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PubMedDate not supplied

[In vitro study of the early membrane effects of C27-steroid hormone ecdysterone, immobilized on the nanodispersed magnetite surface].

The object of the study was to reveal the existence of receptor interactions of C27-steroid hormone ecdysterone with the surface of various cells (liver and spleen macrophages, thymus and spleen lymphocytes, erythrocytes and hepatocytes from rat organs) in experiments in vitro using ecdysterone immobilized on the nanodispersed iron surface (which did not penetrate the cell during observation) and the model of fast (during 15 s) activation of phospholipid signal system with ecdysterone. The parameters, which are characteristic of cell phospholipid signal system activation, were evaluated (the concentrations of free arachidonic acid, diene conjugates, tromboxane B2 and leukotriene C4) and its alteration in response to free and immobilized ecdysterone introduction in suspensins of intact cells and cells with the surface modified in vivo by pre-injection of antigen (human erythrocytes). Concurrent binding of immbilized ecdysterone with intact rat cells in the presence of free ecdysterone was also investigated. It was established that there are high-affinity ecdysterone-specific binding sites on the plasma membranes of all cells investigated, Kd estimated according to two different methods varied in the region of 10(-8)-10(-7) M. The characteristic features of the changes in parameters characteristic of phospholipid system activation were revealed to be queite similar in intact cells, as well as in cells with modified surfaces, under introduction of free ecdysterone and immobilized ecdysterone, which did not penetrate into cytosole. The data obtained point to the existence of ecdysterone receptors on the surface of cells plasma membranes and are indicative of the membrane effects as mechanisms of the early pregenomic phase of cells activation by ecdysterone.

Animals↗
PubMed1983

Effects of exogenous ecdysterone upon moulting, proecdysial development, and limb regeneration in the prawn Palaemon elegans.

Injection of small doses of ecdysterone accelerated moulting and proecdysis in the prawn Palaemon elegans. Injection of large doses of ecdysterone (1-10 micrograms) markedly accelerated proecdysis, but death always occurred prior to or during moulting and was accompanied by abnormal setal development and retarded cuticle formation. Dose-response curves were obtained for a range of hormone doses from 10 to 0.01 micrograms by administering ecdysterone during postmoult (stages A-B) and early premoult (stages DE0-DL0). Accelerated proecdysis and viable moulting were more marked in the group injected during early premoult (stages DE0-DL0). The sensitivity threshold for prawns injected during this time was less than 40 ng g-1 but could not be determined more precisely in view of the range of ecdysterone concentrations used. In contrast, the sensitivity threshold for ecdysterone administered during postmoult (stages A-B) was much higher, between 0.4 and 2 micrograms g-1. The possible mechanisms controlling sensitivity thresholds for ecdysterone are discussed. The effect of ecdysterone on limb regeneration was also studied. Within the concentration range used, ecdysterone was found to have no effect on the rate of limb regeneration.

Animals↗
PubMed1983

Actin gene expression is modulated by ecdysterone in a Drosophila cell line.

The steroid hormone ecdysterone induced characteristic and specific changes of morphology, enzymatic activities and protein synthesis in a Kc 0% Drosophila melanogaster cell line. To study the ecdysterone action at a molecular level, a Drosophila genomic library was screened by differential hybridization to poly(A)+ RNA from control and ecdysterone-treated cells. Two recombinant phages were selected for hybridizing very intensively with poly(A)+ RNA of ecdysterone-treated cells and very weakly with poly(A)+ RNA of untreated ones. These two clones (lambda Dm 1632 and lambda Dm A5A1) mapped at the 5 C locus on polytene chromosomes; they overlap for a 9000 base-pair sequence that contains an abundantly transcribed region in ecdysterone-treated cells of about 2000 base-pairs. This region permits the selection of mRNA that gives, after translation in vitro, two polypeptides identified as cytoplasmic actin II and III. We demonstrated that these two recombinant phages, hybridizing preferentially with poly(A)+ RNA of ecdysterone-treated cells, contain the 5 C actin gene. Poly(A)+ RNA prepared from various times of treatment of cells were electrophoresed on agarose gels, transferred to nitrocellulose paper and then hybridized with the cloned actin probe. Results of these experiments indicate that there is a sharp increase in the level of RNA coding for actin after ecdysterone treatment of the cell, and that there are two forms of actin-specific RNA in the D. melanogaster cells. Using genomic blots with specific probes derived from lambda Dm 1632, we show that there are six actin genes per haploid Drosophila cell genome contained on six EcoRI fragments, as in Drosophila embryos, indicating that there is no rearrangement of these sequences in cultured cells. Our results suggest that the expression of actin genes in D. melanogaster Kc 0% cells is modulated by ecdysterone.

Actins↗
PubMed1984

Regulation of hemoglobin synthesis by ecdysterone and juvenile hormone during development of Chironomus thummi (Diptera).

Chironomus thummi contains nine soluble hemoglobins (Hbs) in the larval hemolymph which can be resolved by 12.7% acrylamide gel electrophoresis (pH 8.65). Hemoglobins 2 and 3 are stage specific for the 4th instar and are first detected by day 4 of this stage in vivo, being absent in the 3rd instar. Fat-body cultures in the presence of 3H-delta-aminolevulinic acid and 14C-amino acids synthesize and secrete labelled Hbs, as was assayed by acrylamide gel electrophoresis and immunoprecipitation of Hbs recovered from the culture medium. During development from 3rd instar to pupa, Chironomus fat body undergoes functional changes, being actively involved in Hb synthesis in intermolt periods and inactive with respect to Hb production during molting. The repression of Hb synthesis is reversed following the molt from the 3rd instar to the 4th instar. Metamorphosis is related to a gradual and irreversible loss of Hb synthesis and secretion by the fat body. The treatment of fat body in vitro with ecdysterone inhibits Hb synthesis in tissue from intermolt animals, even in the presence of excess methoprene, a potent juvenile hormone analogue. In contrast, immunoprecipitation of the translation products from a wheat-germ cell-free system, using mRNA from ecdysterone-treated 4th-instar fat body as a template, shows significant synthesis of globins, suggesting that ecdysterone does not affect the amount or template activity of globin messages. Methoprene induces the precocious in vitro synthesis of Hbs 2 and 3 in day-2 4th-instar fat body and enhances all Hb synthesis in the absence of ecdysterone. In vitro treatment with methoprene activates newly molted fat body to synthesize Hbs 2 and 3 in vitro. The process of Hb induction by this analogue is completely inhibited by actinomycin D or ecdysterone. Fat body from animals already exposed to high endogeneous ecdysterone titer are insensitive to treatment with this juvenile hormone analogue. Intermolt larvae normally possess stable Hb mRNA molecules, because actinomycin-D administration in vitro does not affect Hb synthesis for as long as 30 h, whereas it effectively inhibits all RNA synthesis in the fat body. Immunoprecipitation of globin translated in vitro from mRNA from 2-day-old 4th-instar larvae treated in vivo with methoprene shows enhanced synthesis of globins 2 and 3, as compared to controls with no treatment. It is suggested that both juvenile hormone and ecdysterone regulate Hb synthesis in Chironomus; juvenile hormone affecting the activity of Hb genes, and ecdysterone modulating the level of Hb gene expression.

Animals↗
PubMed1991

Genes for Drosophila small heat shock proteins are regulated differently by ecdysterone.

Genes for small heat shock proteins (hsp27 to hsp22) are activated in late third-instar larvae of Drosophila melanogaster in the absence of heat stress. This regulation has been simulated in cultured Drosophila cells in which the genes are activated by the addition of ecdysterone. Sequence elements (HERE) involved in ecdysterone regulation of the hsp27 and hsp23 genes have been defined by transfection studies and have recently been identified as binding sites for ecdysterone receptor. We report here that the hsp27 and hsp23 genes are regulated differently by ecdysterone. The hsp27 gene is activated rapidly by ecdysterone, even in the absence of protein synthesis. In contrast, high-level expression of the hsp23 gene begins only after a lag of about 6 h, is dependent on the continuous presence of ecdysterone, and is sensitive to low concentrations of protein synthesis inhibitors. Transfection experiments with reporter constructs show that this difference in regulation is at the transcriptional level. Synthetic hsp27 or hsp23 HERE sequences confer hsp27- or hsp23-type ecdysterone regulation on a basal promoter. These findings indicate that the hsp27 gene is a primary, and the hsp23 gene is mainly a secondary, hormone-responsive gene. Ecdysterone receptor is implied to play a role in the regulation of both genes.

Animals↗
PubMed1980

A critical period of ecdysterone action on sensitive clones of Drosophila cultured in vitro: the maturation of the cells.

Ecdysterone-sensitive clones cultured in vitro were isolated from established cell lines of Drosophila melanogaster. The clones FC and 89K are ecdysterone-inducible for two enzymatic activities: acetylcholinesterase and beta-galactosidase. No activity could be detected in untreated cells, whereas after treatment with 50-250 nM ecdysterone, the activity appeared after one day and increased during 3-4 days. We wanted to modulate the response of the cells by varying the conditions of the hormonal stimulus. Mimicking the physiological situation of Drosophila (the ecdysterone peak corresponding to the molts is preceded by low levels) we pretreated the cells with a subthreshold concentration (1-5 nM) for 2 days and then we added the stimulating concentration of 50-250 nM ecdysterone. The enzymatic activities were then detectable within the following hours and the final level of induction was about twice the one of cells without pretreatment. Thus, the continuous presence of a subthreshold concentration of ecdysterone provokes the maturation of the cells which become able to respond to the hormonal stimulus by a quicker and higher enzymatic induction. The cellular maturation seems to be a critical period. It is altosid-sensitive. Altosid (a juvenile hormone analog) abolishes the effects of the ecdysterone-induced maturation.

Acetylcholinesterase↗
PubMed1980

Localization of ecdysterone on polytene chromosomes of Drosophila melanogaster.

Ecdysterone has been crosslinked in situ to polytene chromosomes of salivary glands of Drosophila melanogaster by photoactivation. The crosslinked hormone has been localized on the chromosomes by indirect immunofluorescence microscopy. At different developmental stages the hormone was detected at different chromosomal loci. These chromosomal sites correspond to ecdysterone-inducible puff sites. Thus, the hormone binds directly to chromosomal loci, whose transcription depends on the presence of the hormone. Ecdysterone was also crosslinked to one puff site that regresses during larval development. This indicates that (i) hormone binding to polytene chromosomes activates transcription at specific loci, and (ii) hormone-dependent regression of intermolt puff 68C is mediated by direct binding of ecdysterone. Ecdysterone was not detected on puff sites that are independent of hormone action or in chromosomal interbands. After heat shock, no ecdysterone became crosslinked to polytene chromosomes.

Animals↗
PubMed1983

Selective gene expression induced by ecdysterone in cultured fat bodies of Drosophila.

Expression of the LSP-2 and P1 genes was induced in cultured fat bodies of Drosophila third-instar larvae by supplementing the culture medium with ecdysterone. The fat bodies were isolated from ecdysterone-deficient larvae of the temperature-sensitive mutant ecd1, which were shifted from the permissive to the restrictive temperature either at the beginning of the third instar for the detection of LSP-2 induction or several hours later for the detection of P1 induction. During normal larval development, the LSP-2 gene is expressed before the P1 gene, and this order is also observed in the cultured fat bodies. Induction was demonstrated by increased amounts of LSP-2 and P1 transcripts in the ecdysterone-supplemented fat bodies. The amount of P1 transcript was determined by two methods: one involved measuring the hybridization of a labeled P1 DNA probe to total fat body RNA; the other involved labeling the newly synthesized RNA in nuclei isolated from cultured fat bodies and measuring the hybridization of the labeled RNA to P1 DNA. Only the second method was used for the LSP-2 transcript because the earlier expression of the LSP-2 gene results in a measurable accumulation of the transcript in the fat bodies before ecdysterone supplementation. The maximal level of P1 induction was reached within 2 hr after supplementation, and the induction was not affected by a concentration of cycloheximide that strongly inhibited total protein synthesis, suggesting that ecdysterone acts directly on the P1 gene rather than indirectly by inducing formation of proteins required for the subsequent induction of P1. Ecdysterone appears to function normally in the cultured fat body system because the LSP-2 and P1 genes are induced in culture in the same order as in vivo and a third gene, G12, that is not induced in fat bodies in vivo also is not induced in culture.

Adipose Tissue↗
PubMed1991

Ecdysterone regulatory elements function as both transcriptional activators and repressors.

A synthetic, 23-bp ecdysterone regulatory element (EcRE), derived from the upstream region of the Drosophila melanogaster hsp27 gene, was inserted adjacent to the herpes simplex virus thymidine kinase promoter fused to a bacterial gene for chloramphenicol acetyltransferase (CAT). Hybrid constructs were transfected into Drosophila S3 cells and assayed for ecdysterone-inducible CAT expression. In the absence of ecdysterone a tandem pair of EcREs repressed the high constitutive level of CAT activity found after transfection with the parent reporter plasmid alone. After hormone addition very high levels of CAT activity were observed. Insertion of the EcRE pair 3' of the CAT gene also led to high levels of ecdysterone-induced CAT expression, but the repression of high constitutive levels of CAT activity failed to occur. The EcRE-CAT construct was cotransfected with plasmids containing tandem 10-mers or 40-mers of the EcRE but lacking a reporter gene. These additional EcREs led to a reduced level of ecdysterone-induced CAT activity and to an elevation of basal CAT activity in the absence of hormone. The data suggest that the receptor binds to the EcRE in the absence of hormone, blocking basal transcription from a constitutive promoter. In the presence of ecdysterone, receptor-hormone binding to the EcRE leads to greatly enhanced transcription.

Animals↗
PubMed1975

Ecdysterone and an analogue of juvenile hormone on the autophagy in the cells of fat body of mamestra brassicae.

The effect of ecdysterone and a juvenile hormone analogue (JHa) on autophagy and heterophagy was investigated in the fat body cells of the last larval instar of Mamestra brassicae. In the course of normal development autophagic vacuoles and protein granules of heterophagic origin begin to accumulate in these cells, on the 4th and 5th day of the last larval stage respectively. When ecdysterone (10 mug/g body weight) was administered to the larvae for 24 h either on the 1st or on the 2nd day of the last larval stage, autophagic and heterophagic vacuoles appeared in the cells as early as on the 2nd or 3rd days. Autophagy was also observed in the cells of one-or two-day-old last larval fat body after a 5 h incubation in a medium containing 10 mug/ml ecdysterone, in vitro. Ligation of the last thoracic segment resulted in inhibition of metamorphic changes in the fat body lobules of the isolated abdomen. Injection of 10 mug ecdysterone into the isolated abdomen resulted in an appearence of autophagic vacuoles in these cells, too. JHa treatment, when started on the 2nd or 3rd day of the last larval stage, inhibited both auto- and heterophagy and the fat bodies maintained their larval character. Treatment started on the 4th or 5th day proved either ineffective or lethal. It is concluded that the auto- and heterophagy taking place in the larval fat body cells are stimulated by ecdysterone and inhibited by JHa. Experiments performed in vitro or on ligated animals in vivo provided evidence for a direct action of ecdysterone at the cellular level.

Adipose Tissue↗
PubMedDate not supplied

[Immunomodulating effect of ecdysterones].

Ecdysterone, its 20-desoxy-derivative alpha-ecdysone, their 2-desoxy-derivatives ecdysterone 2, 3, 22-triacetate and preparation BTI-4 have been studied for their effect on [3H]-thymidine incorporation in different populations of animal and human lymphocytes. It is shown the ecdysteron and its analogs in concentrations of 10(-12)-10(-5) M take considerable stimulating effect on DNA biosynthesis in animal lymphocytes activated by polyclonal mitogens. The concentration of ecdysterone being increased to 10(-4) m one can observe complete inhibition of activating effect of polyclonal mitogens. Effect of the studied ecdysteroids did not considerably depend on their structure. In case of splenocytes the stimulating effect of ecdysterone on DNA biosynthesis is less expressed than in the case of activated thymocytes. Ecdysterone was established to have considerable inhibiting effect on DNA biosynthesis in the culture of activated Con A cells of lymphocytes in the peripheral blood of healthy donors.

Animals↗
PubMed1975

Influence of ecdysterone on the growth of cells and synthesis of macromolecules in established cell lines of Drosophila melanogaster.

Ecdysterone (beta-ecdysone) and 2-deoxy-alpha-ecdysone specifically inhibit the growth of established embryonic cells of D. melanogaster. A preparation of alpha-ecdysone is 100 times less active than ecdysterone. The action of ecdysterone is eliminated when it is removed within 24 h, but after 48 h the inhibiting influence of the hormone becomes irreversible. The diploid line, triploid and tetraploid sublines are sensitive to ecdysterone. The diploid subline with a spontaneously arisen translocation of an X-chromosome to an autosome of the third pair is substantially more resistant to ecdysterone. At 24 h after the addition of ecdysterone, there is a 2-5-fold suppression of the synthesis of total RNA; DNA synthesis is lowered to the same degree only after 48 h. The gross synthesis of proteins, measured according to the incorporation of C 14-lysine, was not suppressed even after 48 h.

Animals↗
PubMed1991

Effect of ecdysterone on histamine release from rat peritoneal mast cells.

Ecdysterone dose-dependently inhibited anti-IgE-induced histamine release from mast cells. Moreover, the rate and extent of histamine release from mast cells induced by Concanavalin A (Con A) are significantly diminished in samples incubated with ecdysterone. Ecdysterone inhibited both the initial and gradual rise in fluorescent response by anti-IgE and Con A. The effects of ecdysterone on the fluorescence response was correlated with the inhibition of histamine release. These results suggest the possibility that the inhibition of histamine release from rat mast cells by ecdysterone might be due to inhibition of Ca2+ mobilization from intracellular Ca2+ storage.

Animals↗
PubMed1981

Photoinduced bonding of endogenous ecdysterone to salivary gland chromosomes of Chironomus tentans.

Endogenous ecdysterone has been bonded to chromosomal loci by irradiation of Ch. tentans salivary glands. The hormone has been localized on the polytene chromosomes by indirect immunofluorescence microscopy. Hormone binding to chromosomes is stage-specific. Seven chromosomal loci could be identified which specifically bound hormone in larval salivary glands, and 21 chromosomal loci which specifically bound hormone in prepupal salivary glands. All puffs that have been described by Clever (1961) as being inducible by ecdysterone have been found to contain irreversibly bound ecdysterone in prepupal salivary gland chromosomes. A small number of puff sites in larval salivary gland chromosomes exhibited varying amounts of bound ecdysterone, (as judged by fluorescence intensity) most notably 117B and Balbiani rings 1 and 3 on chromosome IV. In addition to stage specific binding sites, there were many others showing equal binding of the hormone in both, larval and prepupal, stages of development.--Fluorescence intensities (reflecting the amount of bonded hormone) at puff sites along the tip section of the prepupal salivary gland chromosome arm IR have been computed indicating that differences between fluorescence intensities of different puffs can be expressed as multiples of a basic fluorescence intensity. Thus, the amount of fluorescence intensity (bonded hormone) in the various puffs may be quantized.--The data indicate that in Ch. tentans salivary glands ecdysterone acts, at the chromosomal level. The development of larvae into prepupae generates more puff sites and more hormone binding. This is discussed in the light of current models of hormone-receptor function.

Animals↗
PubMed1982

Ecdysterone induced protein synthesis in salivary glands and in fat body of Drosophila melanogaster larvae.

Salivary glands of 3rd instar larvae of Drosophila melanogaster were labeled with 3H-leucine in the presence and absence of ecdysterone. Twenty-six ecdysterone inducible proteins were detected. Their induction was correlated with puff stage. Synthesis of fifteen proteins commenced during early puff stage (PS2); synthesis of seven others at late puff stages (PS8-10). Synthesis of four proteins was induced between puff stage 3/4 and 7/8. Thus, the hormonal induction of protein synthesis generally reflected the appearance of early and of late puffs as described by Ashburner (1972). Eleven ecdysterone inducible proteins were detected in larval fat body in vitro. Comparison of the fat body to the salivary gland proteins revealed that one of the ecdysterone induced fat body proteins was identical in molecular weight and charge to one of the proteins induced by ecdysterone in salivary glands.

Adipose Tissue↗
PubMed1988

Trans-regulation of ecdysterone-induced protein synthesis in Drosophila melanogaster salivary glands.

A set of coordinately expressed genes is actively transcribed after a dramatic increase in the ecdysterone titer in late third-instar development of Drosophila melanogaster, as shown by the appearance of a number of puffs in salivary gland chromosomes and by the synthesis of a number of new proteins. Previous work has suggested that a product of the ecs gene, which is located within the 2B3-5 puff, is necessary for providing alterations in transcriptional activity at the sites of ecdysterone-dependent puffs. The experiments reported here were designed to determine whether the ecs gene's regulatory effect on puffing is confirmed by its regulatory effect on the synthesis of ecdysterone-inducible proteins (EIPs). The first series of experiments showed that in salivary glands in vivo ecdysterone induces 24 EIPs and in vitro induces 26 EIPs. The sets of polypeptides revealed are in good conformity. The second set of experiments demonstrated that mutations in the ecs locus disturb EIP synthesis: ecsl(1)t10 and ecsl(1)t143 mutations affect EIP synthesis to a lesser extent, while ecsl(1)t435 and ecsl(1)t324, as well as the 2B3-5 puff deficiency, prevent EIP synthesis completely. The experiments on dosage dependency revealed two EIPs whose rate of synthesis correlates with the dosage of the 2B3-5 X-chromosomal region. These EIPs are shown to be in fact small heat-shock proteins 23 and 28K, which are known to be encoded within the 67B puff and are under dual control--transient and developmental. The final set of experiments followed the 2B3-5 dosage dependency in vitro and showed that 15 EIPs display either an affected rate of synthesis or, mainly, a quicker induction time. Data obtained show that the ecs locus is trans-regulatory and that its product is necessary for spreading the effect of ecdysterone to other loci.

Animals↗
PubMed1988

The role of JH III and ecdysterone in the regulation of the left colleterial gland activities in Periplaneta americana during the reproductive cycle.

We studied the in vitro effects of JH III and ecdysterone on RNA synthesis and secretory activities of the left colleterial gland (LCG) in mature females of Periplaneta americana during the reproductive cycle. We found that RNA synthesis is a cyclic and highly dynamic process. The major increases in poly(A)- RNA synthesis occurred 8 hr before the peak leucine incorporation into colleterial polypeptides, whereas high poly(A)+ RNA synthesis coincided with high leucine incorporation. Depending on the stage of the cycle JH III exhibited stimulatory or inhibitory effects, or caused no change in RNA synthesis. JH III stimulated RNA synthesis in glands from stages in the reproductive cycle with high endogenous RNA synthesis. The pattern of protein synthesis was not affected by JH III. Ecdysterone lowered RNA synthesis in the LCG and induced secretory activity in LCGs isolated at stages far removed from ovulation. JH III reduced the inhibitory effect of ecdysterone on RNA synthesis and inhibited the ecdysterone-induced secretory activity. The presence of ovarioles isolated at 62 hr of the reproductive cycle (onset of in vivo LCG secretory activity) in the incubation medium inhibited RNA synthesis in 32 hr LCG but induced secretory activity. We suggest that changes in synthetic and secretory activities are coordinated with ovulation and ootheca formation through the interactions between JH III and ovarioles, and ecdysterone may also play a role.

Animals↗
PubMed1985

Alterations in rat lipid metabolism following ecdysterone treatment.

The influence of ecdysterone on the lipid metabolism in liver and adipose tissue from rat was investigated using 14C-acetate and 32P-orthophosphate as precursors. Ecdysterone produced an increase in 14C-acetate incorporation into triglycerides. A concomitant decrease in free fatty acids and diglycerides was observed. The effect of ecdysterone on triglyceride lipase activity was investigated and a significant decrease was found. Ecdysterone produced a significant increase in the specific activity of phosphatidylethanolamine and phosphatidylserine in liver. On the contrary, the specific activity of phosphatidylcholine was reduced. In adipose tissue, the most evident effect observed was the increase of specific activity of phosphatidylcholine. These results contribute to knowledge of the heterophylic action of ecdysterone.

Acetates↗