Insect storage proteins: Gene families and receptors

Haunerland, Norbert H.

doi:10.1016/s0965-1748(96)00035-5

Cited by 152 publications

(147 citation statements)

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“…As demonstrated, HP19 inhibits the 20E-induced phosphorylation of the hexamerin receptor. The physiological significance of this inhibition lies in the experimental evidence that uptake of hexamerin is a stage-specific event (46,56). As we have shown earlier, the receptor is present during the last larval instar in an inactive form and is not capable of sequestering hexamerins, i.e.…”

Section: E-stimulated Acp Activity Regulation By Hp19mentioning

confidence: 75%

“…Although a few nanograms of the protein were found to be sufficient for stimulation even in crude or partially purified fractions, the yield of the purified protein was very low. Other limitations were the requirement of a large quantity of hemolymph of a specific developmental stage (LLI) and removal of the major contaminating protein, hexamerin, which constitutes 75-80% of total hemolymph protein (46). Therefore, an antibody against HP19 was raised by electroeluting HP19, and its specificity against HP19 was 5.…”

Section: E-stimulated Acp Activity Regulation By Hp19mentioning

confidence: 99%

“…The major fraction consists of hexamerins, which are sequestered by the larval fat body by receptor-mediated endocytosis, stored in vacuoles, and utilized by the activity of lysosomal enzymes (46,56,57). The hexamerin receptor of Corcyra, a 120-kDa protein, is activated through phosphorylation by a tyrosine kinase in the fat body membrane (22).…”

Section: E-stimulated Acp Activity Regulation By Hp19mentioning

confidence: 99%

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The Insect Hemolymph Protein HP19 Mediates the Nongenomic Effect of Ecdysteroids on Acid Phosphatase Activity

Arif

Vasanthi

Hansen

et al. 2004

Journal of Biological Chemistry

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The activity of acid phosphatase (ACP) in insect fat bodies is stimulated by the steroid hormone 20-hydoxyecdysone (20E) in vivo. However, in fat bodies kept in culture, a factor from the hemolymph is required to enhance the ACP activity. We identified the factor as a protein with a molecular mass of 19 kDa (HP19) from the hemolymph of a lepidopteran insect, the rice moth, Corcyra cephalonica. Western analysis of hemolymph proteins with denaturing and non-denaturing PAGE using antibodies raised against HP19 suggest that this protein exists as a monomer. It is synthesized by the hind gutassociated lobular fat body of the larvae and is released into the hemolymph. The stimulatory effect of HP19 on the ACP activity is developmentally regulated and exhibits its maximal effect shortly before the onset of metamorphosis. We cloned the HP19 cDNA by immunoscreening a hind gut-associated lobular fat body cDNA expression library. Analysis of the amino acid sequence shows that HP19 belongs to the family of glutathione S-transferase (GST) like proteins. However, affinity-purified GST from Corcyra failed to show any mediation effect on 20E-stimulated ACP activity, and HP19 lacks GST enzymatic activity. Notably, HP19 mediates the hormone-stimulated ACP activity in intact fat body tissue and homogenates even in the presence of inhibitors of transcription and translation, suggesting a nongenomic mode of action. In addition, we show that HP19 inhibits the 20E-induced phosphorylation of the hexamerin receptor protein.Insect metamorphosis, the transition from the larval to the adult stage of insects, is controlled by ecdysteroid hormones (1-3). The ecdysteroids, like the steroids in vertebrates, regulate gene transcription by binding to the nuclear receptors, which are ligand-activated transcription factors that convert the hormonal stimulus into a transcription response (4 -7).Metamorphosis involves the breakdown of larval structures and the formation of new tissues (1). As a part of cell remodeling during metamorphosis, acidic autophagic vacuoles accumulate in the cells of the fat body, and the activity of several lysosomal enzymes such as acid phosphatases increase and cause the lysis of larval tissues (8 -11). The fat body fills a large fraction of the insect, and its function has been considered equivalent to the role of the vertebrate liver in the intermediary metabolism (12). It has been demonstrated that the stimulation of the lysosomal activity is governed by ecdysteroids (11, 13-16). There is an indication that in this case the hormone possibly acts on a nongenomic level (17). Although the molecular mechanism of the genomic mode of steroid action is well known, the mechanism of nongenomic steroid action remains unclear to date (18). Earlier studies show that 20E 1 stimulates ACP activity in fat bodies in vivo but not in vitro (19,20). This result suggests that 20E, the active form of ecdysone, requires an additional factor (or factors) to enhance ACP activity. Hence, we have focused on the process of acid phosphatase acti...

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Section: E-stimulated Acp Activity Regulation By Hp19mentioning

confidence: 75%

Section: E-stimulated Acp Activity Regulation By Hp19mentioning

confidence: 99%

Section: E-stimulated Acp Activity Regulation By Hp19mentioning

confidence: 99%

See 1 more Smart Citation

The Insect Hemolymph Protein HP19 Mediates the Nongenomic Effect of Ecdysteroids on Acid Phosphatase Activity

Arif

Vasanthi

Hansen

et al. 2004

Journal of Biological Chemistry

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“…SPs function as an amino acids reserve for the production of adult proteins. 1,2 Insect SPs are generally categorized into two groups: methionine-rich proteins and aromatic-rich proteins (arylphorins). In Bombyx mori, storage protein 1 (SP1) is named for methionine-rich protein, and storage protein 2 (SP2) is named for aromatic-rich protein (arylphorin).…”

Section: Introductionmentioning

confidence: 99%

Crystal structure of Bombyx mori arylphorins reveals a 3:3 heterohexamer with multiple papain cleavage sites

Hou

et al. 2014

Protein Science

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In holometabolous insects, the accumulation and utilization of storage proteins (SPs), including arylphorins and methionine-rich proteins, are critical for the insect metamorphosis. SPs function as amino acids reserves, which are synthesized in fat body, secreted into the larval hemolymph and taken up by fat body shortly before pupation. However, the detailed molecular mechanisms of digestion and utilization of SPs during development are largely unknown. Here, we report the crystal structure of Bombyx mori arylphorins at 2.8 Å , which displays a heterohexameric structural arrangement formed by trimerization of dimers comprising two structural similar arylphorins. Our limited proteolysis assay and microarray data strongly suggest that papain-like proteases are the major players for B. mori arylphorins digestion in vitro and in vivo. Consistent with the biochemical data, dozens of papain cleavage sites are mapped on the surface of the heterohexameric structure of B. mori arylphorins. Hence, our results provide the insightful information to understand the metamorphosis of holometabolous insects at molecular level.

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“…Together, the studies by Djawdan et al (1996) and Simmons and Bradley (1997) suggest that long-lived insects increase storage of carbohydrates and lipids. However, insects are well known to store proteins as well as carbohydrates and lipids (e.g., Haunerland 1996). Further, proteins are the limiting nutrient for development in many insects.…”

Section: Introductionmentioning

confidence: 99%

Calorie restriction and late-onset calorie restriction extend lifespan but do not alter protein storage in female grasshoppers

Hatle

Wells

Fuller

et al. 2006

Mechanisms of Ageing and Development

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SummaryCalorie restriction (CR) and late-onset CR enhance longevity in many organisms. Resource allocation theory suggests that longevity is enhanced by increasing somatic storage, at the expense of current reproduction. Phytophagous insects accumulate amino acids as hemolymph storage proteins for major developmental events. We hypothesized that protein storage is involved in life extension from CR. In a longitudinal experiment, we tested whether CR altered protein storage in female grasshoppers. Individuals on CR (60% or 70%) or late-onset CR had at least 60% greater longevity than ad libitum individuals. Age at first oviposition, dry mass of the first clutch, or lifetime fecundity were not affected by CR, but CR did increase the number of clutches produced. Most important, females on life-extending CR and late-onset CR did not differ in the concentration of hemolymph storage of proteins in comparison to ad libitum females. Protein storage changed with time in all groups, demonstrating sufficient sensitivity in our methods. Previous experiments have shown that severe CR (~30% of ad libitum) can reduce hemolymph storage. Therefore, the reduction in intake needed to extend lifespan is not sufficient to reduce protein storage in the hemolymph. These results do not support the hypothesis that protein storage is involved in life extension from CR.

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Insect storage proteins: Gene families and receptors

Cited by 152 publications

References 50 publications

The Insect Hemolymph Protein HP19 Mediates the Nongenomic Effect of Ecdysteroids on Acid Phosphatase Activity

The Insect Hemolymph Protein HP19 Mediates the Nongenomic Effect of Ecdysteroids on Acid Phosphatase Activity

Crystal structure of Bombyx mori arylphorins reveals a 3:3 heterohexamer with multiple papain cleavage sites

Calorie restriction and late-onset calorie restriction extend lifespan but do not alter protein storage in female grasshoppers

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