Insights into the transcriptome of oenocytes from Aedes aegypti pupae

Martins, Gustavo Ferreira; Ramalho-Ortigão, José Marcelo; Lobo, Neil F.; Severson, David W.; McDowell, Mary Ann; Pimenta, Paulo Filemon Paolucci

doi:10.1590/s0074-02762011000300009

Cited by 23 publications

(20 citation statements)

References 34 publications

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“…Another common finding is the absence of lipid droplets and glycogen granules in the oenocyte's cytoplasm (Sohal 1973, Tobe et al 1973, Stoppie et al 1981. Histochemically, oenocytes have a cytoplasm that is strongly and uniformly stained for proteins, which is evidence of the synthesis of proteins in these cells in the adult mosquito (Wigglesworth 1988, Fan et al 2003, Roma et al 2006, Gutierrez et al 2007, Martins et al 2011b.…”

Section: Discussionmentioning

confidence: 99%

“…darlingi may also be involved in lipid metabolism, including the synthesis of components of a lipidic nature, as suggested by the presence of a well-developed SER (Jackson & Locke 1989, Fan et al 2003 and by their gene expression profile in Drosophila melanogaster (Gutierrez et al 2007) and Ae. aegypti (Martins et al 2011b).…”

Section: Discussionmentioning

confidence: 99%

“…Ectodermic cells, such as oenocytes, are also present in the mosquito fat body (Martins et al 2011c). Oenocytes can be associated with either epidermal cells or trophocytes whose functions are linked with the synthesis of hydrocarbons and homeostasis (Gutierrez et al 2007, Martins et al 2011b.…”

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confidence: 99%

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A comparative study of fat body morphology in five mosquito species

Martins

Serrão

Ramalho-Ortigão

et al. 2011

Mem. Inst. Oswaldo Cruz

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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A comparative study of fat body morphology in five mosquito species

Martins

Serrão

Ramalho-Ortigão

et al. 2011

Mem. Inst. Oswaldo Cruz

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“…Using specific RNAi to each of the twenty Drosophila elongase subunits, we have found that only one of them could recapitulate the phenotype due to oenocyte disruption of ACC, arguing for a particular VLCFA in this essential function. Interestingly, a transcriptome analysis revealed that several genes encoding FA anabolic enzymes are upregulated in mosquito oenocytes, including FAS and two putative elongases [50]. Desat1, the Drosophila homologue of the Stearoyl CoA-desaturase-1—which catalyzes the formation of a double bound to generate the unsaturated palmitoleic and oleic acids—is one of the gene products reported to be highly expressed in oenocytes [51].…”

Section: Discussionmentioning

confidence: 99%

Drosophila melanogaster Acetyl-CoA-Carboxylase Sustains a Fatty Acid–Dependent Remote Signal to Waterproof the Respiratory System

et al. 2012

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Fatty acid (FA) metabolism plays a central role in body homeostasis and related diseases. Thus, FA metabolic enzymes are attractive targets for drug therapy. Mouse studies on Acetyl-coenzymeA-carboxylase (ACC), the rate-limiting enzyme for FA synthesis, have highlighted its homeostatic role in liver and adipose tissue. We took advantage of the powerful genetics of Drosophila melanogaster to investigate the role of the unique Drosophila ACC homologue in the fat body and the oenocytes. The fat body accomplishes hepatic and storage functions, whereas the oenocytes are proposed to produce the cuticular lipids and to contribute to the hepatic function. RNA–interfering disruption of ACC in the fat body does not affect viability but does result in a dramatic reduction in triglyceride storage and a concurrent increase in glycogen accumulation. These metabolic perturbations further highlight the role of triglyceride and glycogen storage in controlling circulatory sugar levels, thereby validating Drosophila as a relevant model to explore the tissue-specific function of FA metabolic enzymes. In contrast, ACC disruption in the oenocytes through RNA–interference or tissue-targeted mutation induces lethality, as does oenocyte ablation. Surprisingly, this lethality is associated with a failure in the watertightness of the spiracles—the organs controlling the entry of air into the trachea. At the cellular level, we have observed that, in defective spiracles, lipids fail to transfer from the spiracular gland to the point of air entry. This phenotype is caused by disrupted synthesis of a putative very-long-chain-FA (VLCFA) within the oenocytes, which ultimately results in a lethal anoxic issue. Preventing liquid entry into respiratory systems is a universal issue for air-breathing animals. Here, we have shown that, in Drosophila, this process is controlled by a putative VLCFA produced within the oenocytes.

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“…Insect CPR genes are expressed in antennae of Drosophila melanogaster Meigen (Hovemann et al 1997), Mamestra brassicae L. (Maṏbè cheCoisne et al 2005), and Spodoptera littoralis (Boisduval) (Pottier et al 2012), and in oenocytes of Aedes aegypti L. (Martins et al 2011) and Anopheles gambiae Giles (Lycett et al 2006).…”

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confidence: 99%

Identification and Analysis of NADPH-Cytochrome P450 Reductase inAedes sollicitans(Diptera: Culicidae)

2014

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An NADPH-cytochrome P450 reductase (CPR) gene was identiÞed in Aedes sollicitans Walker (Diptera: Culicidae). The open reading frame is 2,040 bp long, encoding a 679-residue polypeptide. Amino acid sequence analysis indicates that the Ae. sollicitans CPR carries conserved ligand-binding domains and belongs to the same phylogenetic group as CPRs in other mosquitoes. The cDNA of the CPR gene was cloned, and the recombinant protein was expressed in Escherichia coli. Cytochrome c reductase activity was detected in the bacterial cytosolic and membrane fractions and in larval microsomes from two New Jersey Ae. sollicitans populations, indicating that the Ae. sollicitans CPR is enzymatically functional and closely related to that in other dipterans.

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Insights into the transcriptome of oenocytes from Aedes aegypti pupae

Cited by 23 publications

References 34 publications

A comparative study of fat body morphology in five mosquito species

A comparative study of fat body morphology in five mosquito species

Drosophila melanogaster Acetyl-CoA-Carboxylase Sustains a Fatty Acid–Dependent Remote Signal to Waterproof the Respiratory System

Identification and Analysis of NADPH-Cytochrome P450 Reductase inAedes sollicitans(Diptera: Culicidae)

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