Developmentally Controlled Cleavage of the <i>Calliphora</i> Arylphorin Receptor and Posttranslational Action of the Steroid Hormone 20‐Hydroxyecysone

Burmester, Thorsten; Scheller, Klaus

doi:10.1111/j.1432-1033.1997.00695.x

Cited by 24 publications

(29 citation statements)

References 37 publications

(46 reference statements)

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“…Fat body ribbons in the perivisceral region are almost cylindrical while the ribbons are wide and flat in the peripheral region. The uptake of SP occurs only during a brief time period shortly before and after pupation, and this uptake is a receptor-mediated endocytosis (Ueno and Natori, 1987;Haunerland, 1996;Burmester and Scheller, 1997). Uptake and accumulation of SP in the fat body has been biochemically and electron microscopically well documented (Tojo et al, 1978(Tojo et al, , 1980Wang and Haunerland, 1991.…”

mentioning

confidence: 96%

Expression and localization of storage protein 1 (SP1) in differentiated fat body tissues of red hairy caterpillar,Amsacta albistrigaWalker

Chandrasekar

Jae

Krishnan

2008

Arch Insect Biochem Physiol

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The accumulation and utilization of storage proteins are prominent events linked to the metamorphosis of holometabolous insects. The female-specific storage protein 1 (SP1) is the major storage protein found in the hemolymph and fat body of female larvae of the groundnut pest, Amsacta albistriga. Here we show SP1 expression and localization in differentiated fat body tissues using biochemical and immunohistochemistry scrutiny. Comparison of A. albistriga SP1 with that of other species with respect to amino acid composition and N-terminal sequences show that SP1 is a methonine-rich protein and its identity was confirmed by means of immunoblot analysis. Northern blot studies revealed that the SP1 gene demonstrates stage- and tissue-specific expression in the peripheral fat body cells during the mid-larval period of fifth instar of A. albistriga. During the larval pupal transformation, SP1 are sequestered mainly by the perivisceral fat body tissues, until they serve the purpose of supplying amino acids for the production of egg yolk proteins. Further, electron microscopic studies using immunogold tracer techniques confirmed the localization of crystalline SP1 reserves, stored in the perivisceral fat body tissues. Hence, the peripheral fat body is responsible for biosynthesis of storage proteins, whereas the perivisceral fat body is a specialized storage organ.

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mentioning

confidence: 96%

Expression and localization of storage protein 1 (SP1) in differentiated fat body tissues of red hairy caterpillar,Amsacta albistrigaWalker

Chandrasekar

Jae

Krishnan

2008

Arch Insect Biochem Physiol

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“…behind the hormone producing glands, the posterior part of the animal is known to be relatively free of endogenous ecdysteroids (35)(36)(37). Fig.…”

Section: Identification Of a Protein In The Hemolymph Of Corcyra Thatmentioning

confidence: 99%

“…However, studies on these mechanisms are restricted to a small number of experimental systems, e.g. the activation of lysosomal enzymes and the hexamerin receptor (17,22,37).…”

Section: E-stimulated Acp Activity Regulation By Hp19mentioning

confidence: 99%

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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“…Hexamerins are taken up by the fat body shortly before pupation and stored in protein granules. The rise in the level of the steroid hormone 20-hydroxyecdysone (20E) at the end of larval life triggers the incorporation of these hexamerins from the haemolymph into the fat body (Burmester and Scheller 1997;Kirankumar et al 1997). Even though the endocytosis of vitellogenins by oocytes is well established, the regulation of hexamerin uptake and their delivery to protein storage granules of the fat body remains elusive, in spite of extensive studies that proposed to investigate whether the uptake process is a 'classical' endocytosis or anything different (Burmester and Scheller 1999).…”

Section: Introductionmentioning

confidence: 99%

Is hexamerin receptor a GPI-anchored protein in Achaea janata (Lepidoptera: Noctuidae)?

2011

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The process of uptake of hexamerins during metamorphosis from insect haemolymph by fat body cells is reminiscent of receptor-mediated endocytosis. Previously, we had identified a hexamerin-binding protein (HBP) and reported for the first time that uptake of hexamerins is dependent on the phosphorylation of HBP partly by a tyrosine kinase, which is, in turn, activated by 20-hydroxyecdysone (20E). However, the exact nature of HBP and the mechanism of interaction are still unknown. Here we report the possibility of HBP being a GPI-anchored protein in the fat body of Achaea janata and its role in the tyrosine-kinase-mediated phosphorylation signalling. Digestion of fat body membrane preparation with bacterial phosphatidylinositol-specific phospholipase C (PI-PLC), and the subsequent recognition by antibodies specific for the cross-reacting determinant (CRD), revealed that HBP is glycosylphosphatidylinositol (GPI)-anchored protein and, further, that the hexamerin binding to HBP was inhibited after digestion. Hexamerin overlay assay (HOA) of co-immunoprecipitated in vitro phosphorylated HBP showed exclusive binding to ~120 kDa protein. Lectin-binding analysis of hexamerins revealed the presence of N-acetylgalactosamine (GalNAc) and N-acetylglucosamine (GluNAc), whereas HBP showed the presence of GalNac alone. Mild chemical deglycosylation studies and binding interaction in the presence of sugars revealed that glycan moieties are possibly not involved in the interaction between HBP and hexamerins. Taken together, these results suggest that HBP may be a GPI-anchored protein, and interaction and activation of HBP is through lipid-linked non-receptor src tyrosine kinases. However, additional studies are needed to prove that HBP is a GPI-anchored protein.

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Developmentally Controlled Cleavage of the Calliphora Arylphorin Receptor and Posttranslational Action of the Steroid Hormone 20‐Hydroxyecysone

Cited by 24 publications

References 37 publications

Expression and localization of storage protein 1 (SP1) in differentiated fat body tissues of red hairy caterpillar,Amsacta albistrigaWalker

Expression and localization of storage protein 1 (SP1) in differentiated fat body tissues of red hairy caterpillar,Amsacta albistrigaWalker

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

Is hexamerin receptor a GPI-anchored protein in Achaea janata (Lepidoptera: Noctuidae)?

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