Cyclooxygenase and lipoxygenase-like activity in drosophila melanogaster

Pagès, Montserrat; Roselló, J.; Casas, Josefina; Gelpí, E.; Gualde, N.; Rigaud, M.

doi:10.1016/0090-6980(86)90195-4

Cited by 35 publications

(21 citation statements)

References 23 publications

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“…HETEs are monohydroxyl fatty acids, produced enzymatically and non-enzymatically from arachidonic acid (C20:4). 11,12) They contain a hydroxyl group in their structure, like firefly luciferin, but they were poor substrates (0 to 30% activity with arachidonic acid) for firefly luciferases. In contrast, some HETEs (5-HETE, 12-HETE, 15-HETE) were good substrates (150 to 180% activity with arachidonic acid) for CG6178 (Fig.…”

Section: Substrate Specificitymentioning

confidence: 99%

Enzymatic and Genetic Characterization of Firefly Luciferase andDrosophilaCG6178 as a Fatty Acyl-CoA Synthetase

Oba

Sato

Ojika

et al. 2005

Bioscience, Biotechnology, and Biochemistry

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Recently we found that firefly luciferase is a bifunctional enzyme, catalyzing not only the luminescence reaction but also long-chain fatty acyl-CoA synthesis. Further, the gene product of CG6178 (CG6178), an ortholog of firefly luciferase in Drosophila melanogaster, was found to be a long-chain fatty acyl-CoA synthetase and dose not function as a luciferase. We investigated the substrate specificities of firefly luciferase and CG6178 as an acyl-CoA synthetase utilizing a series of carboxylic acids. The results indicate that these enzymes synthesize acyl-CoA efficiently from various saturated medium-chain fatty acids. Lauric acid is the most suitable substrate for these enzymes, and the product of lauroyl CoA was identified with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). Phylogenetic analysis indicated that firefly luciferase and CG6178 genes belong to the group of plant 4-coumarate:CoA ligases, and not to the group of medium-and long-chain fatty acyl-CoA synthetases in mammals. These results suggest that insects have a novel type of fatty acyl-CoA synthetase.

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Section: Substrate Specificitymentioning

confidence: 99%

Enzymatic and Genetic Characterization of Firefly Luciferase andDrosophilaCG6178 as a Fatty Acyl-CoA Synthetase

Oba

Sato

Ojika

et al. 2005

Bioscience, Biotechnology, and Biochemistry

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“…four starfish species (Meijer et al 1986), the sea squirt Ciona intestinalis, and the surf clam Spisula solidissima (Hada et al 1997). Pagés et al (1986) demonstrated lipoxygenase activity in Drosophila melanogaster extracts and also the presence of lipoxygenase-like immunoreactivity in ejaculatory bulb of male flies. The reproductive tract of mated firebrat Thermobia domestica has lipoxygenase activity (Ragab et al 1987(Ragab et al , 1991, and the egg laying behavior is dependent of phospholipase A 2 activity, which seems to be augmented after mating (Bitsch et al 1995).…”

Section: Eicosanoids As Local Regulators Of Oogenesismentioning

confidence: 99%

Oogenesis and egg development in triatomines: a biochemical approach

Atella

Gondim

Machado

et al. 2005

An. Acad. Bras. Ciênc.

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In triatomines, as well as in other insects, accumulation of yolk is a process in which an extra-ovarian tissue, the fat body, produces yolk proteins that are packed in the egg. The main protein, synthesized by the fat body, which is accumulated inside the oocyte, is vitellogenin. This process is also known as vitellogenesis. There are growing evidences in triatomines that besides fat body the ovary also produces yolk proteins. The way these yolk proteins enter the oocyte will be discussed. Yolk is a complex material composed of proteins, lipids, carbohydrates and other minor components which are packed inside the oocyte in an organized manner. Fertilization triggers embryogenesis, a process where an embryo will develop. During embryogenesis the yolk will be used for the construction of a new individual, the first instar nymph. The challenge for the next decade is to understand how and where these egg proteins are used up together with their non-protein components, in pace with the genetic program of the embryo, which enables cell differentiation (early phase of embryogenesis) and embryo differentiation (late phase) inside the egg.

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“…Cox2 knockout mice are defective in all aspects of female reproduction (Lim et al, 1997), while loss of Cox1 blocks labor. PGs and PG synthetic activity has also been found in many invertebrates (Stanley, 2006;Stanley-Samuelson and Pedibhotla, 1996), including Drosophila (Pages et al, 1986). PG levels in these animals frequently rise upon mating, while exogenous PGs stimulate both egg development and laying (Stanley, 2006;Stanley-Samuelson and Pedibhotla, 1996).…”

Section: Introductionmentioning

confidence: 99%

DrosophilaPxt: a cyclooxygenase-like facilitator of follicle maturation

2008

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Prostaglandins are local transient hormones that mediate a wide variety of biological events, including reproduction. The study of prostaglandin biology in a genetically tractable invertebrate model organism has been limited by the lack of clearly identified prostaglandin-mediated biological processes and prostaglandin metabolic genes, particularly analogs of cyclooxygenase (COX), the rate-limiting step in vertebrate prostaglandin synthesis. Here, we present pharmacological data that Drosophila ovarian follicle maturation requires COX-like activity and genetic evidence that this activity is supplied in vivo by the Drosophila peroxidase Pxt. pxt mutant females are sterile, and maturing follicles show defects in actin filament formation, nurse cell membrane stability and border cell migration. Maturation of pxt follicles in vitro is stimulated by prostaglandin treatment and fertility is restored in vivo to pxt mutants by expressing mammalian Cox1 protein. Our experiments suggest that prostaglandins promote Drosophila follicle maturation, in part by modulating the actin cytoskeleton, and establish Drosophila oogenesis as a model for understanding these critical biological regulators.

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Cyclooxygenase and lipoxygenase-like activity in drosophila melanogaster

Cited by 35 publications

References 23 publications

Enzymatic and Genetic Characterization of Firefly Luciferase andDrosophilaCG6178 as a Fatty Acyl-CoA Synthetase

Enzymatic and Genetic Characterization of Firefly Luciferase andDrosophilaCG6178 as a Fatty Acyl-CoA Synthetase

Oogenesis and egg development in triatomines: a biochemical approach

DrosophilaPxt: a cyclooxygenase-like facilitator of follicle maturation

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