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  1 / 63 MEDLINE  
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PMID:27642094
Author:S V; C J; K C S; Jose S; Jose B; Philip R; I S BS
Address:National Centre for Aquatic Animal Health, Cochin University of Science and Technology, Cochin 682 016, India.
Title:Regulating gonad inhibition and vitellogenin/vitellin induction in Penaeus monodon using mature GIH fusion protein and polyclonal antisera.
Source:Comp Biochem Physiol A Mol Integr Physiol; 203:167-178, 2017 Jan.
ISSN:1531-4332
Country of publication:United States
Language:eng
Abstract:Gonad inhibiting hormone (GIH), type II class of the CHH family neuropeptides, is released by the neurohaemal XO-SG complex of the eyestalk. The inhibitory function of GIH has a pivotal role in gonad development and reproduction. In this study, we report the expression and production of a thioredoxin-fused mature GIH protein (mf-PmGIH) of Penaeus monodon in a bacterial system and its use as antigen to raise polyclonal antiserum (anti-mf-PmGIH). The mature GIH gene of 237bp that codes for 79 amino acids, was cloned into the Escherichia coli thioredoxin gene fusion expression system. The expression vector construct (mf-PmGIH+pEt32a+) upon induction produced 32.16kDa mature GIH fusion protein (mf-PmGIH)·The purified fusion protein was used as exogenous GIH and as antigen to raise polyclonal antisera. The fusion protein when injected into juvenile shrimp significantly reduced vitellogenin/vitellin levels by 31.55% within 72h in comparison to the controls showing the gonad inhibiting property. Vitellogenin/vitellin levels were significantly induced by 74.10% within 6h when polyclonal antiserum (anti-mf-PmGIH - 1:500) was injected in P. monodon. Anti-mf-PmGIH immunolocalized GIH producing neurosecretory cells in the eyestalk of P. monodon. The present manuscript reports an innovative means of gonad inhibition and vitellogenin/vitellin induction with thioredoxin fused GIH and antisera developed.
Publication type:JOURNAL ARTICLE
Name of substance:0 (Antibodies, Neutralizing); 0 (Arthropod Proteins); 0 (Carrier Proteins); 0 (Escherichia coli Proteins); 0 (Invertebrate Hormones); 0 (Recombinant Fusion Proteins); 0 (Reproductive Control Agents); 0 (Vitellins); 0 (Vitellogenins); 138360-48-2 (vitellogenesis inhibiting hormone); 52500-60-4 (Thioredoxins)


  2 / 63 MEDLINE  
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PMID:27452121
Author:Wang J; Peng YD; He C; Wei BY; Liang YS; Yang HL; Wang Z; Stanley D; Song QS
Address:College of Bioscience and Biotechnology, Hunan Agriculture University, Changsha, Hunan 410128, China.
Title:Cry1Ab-expressing rice did not influence expression of fecundity-related genes in the wolf spider Pardosa pseudoannulata.
Source:Gene; 592(1):1-7, 2016 Oct 30.
ISSN:1879-0038
Country of publication:Netherlands
Language:eng
Abstract:The impact of Bacillus thuringiensis (Bt) toxin proteins on non-target predatory arthropods is not well understood at the cellular and molecular levels. Here, we investigated the potential effects of Cry1Ab expressing rice on fecundity of the wolf spider, Pardosa pseudoannulata, and some of the underlying molecular mechanisms. The results indicated that brown planthoppers (BPHs) reared on Cry1Ab-expressing rice accumulated the Cry toxin and that reproductive parameters (pre-oviposition period, post-oviposition stage, number of eggs, and egg hatching rate) of the spiders that consumed BPHs reared on Bt rice were not different from those that consumed BPHs reared on the non-Bt control rice. The accumulated Cry1Ab did not influence several vitellin (Vt) parameters, including stored energy and amino acid composition, during one generation. We considered the possibility that the Cry toxins exert their influence on beneficial predators via more subtle effects detectable at the molecular level in terms of gene expression. This led us to transcriptome analysis to detect differentially expressed genes in the ovaries of spiders exposed to dietary Cry1Ab and their counterpart control spiders. Eight genes, associated with vitellogenesis, vitellogenin receptor activity, and vitellin membrane formation were not differentially expressed between ovaries from the treated and control spiders, confirmed by qPCR analysis. We infer that dietary Cry1Ab expressing rice does not influence fecundity, nor expression levels of Vt-associated genes in P. pseudoannulata.
Publication type:JOURNAL ARTICLE
Name of substance:0 (Bacterial Proteins); 0 (Cry toxin receptors, Bacillus thuringiensis); 0 (Receptors, Cell Surface); 0 (Vitellins)


  3 / 63 MEDLINE  
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PMID:27056273
Author:Wang J; Collins JJ
Address:Department of Pharmacology, UT Southwestern Medical Center, Dallas, TX 75390, USA.
Title:Identification of new markers for the Schistosoma mansoni vitelline lineage.
Source:Int J Parasitol; 46(7):405-10, 2016 06.
ISSN:1879-0135
Country of publication:England
Language:eng
Abstract:Schistosomes cause significant morbidity and mortality in millions of the world's poorest people. While parasite egg-induced inflammation is the primary driver of host pathology, relatively little is known at the molecular level about the organ systems that participate in schistosome egg production (i.e., testes, ovaries and vitellaria). Here we use transcriptional profiling and in situ hybridization to characterise the vitellarium of Schistosoma mansoni. We uncovered several previously uncharacterised vitellaria-specific factors and defined molecular markers for various stages in the vitellocyte differentiation process. These data provide the framework for future in-depth molecular studies exploring the biology of this important parasite organ.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
Name of substance:0 (Biomarkers); 0 (RNA, Helminth); 0 (Vitellins)


  4 / 63 MEDLINE  
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PMID:26728459
Author:Wu Z; Guo W; Xie Y; Zhou S
Address:From the School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, China.
Title:Juvenile Hormone Activates the Transcription of Cell-division-cycle 6 (Cdc6) for Polyploidy-dependent Insect Vitellogenesis and Oogenesis.
Source:J Biol Chem; 291(10):5418-27, 2016 Mar 04.
ISSN:1083-351X
Country of publication:United States
Language:eng
Abstract:Although juvenile hormone (JH) is known to prevent insect larval metamorphosis and stimulate adult reproduction, the molecular mechanisms of JH action in insect reproduction remain largely unknown. Earlier, we reported that the JH-receptor complex, composed of methoprene-tolerant and steroid receptor co-activator, acts on mini-chromosome maintenance (Mcm) genes Mcm4 and Mcm7 to promote DNA replication and polyploidy for the massive vitellogenin (Vg) synthesis required for egg production in the migratory locust (Guo, W., Wu, Z., Song, J., Jiang, F., Wang, Z., Deng, S., Walker, V. K., and Zhou, S. (2014) PLoS Genet. 10, e1004702). In this study we have investigated the involvement of cell-division-cycle 6 (Cdc6) in JH-dependent vitellogenesis and oogenesis, as Cdc6 is essential for the formation of prereplication complex. We demonstrate here that Cdc6 is expressed in response to JH and methoprene-tolerant, and Cdc6 transcription is directly regulated by the JH-receptor complex. Knockdown of Cdc6 inhibits polyploidization of fat body and follicle cells, resulting in the substantial reduction of Vg expression in the fat body as well as severely impaired oocyte maturation and ovarian growth. Our data indicate the involvement of Cdc6 in JH pathway and a pivotal role of Cdc6 in JH-mediated polyploidization, vitellogenesis, and oogenesis.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Name of substance:0 (Cdc6 protein, Drosophila); 0 (Cell Cycle Proteins); 0 (Drosophila Proteins); 0 (Juvenile Hormones); 0 (Vitellins)


  5 / 63 MEDLINE  
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PMID:26546815
Author:Kayser H; Nimtz M; Ringler P; Müller SA
Address:Institute of General Zoology and Endocrinology, Ulm University, Helmholtzstrasse 8/1, 89081, Ulm, Germany. Electronic address: hartmut.kayser@uni-ulm.de.
Title:Very high-density lipoprotein and vitellin as carriers of novel biliverdins IXα with a farnesyl side-chain presumably derived from heme A in Spodoptera littoralis.
Source:Insect Biochem Mol Biol; 68:41-51, 2016 Jan.
ISSN:1879-0240
Country of publication:England
Language:eng
Abstract:Bilins in complex with specific proteins play key roles in many forms of life. Biliproteins have also been isolated from insects; however, structural details are rare and possible functions largely unknown. Recently, we identified a high-molecular weight biliprotein from a moth, Cerura vinula, as an arylphorin-type hexameric storage protein linked to a novel farnesyl biliverdin IXα; its unusual structure suggests formation by cleavage of mitochondrial heme A. In the present study of another moth, Spodoptera littoralis, we isolated two different biliproteins. These proteins were identified as a very high-density lipoprotein (VHDL) and as vitellin, respectively, by mass spectrometric sequencing. Both proteins are associated with three different farnesyl biliverdins IXα: the one bilin isolated from C. vinula and two new structurally closely related bilins, supposed to be intermediates of heme A degradation. The different bilin composition of the two biliproteins suggests that the presumed oxidations at the farnesyl side-chain take place mainly during egg development. The egg bilins are supposedly transferred from hemolymph VHDL to vitellin in the female. Both biliproteins show strong induced circular dichroism activity compatible with a predominance of the M-conformation of the bilins. This conformation is opposite to that of the arylphorin-type biliprotein from C. vinula. Electron microscopy of the VHDL-type biliprotein from S. littoralis provided a preliminary view of its structure as a homodimer and confirmed the biochemically determined molecular mass of ∼350 kDa. Further, images of S. littoralis hexamerins revealed a 2 × 3 construction identical to that known from the hexamerin from C. vinula.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Name of substance:0 (Carrier Proteins); 0 (Lipoproteins, HDL); 0 (Vitellins); 0 (very high density lipoproteins); 18535-39-2 (heme a); 42VZT0U6YR (Heme); 4602-84-0 (Farnesol); O9MIA842K9 (Biliverdine)


  6 / 63 MEDLINE  
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PMID:26111116
Author:Paes MC; Silveira AB; Ventura-Martins G; Luciano M; Coelho MG; Todeschini AR; Bianconi ML; Atella GC; Silva-Neto MA
Address:Laboratório de Interação Tripanossomatídeos e Vetores, Departamento de Bioquímica, Instituto de Biologia Roberto Alcântara Gomes (IBRAG), Universidade do Estado do Rio de Janeiro (UERJ), Rio de Janeiro, RJ, Brasil.
Title:CALCIUM-INDUCED LIPID PEROXIDATION IS MEDIATED BY RHODNIUS HEME-BINDING PROTEIN (RHBP) AND PREVENTED BY VITELLIN.
Source:Arch Insect Biochem Physiol; 90(2):104-15, 2015 Oct.
ISSN:1520-6327
Country of publication:United States
Language:eng
Abstract:Lipid peroxidation is promoted by the quasi-lipoxygenase (QL) activity of heme proteins and enhanced by the presence of free calcium. Unlike mammalian plasma, the hemolymph of Rhodnius prolixus, a vector of Chagas disease, contains both a free heme-binding protein (RHBP) and circulating lipoproteins. RHBP binds and prevents the heme groups of the proteins from participating in lipid peroxidation reactions. Herein, we show that despite being bound to RHBP, heme groups promote lipid peroxidation through a calcium-dependent QL reaction. This reaction is readily inhibited by the presence of ethylene glycol tetraacetic acid (EGTA), the antioxidant butylated hydroxytoluene or micromolar levels of the main yolk phosphoprotein vitellin (Vt). The inhibition of lipid peroxidation is eliminated by the in vitro dephosphorylation of Vt, indicating that this reaction depends on the interaction of free calcium ions with negatively charged phosphoamino acids. Our results demonstrate that calcium chelation mediated by phosphoproteins occurs via an antioxidant mechanism that protects living organisms from lipid peroxidation.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Name of substance:0 (Carrier Proteins); 0 (Hemeproteins); 0 (Insect Proteins); 0 (Vitellins); 0 (heme-binding protein); SY7Q814VUP (Calcium)


  7 / 63 MEDLINE  
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PMID:26091289
Author:Leyria J; Fruttero LL; Nazar M; Canavoso LE
Address:Departamento de Bioquímica Clínica, Centro de Investigaciones en Bioquímica Clínica e Inmunología (CIBICI-CONICET), Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Córdoba, CP 5000, Argentina.
Title:The Role of DmCatD, a Cathepsin D-Like Peptidase, and Acid Phosphatase in the Process of Follicular Atresia in Dipetalogaster maxima (Hemiptera: Reduviidae), a Vector of Chagas' Disease.
Source:PLoS One; 10(6):e0130144, 2015.
ISSN:1932-6203
Country of publication:United States
Language:eng
Abstract:In this work, we have investigated the involvement of DmCatD, a cathepsin D-like peptidase, and acid phosphatase in the process of follicular atresia of Dipetalogaster maxima, a hematophagous insect vector of Chagas' disease. For the studies, fat bodies, ovaries and hemolymph were sampled from anautogenous females at representative days of the reproductive cycle: pre-vitellogenesis, vitellogenesis as well as early and late atresia. Real time PCR (qPCR) and western blot assays showed that DmCatD was expressed in fat bodies and ovaries at all reproductive stages, being the expression of its active form significantly higher at the atretic stages. In hemolymph samples, only the immunoreactive band compatible with pro-DmCatD was observed by western blot. Acid phosphatase activity in ovarian tissues significantly increased during follicular atresia in comparison to pre-vitellogenesis and vitellogenesis. A further enzyme characterization with inhibitors showed that the high levels of acid phosphatase activity in atretic ovaries corresponded mainly to a tyrosine phosphatase. Immunofluorescence assays demonstrated that DmCatD and tyrosine phosphatase were associated with yolk bodies in vitellogenic follicles, while in atretic stages they displayed a different cellular distribution. DmCatD and tyrosine phosphatase partially co-localized with vitellin. Moreover, their interaction was supported by FRET analysis. In vitro assays using homogenates of atretic ovaries as the enzyme source and enzyme inhibitors demonstrated that DmCatD, together with a tyrosine phosphatase, were necessary to promote the degradation of vitellin. Taken together, the results strongly suggested that both acid hydrolases play a central role in early vitellin proteolysis during the process of follicular atresia.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Name of substance:0 (Insect Proteins); 0 (Vitellins); EC 3.1.3.2 (Acid Phosphatase); EC 3.4.23.5 (Cathepsin D)


  8 / 63 MEDLINE  
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PMID:25641503
Author:Yoneva A; Scholz T; Brunanská M; Kuchta R
Address:Institute of Biodiversity and Ecosystem Research, Bulgarian Academy of Sciences, 2, Gagarin Street, 1113 Sofia, Bulgaria; Institute of Parasitology, Biology Centre of the Czech Academy of Sciences, Branisovská 31, 370 05 Ceské Budejovice, Czech Republic. Electronic address: anetayoneva@gmail.com.
Title:Vitellogenesis of diphyllobothriidean cestodes (Platyhelminthes).
Source:C R Biol; 338(3):169-79, 2015 Mar.
ISSN:1768-3238
Country of publication:France
Language:eng
Abstract:The recently erected cestode order Diphyllobothriidea is unique among all tapeworm orders in that its species infect all major groups of tetrapods, including man. In the present paper, the vitellogenesis of representatives of all three currently recognized families of this order was evaluated, based on ultrastructural (transmission electron microscopy) and cytochemical (detection of glycogen) observations. Vitelline follicles of all taxa studied, i.e. Cephalochlamys namaquensis from clawed frogs (Xenopus), Duthiersia expansa from monitors (Varanus) and Schistocephalus solidus that matures in fish-eating birds, contain vitelline cells at various stages of development and interstitial cells. Developing vitellocytes are characterized by the presence of mitochondria, granular endoplasmic reticulum and Golgi complexes involved in the synthesis of shell globules and formation of shell globule clusters. Mature vitellocytes contain lipids and glycogen in different proportions. The most significant differences among the three diphyllobothriidean families were found in the presence or absence of lamellar bodies. Variations of vitelline clusters morphology and types of lipid droplets are described and discussed in relation to the presumed evolutionary history of diphyllobothriideans, which belong to the most basal cestode groups.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Name of substance:0 (Lipids); 0 (Vitellins); 9005-79-2 (Glycogen)


  9 / 63 MEDLINE  
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PMID:25524510
Author:Yang X; Yu Z; He Y; Xu X; Gao Z; Wang H; Chen J; Liu J
Address:Key Laboratory of Animal Physiology, Biochemistry and Molecular Biology of Hebei Province, College of Life Sciences, Hebei Normal University, Shijiazhuang, 050024, China.
Title:Purification of vitellin and dynamics of vitellogenesis in the parthenogenetic tick Haemaphysalis longicornis (Acari: Ixodidae).
Source:Exp Appl Acarol; 65(3):377-88, 2015 Mar.
ISSN:1572-9702
Country of publication:Netherlands
Language:eng
Abstract:Vitellin (Vt) was purified from eggs of parthenogenetic bush tick Haemaphysalis longicornis by gel filtration and ion exchange chromatography. Our results revealed that only one single Vt existed in parthenogenetic bush tick, and the purified Vt was proved to be a hemoglycolipoprotein consisting of nine polypeptides with molecular weights of 203, 147, 126, 82, 74, 70, 61, 47 and 31 kDa, respectively. Polyclonal antibody and monoclonal antibody against Vt were produced using the purified Vt. The change in vitellogenin (Vg) and Vt levels over time of the parthenogenetic H. longicornis was established, and the Vg content in haemolymph and Vt in ovary at different feeding or engorgement statuses was also determined using a double antibody sandwich enzyme-linked immunosorbent assay. The Vg level in haemolymph was distinctly increased on the day of engorgement (1.785 mg/mL) and continued to increase until 2nd day post-engorgement (5.611 mg/mL). There was a slight decrease in Vg level after 4 days of engorgement, and a second peak was observed on day 2 post-oviposition (10.774 mg/mL). Subsequently, Vg content continuously decreased and reached a low level on the 10th day post-oviposition. The Vt content in ovary continuously increased once the female reached its critical weight (0.024 mg per female), and reached the maximum level on day 2 post-oviposition (1.942 mg per female). Afterwards, Vt content rapidly decreased.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Name of substance:0 (Antibodies, Monoclonal); 0 (Vitellins)


  10 / 63 MEDLINE  
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PMID:25121096
Author:Peranandam R; Palanisamy I; Lourdaraj AV; Natesan M; Vimalananthan AP; Thangaiyan S; Perumal A; Muthukalingan K
Address:Department of Environmental Biotechnology, Bharathidasan University, Trichy, Tamil Nadu 620 024, India.
Title:TBT effects on the development of intersex (ovotestis) in female fresh water prawn Macrobrachium rosenbergii.
Source:Biomed Res Int; 2014:412619, 2014.
ISSN:2314-6141
Country of publication:United States
Language:eng
Abstract:The impact of tributyltin (TBT) on the female gonad and the endocrine system in Macrobrachium rosenbergii was studied. Prawns were exposed to environmentally realistic concentrations of 10, 100, and 1000 ng/L of TBT for 6 months. Dose dependent effects were noticed in TBT exposed prawns. At 1000 ng/L TBT caused ovotestis formation (formation of male germ cells in ovary). Presence immature oocytes, fusion of developing oocytes, increase in interstitial connective tissues, and its modification into tubular like structure and abundance of spermatogonia in the ovary of TBT treated prawns. The control prawn ovary showed normal architecture of cellular organelles such as mature oocytes with type 2 yolk globules, lipid droplets, normal appearance of yolk envelop, and uniformly arranged microvilli. On the other hand, type 1 yolk globules, reduced size of microvilli, spermatogonial cells in ovary, spermatogonia with centrally located nucleus, and chromatin distribution throughout the nucleoplasm were present in the TBT treated group. Immunofluorescence staining indicated a reduction in vitellin content in ovary of TBT treated prawn. Moreover, TBT had inhibited the vitellogenesis by causing hormonal imbalance in M. rosenbergii. Thus, the present investigation demonstrates that TBT substantially affects sexual differentiation and gonadal development in M. rosenbergii.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Name of substance:0 (Biomarkers); 0 (Gonadal Steroid Hormones); 0 (Trialkyltin Compounds); 0 (Vitellins); 0 (Vitellogenins); 4XDX163P3D (tributyltin)



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