Insect Biochemistry最新文献

{"title":"Cyanoprotein: Quantitative changes and synthesis in diapause and juvenile hormone analog treated bean bug, Riptortus clavatus","authors":"Ken Miura ,&nbsp;Yasuo Chinzei ,&nbsp;Tetsuro Shinoda ,&nbsp;Hideharu Numata","doi":"10.1016/0020-1790(91)90110-Z","DOIUrl":"10.1016/0020-1790(91)90110-Z","url":null,"abstract":"<div><p>Quantitative changes of cyanoproteins (CPs) in diapause and juvenile hormone (JH) analog treated bean bug, <em>Riptortus clavatus</em>, were analyzed by rocket immunoelectrophoresis (RIE). In diapause-oriented nymphal females and males, CP-A (CP-1, 2 and 3) and CP-B (CP-4) increased and reached a maximum level just before nymphal-adult ecdysis, which was the same in non-diapause female and male nymphs. Both CP-A and B disappeared immediately after adult emergence. After this initial decline CP-4 appeared again in the hemolymph, followed after a few days by CP-1, 2 and 3. CP-A and B then increased slowly but constantly in both diapause female and male adults. Both diapause females and males at day 30 after adult emergence had large amounts of CP-A (CP-1, 2 and 3) and CP-B (CP-4). Treatment of diapause females (day 30) with methoprene induced only CP-1 synthesis and increased CP-A content about twice in both the whole body and the hemolymph, but did not effect on CP-B content. Methoprene treated females developed ovaries which accumulated yolk containing CPegg and vitellin (Vn). In diapause males treated with methoprene CP-A and B were not induced and decreased gradully in concentration, eventually disappearing completely, similar to post-diapause males (30 days after transferred to long day condition) in which CPs were not detected. These results show that methoprene treatment of diapause females and males induced the same dynamical situations of CP-A and B seen in non-diapause adults, i.e. only CP-A was induced in females and CPs disappeared in males. This suggests that CP synthesis is regulated by juvenile hormone.</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 5","pages":"Pages 553-562"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-1790(91)90110-Z","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75556357","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Immunodetection of phosphotyrosine-containing proteins in the integument, fat body and haemocytes of the mediterranean fruit-fly Ceratitis capitata: Possible involvement in pupariation","authors":"Panagiotis G. Katsoris,&nbsp;Sotiris Tsakas,&nbsp;Stavros N. Bournazos,&nbsp;Vassilis J. Marmaras","doi":"10.1016/0020-1790(91)90088-V","DOIUrl":"10.1016/0020-1790(91)90088-V","url":null,"abstract":"<div><p>Antibodies raised against the synthetic hapten <span><math><mtext>p-</mtext><mtext>azobenzyl</mtext></math></span> phosphonate (ABP), which specifically cross react with phosphotyrosine, were used to detect phosphotyrosine-containing proteins in integument, fat body, and haemocytes of <em>C. capitata</em> white pupae. Immunofluorescence experiments demonstrated that fat body, integument, and haemocytes contained proteins phosphorylated in tyrosine residues, while other tissues, such as muscle, showed no fluorescence. To determine which polypeptides are recognized by ABP antibodies, an immunoblotting analysis was performed. The results revealed that the majority of the immunoreactive polypeptide with a <span><math><mtext>M</mtext><msub><mi></mi><mn><mtext>r</mtext></mn></msub></math></span> ranging between 35- and 130 kDa were detected in the integument of <em>C. capitata</em>. Three immunoreactive polypeptides seem to be common in tissues we have examined. 130 kDa is common in integument and fat body, 98 kDa in integument and haemocytes, and 93 kDa is common in haemocytes and fat body. Solubilization of integumental proteins in Tris-HCl buffer pH 7.2 containing either KCl, or NaCl, or urea, or swittergen shows that several phosphotyrosine-containing proteins form non-covalent links with other cuticular components and/or cytoskeleton. Furthermore, treatment of unsolubilized fraction with lysozyme, indicated that some N-acetylglucosamine-containing material prevents extraction with salt solution; this material may be chitin or some intracellular material. The possible contribution of phosphotyrosine containing proteins in the pupariation process is discussed.</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 8","pages":"Pages 815-824"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-1790(91)90088-V","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86585080","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Studies on the subcellular distribution of (Na+ + K+)-ATPase, K+-stimulated ATPase and HCO3−-stimulated ATPase activities in malpighian tubules of Locusta migratoria L.","authors":"K.E. Fogg,&nbsp;J.H. Anstee,&nbsp;D. Hyde","doi":"10.1016/0020-1790(91)90116-V","DOIUrl":"https://doi.org/10.1016/0020-1790(91)90116-V","url":null,"abstract":"","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 7","pages":"749-758"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-1790(91)90116-V","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72261728","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Dietary ascorbic acid, pyridoxine and riboflavin reduce the light sensitivity of larvae and pupae of Drosophila melanogaster","authors":"B.G. Bruins,&nbsp;W. Scharloo,&nbsp;G.E.W. Thörig","doi":"10.1016/0020-1790(91)90108-Q","DOIUrl":"10.1016/0020-1790(91)90108-Q","url":null,"abstract":"<div><p><em>Drosophilia melanogaster</em> is light sensitive. On low yeast media, light induces high mortality during the development from egg to adulthood and increases development time. This effect of light is strongly dependent on the yeast-concentration. Addition of 8 vitamins, normally present in yeast, protects <em>Drosophila</em> against light under laboratory conditions. In this study we have analyzed the significance of the individual vitamins for both survival and development at high light intensities. Two <em>D. melanogaster</em> strains were utilized: a control strain C and a strain P. The latter had been adapted to a palmitic acid supplemented medium. In addition, we investigated the effect of vitamin C, a vitamin typically found in fruit, but not in yeast. It appears that both pyridoxine and riboflavin are essential for the survival of the control strain C under high light intensities, and they act synergistically. The other 6 tested vitamins can be omitted in these survival experiments. Moreover survival under high light conditions also improved strongly on media supplemented with vitamin C. The other strain (P), which was for many generations kept on a different food-medium, also was protected on yeast media by riboflavin and pyridoxine, and by vitamin C, although the survival at high light intensities on media with riboflavin and pyridoxine was less than the survival of the control strain.</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 5","pages":"Pages 541-544"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-1790(91)90108-Q","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74698514","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Developmental expression and hormonal regulation of a desiccation stress protein in Tenebrio molitor","authors":"Ernest M. Kroeker ,&nbsp;Virginia K. Walker","doi":"10.1016/0020-1790(91)90033-B","DOIUrl":"10.1016/0020-1790(91)90033-B","url":null,"abstract":"<div><p>In a previous study it has been reported that dsp28 is induced during desiccation in <em>Tenebrio</em> larvae. During that study it was observed that in non-stressed larvae the concentration of dsp28 in hemolymph drops dramatically just prior to pupation. These results suggested that control of dsp28 synthesis is subject to environmental as well as hormonal cues. This study identifies a site of synthesis as fat body, as dsp28 was secreted into the medium during <em>in vitro</em> incubation of larval fat bodies. Using immunoelectrophoresis to determine protein concentration a developmental profile showing changes in levels of dsp28 in hemolymph during larval, pupal and adult stages of <em>Tenebrio molitor</em> was established. The concentration of dsp28 in larval hemolymph dropped from 4 to 5 mg/ml to 1.5 mg/ml just prior to pupation. This lower level was maintained until adults emerged when the concentration of dsp28 rose to prepupal levels again. Hormonal regulation is suggested since application of methoprene to newly-emerged pupae resulted in an increased incorporation of radiolabeled cysteine into dsp28.</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 6","pages":"Pages 631-640"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-1790(91)90033-B","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86451404","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Sequences of two cDNAs and expression of the genes encoding methionine-rich storage proteins of Manduca sexta","authors":"Lolita M. Corpuz ,&nbsp;Hee Choi ,&nbsp;S. Muthukrishnan ,&nbsp;Karl J. Kramer","doi":"10.1016/0020-1790(91)90016-8","DOIUrl":"10.1016/0020-1790(91)90016-8","url":null,"abstract":"<div><p>In <em>Manduca sexta</em>, storage proteins accumulate during the final larval stadium for utilization during subsequent larval-pupal-adult transformations. Two cDNA clones (designated clone 119 and clone 201), that represent two distinct but related genes (42% sequence identity), were isolated from a cDNA library prepared from day 7 fifth instar larval fat body and found to encode two different storage proteins synthesized during the last larval instar. Northern blot analyses revealed that the two clones hybridize to 2.4 kb transcripts that are translated to 79 kDa protein products during <em>in vitro</em> translation experiments. Clone 119 encodes a methionine-rich storage protein, designated as SP1A, that shares 37% sequence identity with the <em>Bombyx mori</em> sex-specific storage protein SP1. Clone 201, on the other hand encodes a storage protein, designated as SP1B, that is more closely related to <em>B. mori</em> SP1 (63% identity), and is probably identical to the <em>Manduca</em> female-specific storage protein (FSP). Insert DNA from clone 201, but not clone 119, cross-hybridizes to that of FSP cDNA (Webb and Riddiford, <em>Dev. Biol.</em><strong>130,</strong> 671–691, 1988a). Both storage proteins are synthesized only in the fat body and only during the fifth larval stadium, indicating tissue- and stage-specific expression of the two genes. Both genes exhibit sex-specific differences in expression. In the fifth larval stadium, the mRNAs for the SP1A and SP1B proteins begin to accumulate at about day 2 in the female fat body but appear 2 or 3 days later in the male fat body. In both sexes SP1A mRNA remains relatively high beyond the time when SP1B mRNA has already declined to low levels, suggesting differences in mRNA stability or expression. Injection of 20-hydroxyecdysone into ligated fifth instar abdomens causes substantial increases in the levels of both mRNAs, whereas topical application of the juvenile hormone mimc, fenoxycarb, to feeding fifth instar larvae produces substantial declines in the mRNA levels, indicating hormonal effects at the transcriptional level. The data support the hypothesis that the expression of these <em>M. sexta</em> methionine-rich storage protein genes is stimulated by ecdysteroid and inhibited by juvenile hormone.</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 3","pages":"Pages 265-276"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-1790(91)90016-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84745673","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"cDNA and deduced amino acid sequence of a blood meal-induced trypsin from the mosquito, Aedes aegypti","authors":"Carolina Barillas-Mury ,&nbsp;Rolf Graf ,&nbsp;Henry H. Hagedorn ,&nbsp;Michael A. Wells","doi":"10.1016/0020-1790(91)90089-W","DOIUrl":"10.1016/0020-1790(91)90089-W","url":null,"abstract":"<div><p>A cDNA for a midgut trypsin induced by a blood meal has been cloned and sequenced from the mosquito <em>Aedes aegypti</em>. The 862 base sequence codes for a 257 amino acid protein, which is presumably a trypsin precursor, since the sequence of purified mosquito trypsin begins at residue 26, immediately following an arginine residue in the precursor. The amino terminal 25 amino acids in the precursor are composed of a putative 15 amino acid signal peptide and a 10 amino acid activation peptide. Compared to vertebrate trypsinogens, the putative mosquito trysinogen lacks the four acidic amino acids immediately preceding the basic amino acid at the activation peptide cleavage site, suggesting the mechanism of its activation may be different from the activation of vertebrate trypsinogens. However, since a trypsinogen has not yet been isolated from the mosquito, these conclusions are tentative. The deduced amino acid sequence is homologous to that of other trypsins in those residues around the catalytic triad, and in several residues which are found only in trypsins. However, the sequence of the specificity pocket in mosquito trypsin, KESPC, differs from that found in other trypins, KDSC. The Asp is thought to bind the basic residue of the substrate, and the Glu in the mosquito trypsin may serve the same role. The changes in trypsin protein and mRNA levels following a blood meal indicate that an important component of the regulation of trypsin synthesis is at the transcriptional level.</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 8","pages":"Pages 825-831"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-1790(91)90089-W","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91248144","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Immunoanalysis of unique protein in Trichoplusia ni larvae parasitized by the braconid wasp Chelonus near curvimaculatus","authors":"Ana I. Soldevila ,&nbsp;Davy Jones","doi":"10.1016/0020-1790(91)90091-R","DOIUrl":"10.1016/0020-1790(91)90091-R","url":null,"abstract":"<div><p>Parasitization in insects brings about profound biochemical and physiological effects in the host which may include complete overriding of the normal endocrinological program, resulting in precocious metamorphosis and in blockage of pupal development. The subtle effects of parasitization include changes in the expression of hemolymph proteins and the appearance of proteins which are unique to parasitized hosts. One such protein has been identified in the hemolymph of <em>Trichoplusia ni</em> larvae parasitized by the braconid wasp <em>Chelonus</em> near <em>curvimaculatus</em>. In this study, purified preparations of the parasitism-specific protein were used to generate polyconal antibodies against the protein. Results from the immunocharacterization indicate the antibodies obtained are highly specific for the protein and are present in a high titer (1:8000 antiserum dilution yielded strong signals in analysis of the protein in 0.25 μl hemolymph). Subsequently, the expression of the parasitism-specific protein in the hemolymph and tissues was analyzed by immunoblotting during the entire course of development in normal and parasitized insects. The parasitism-specific protein was not detected in normal, unparasitized larvae. In parasitized insects, expression of the parasitism-specific protein appears to be stage-specific in that it is only detected during the last larval stadium of precociously metamorphosing larvae, but is absent from all earlier stages of development.</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 8","pages":"Pages 845-856"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-1790(91)90091-R","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79393902","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Enzymes of ecdysteroid 3-epimerization in midgut cytosol of Manduca sexta: pH optima cosubstrate kinetics, and sodium chloride effect","authors":"Gunter F. Weirich,&nbsp;Malcolm J. Thompson,&nbsp;James A. Svoboda","doi":"10.1016/0020-1790(91)90065-M","DOIUrl":"10.1016/0020-1790(91)90065-M","url":null,"abstract":"<div><p>Five enzyme activities in midgut cytosol of <em>Manduca sexta</em> last instar larvae are potentially involved in the interconversion of 3β-hydroxyecdysteroids, 3-oxoecdysteroids, and 3α-hydroxyecdysteroids. A Sephadex G-25-filtered high-speed supernatant was used to determine some of the characteristics of the corresponding enzymes. The pH optima of ecdysone oxidase and NADH-dependent 3-oxoecdysteroid 3α-reductase were 7.5, the pH of the midgut cytosol was 7.9. The apparent kinetic parameters for the NADH-dependent 3α-reductase were <span><math><mtext>K</mtext><msub><mi></mi><mn>m</mn></msub><mtext> (for NADH)</mtext><mtext> = 80.8 ± 10.8</mtext></math></span> μM and <span><math><mtext>V</mtext><msub><mi></mi><mn><mtext>max</mtext></mn></msub><mtext> = 0.58 ± 0.30</mtext></math></span> nmol/min/mg protein, and for the NADPH-dependent 3-oxoecdysteroid 3β-reductase, <span><math><mtext>K</mtext><msub><mi></mi><mn>m</mn></msub><mtext> (for NADPH)</mtext><mtext> = 19.3 ± 2.5</mtext></math></span> μM and <span><math><mtext>V</mtext><msub><mi></mi><mn><mtext>max</mtext></mn></msub><mtext> = 4.39 ± 0.40</mtext></math></span> nmol/min/mg protein. NAD⁺ and NADP⁺ inhibited the enzymatic 3-oxoecdysteroid reductions, but the reactions were not reversible (i.e. no conversion of ecdysone or 3-epiecdysone to 3-dehydroecdysone). Sodium chloride (0.2 M) inhibited the 3α-reductase activity with NADH and strongly increased the 3α-reductase activity with NADPH.</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 1","pages":"Pages 65-71"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-1790(91)90065-M","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75021863","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"5-Hydroxytryptamine metabolism in nervous tissue of two acridids, Oedipoda caerulescens and Paracinema tricolor: A comparative study","authors":"R. Vieira,&nbsp;F. Martín,&nbsp;M. Aldegunde","doi":"10.1016/0020-1790(91)90109-R","DOIUrl":"10.1016/0020-1790(91)90109-R","url":null,"abstract":"<div><p>The concentrations of 5-hydroxytryptamine (5-HT), N-acetyl-5-hydroxytryptamine (NAS), 5-hydroxyindoleacetic acid (5-HIAA) (HPLC-EC) and tryptophan (Trp) were determined in the cerebral ganglia and ventral nerve cord (VNC) of both sexes of two acridids. In both species, the maximum values for all compounds appeared in the brain region, the converse occurring for Trp levels. 5-HT and its metabolites followed in both acridids the same tendency, males showing higher values than females. These male-female differences were markedly significant for NAS and 5-HIAA concentrations in <em>Paracinema tricolor</em>, and for 5-HT concentrations in <em>Oedipoda caerulescens</em>. Both acridids differed for brain concentrations of such compounds. Thus, <em>P. tricolor</em> showed the maximum values for NAS and 5-HIAA and <em>O. caerulescens</em> for 5-HT levels. Furthermore, in both species NAS represented about 75–90% of both catabolic products considered as a whole. The results support the idea of a coexistence of N-acetylation and oxidative deamination in both acridids, with higher importance of the 5-HT N-acetyl derivative. A differential 5-HT turnover between sexes is also suggested.</p></div>","PeriodicalId":13955,"journal":{"name":"Insect Biochemistry","volume":"21 5","pages":"Pages 545-552"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-1790(91)90109-R","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"78963083","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}