and cell biology

2018

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Ommochromes are widely occurring coloured molecules of invertebrates, arising from tryptophan catabolism through the so-called Tryptophan → Ommochrome pathway. They are mainly known to mediate compound eye vision, as well as reversible and irreversible colour patterning. Ommochromes might also be involved in cell homeostasis by detoxifying free tryptophan and buffering oxidative stress. These biological functions are directly linked to their unique chromophore, the phenoxazine/phenothiazine system. The most recent reviews on ommochrome biochemistry were published more than 30 years ago, since when new results on the enzymes of the ommochrome pathway, on ommochrome photochemistry as well as on their antiradical capacities have been obtained. Ommochromasomes are the organelles where ommochromes are synthesised and stored. Hence, they play an important role in mediating ommochrome functions. Ommochromasomes are part of the lysosome-related organelles (LROs) family, which includes other pigmented organelles such as vertebrate melanosomes. Ommochromasomes are unique because they are the only LRO for which a recycling process during reversible colour change has been described. Herein, we provide an update on ommochrome biochemistry, photoreactivity and antiradical capacities to explain their diversity and behaviour both in vivo and in vitro. We also highlight new biochemical techniques, such as quantum chemistry, metabolomics and crystallography, which could lead to major advances in their chemical and functional characterisation. We then focus on ommochromasome structure and formation by drawing parallels with the well-characterised melanosomes of vertebrates. The biochemical, genetic, cellular and microscopic tools that have been applied to melanosomes should provide important information on the ommochromasome life cycle. We propose LRO-based models for ommochromasome biogenesis and recycling that could be tested in the future. Using the context of insect compound eyes, we finally emphasise the importance of an integrated approach in understanding the biological functions of ommochromes.

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