Methionine-rich hexamerin and arylphorin as precursor reservoirs for reproduction and metamorphosis in female luna moths

Pan, M. L.; Telfer, William H.

doi:10.1002/(sici)1520-6327(1996)33:2<149::aid-arch5>3.0.co;2-t

Cited by 57 publications

(43 citation statements)

References 23 publications

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“…In contrast, aspartate exhibited relatively low turnover with the adult diet even though its precursor, oxaloacetate, is also a (31,32). Breakdown of this protein store should contribute aspartate with a larval isotopic signature throughout a female's lifetime, thus contributing to its low turnover with the adult diet.…”

Section: Discussionmentioning

confidence: 99%

“…These modest fractionations are interesting given the massive morphological, physiological, and biochemical changes that the moths undergo during larval growth, metamorphosis, and reproduction. They suggest that the larval-derived amino acids used in eggs are relatively inactive metabolically, a view that accords with the possibility that storage proteins serve as a reservoir for these compounds (31,32).…”

Section: Discussionmentioning

confidence: 99%

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Renewable and nonrenewable resources: Amino acid turnover and allocation to reproduction in Lepidoptera

O’Brien

Fogel

Boggs

2002

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

275

293

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The allocation of nutritional resources to reproduction in animals is a complex process of great evolutionary significance. We use compound-specific stable isotope analysis of carbon (GC͞combus-tion͞isotope ratio MS) to investigate the dietary sources of egg amino acids in a nectar-feeding hawkmoth. Previous work suggests that the nutrients used in egg manufacture fall into two classes: those that are increasingly synthesized from adult dietary sugar over a female's lifetime (renewable resources), and those that remain exclusively larval in origin (nonrenewable resources). We predict that nonessential and essential amino acids correspond to these nutrient classes and test this prediction by analyzing egg amino acids from females fed isotopically distinct diets as larvae and as adults. The results demonstrate that essential egg amino acids originate entirely from the larval diet. In contrast, nonessential egg amino acids were increasingly synthesized from adult dietary sugars, following a turnover pattern across a female's lifetime. This study demonstrates that female Lepidoptera can synthesize a large fraction of egg amino acids from nectar sugars, using endogenous sources of nitrogen. However, essential amino acids derive only from the larval diet, placing an upper limit on the use of adult dietary resources to enhance reproductive success.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Renewable and nonrenewable resources: Amino acid turnover and allocation to reproduction in Lepidoptera

O’Brien

Fogel

Boggs

2002

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

275

293

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“…From the hemolymph and fat-body storage compartments, hexamerins replenish amino acid reserves depleted during metamorphosis and adult development. Studies have suggested that differential storage and utilization of insect hexamerins may be based in part on their amino acid composition [2,44]. Enhanced production of methionine-rich hexamerins in female lepidopteran larvae may provide an important methionine reserve for oogenesis when cysteine is needed for chorion (egg shell) protein cross-linking [2, 101.…”

Section: Discussionmentioning

confidence: 99%

Molecular Cloning and Expression of a Hexamerin cDNA from the Malaria Mosquito, Anopheles Gambiae

Zakharkin

Gordadze

Korochkina

et al. 1997

European Journal of Biochemistry

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During the last larval instar, dipteran insects synthesize two hexamerins rich in aromatic residues, typified by the larval serum proteins 1 and 2 (LSP‐1 and LSP‐2) of Drosophila melanogaster. We report here the characterization of a complete cDNA sequence encoding a LSP‐1‐like protein from a lower dipteran insect, the malaria mosquito Anopheles gambiae. The cDNA encodes the subunit of a homohexamer, A. gambiae hexamerin‐1.1 (AgHex‐1.1), which is a major pupal protein but only a minor constituent of late larval hemolymph. AgHex‐1.1 is moderately rich in methionine (3.9%) and particularly rich in aromatic residues (21% Phe + Tyr). Cytogenetic analysis reveals AgHex‐1.1 to be encoded by a single‐copy gene localized to division 22F within the proximal 2La inversion breakpoint of chromosome 2 of A. gambiae. The AgHex‐1.1 transcript is first detected in fourth‐instar larvae (L4) and disappears abruptly in early pupae. In situ hybridization shows accumulation of the transcript uniquely in the larval fat body. AgHex‐1.1 mRNA is re‐expressed in male and female adults at about 10% of the L4 level, with no effect of bloodfeeding in females. The potential roles of AgHex‐1.1 in Anopheles development and reproductive maturation are discussed.

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“…Met-rich hexamerins are more abundant in the female than in the male, and it has been assumed that they support female reproduction and egg development by enhancing the pool of sulphurcontaining amino acids at the time of vitellogenesis (Pan and Telfer, 1996). Likewise, the juvenile-hormone binding hexamerins of Orthoptera (cf.…”

Section: Article In Pressmentioning

confidence: 99%

Diversity of stonefly hexamerins and implication for the evolution of insect storage proteins

Hagner-Holler

Pick

Girgenrath

et al. 2007

Insect Biochemistry and Molecular Biology

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Methionine-rich hexamerin and arylphorin as precursor reservoirs for reproduction and metamorphosis in female luna moths

Cited by 57 publications

References 23 publications

Renewable and nonrenewable resources: Amino acid turnover and allocation to reproduction in Lepidoptera

Renewable and nonrenewable resources: Amino acid turnover and allocation to reproduction in Lepidoptera

Molecular Cloning and Expression of a Hexamerin cDNA from the Malaria Mosquito, Anopheles Gambiae

Diversity of stonefly hexamerins and implication for the evolution of insect storage proteins

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