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Pesquisa : D06.472.445 [Categoria DeCS]
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  1 / 1804 MEDLINE  
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[PMID]:28935584
[Au] Autor:Liu C; Jia X; Zou Z; Wang X; Wang Y; Zhang Z
[Ad] Endereço:Key Laboratory of Healthy Mariculture for the East China Sea, Ministry of Agriculture, Fisheries College, Jimei University, Xiamen 361021, China.
[Ti] Título:VIH from the mud crab is specifically expressed in the eyestalk and potentially regulated by transactivator of Sox9/Oct4/Oct1.
[So] Source:Gen Comp Endocrinol;255:1-11, 2018 Jan 01.
[Is] ISSN:1095-6840
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Vitellogenesis-inhibiting hormone (VIH) is known to regulate ovarian maturation by suppressing the synthesis of vitellogenin (Vtg) in crustaceans, which belongs to a member of crustacean hyperglycemic hormone (CHH) family synthesized and secreted from the X-organ/sinus gland complex of eyestalks. In this study, the cDNA, genomic DNA (gDNA) and the 5'-upstream regulatory (promoter region) sequences of VIH gene were obtained by conventional PCR, genome walker and tail-PCR techniques according to our transcriptomic database of Scylla paramamosain. The full-length cDNA of SpVIH is 634bp including 105bp 5'UTR, 151bp 3'UTR and 378bp ORF that encodes a peptide of 125 amino acids. The full length gDNA of SpVIH is 790bp containing two exons and one intron. The 5'-flanking promoter regions of SpVIH we isolated are 3070bp from the translation initiation (ATG) and 2398bp from the predicted transcription initiation (A), which consists of putative core promoter region and multiple potential transcription factor binding sites. SpVIH was only expressed in eyestalk. The expression level of SpVIH in eyestalk of female crab decreased gradually along with the development of ovary. As there is not cell line of crabs available, we chose the mature transfection system HEK293FT cell lines to explore the mechanism of transcription regulation of SpVIH in crabs. Sequential deletion assays using luciferase reporter gene in HEK293FT cells revealed that the possible promoter activity regions (including positive and negative transcription factors binding sites simultaneously) presented between pSpVIH-4 and pSpVIH-6. In order to further identify the crucial transcription factors binding site in this region, the site-directed mutagenesis of Sox9/Oct4/Oct1 binding site of pSpVIH-4 was created. The results demonstrated that the transcriptional activity of pSpVIH-4â–³ decreased significantly (p<0.05). Thus, it is reasonable to deduce that the Sox9/Oct4/Oct1 may be the essential positive transcription factors which regulate the expression of SpVIH.
[Mh] Termos MeSH primário: Braquiúros/metabolismo
Proteínas de Transporte/metabolismo
Olho/metabolismo
Hormônios de Invertebrado/metabolismo
Fator 1 de Transcrição de Octâmero/metabolismo
Fator 3 de Transcrição de Octâmero/metabolismo
Fatores de Transcrição SOX9/metabolismo
Transativadores/metabolismo
[Mh] Termos MeSH secundário: Região 5'-Flanqueadora/genética
Sequência de Aminoácidos
Animais
Sequência de Bases
Proteínas de Transporte/química
Proteínas de Transporte/genética
DNA Complementar/genética
Feminino
Regulação da Expressão Gênica no Desenvolvimento
Células HEK293
Seres Humanos
Hormônios de Invertebrado/química
Hormônios de Invertebrado/genética
Mutação/genética
Ovário/embriologia
Ovário/metabolismo
Filogenia
Regiões Promotoras Genéticas/genética
Análise de Sequência de DNA
Transgenes
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (DNA, Complementary); 0 (Invertebrate Hormones); 0 (Octamer Transcription Factor-1); 0 (Octamer Transcription Factor-3); 0 (SOX9 Transcription Factor); 0 (Trans-Activators); 138360-48-2 (vitellogenesis inhibiting hormone)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170923
[St] Status:MEDLINE


  2 / 1804 MEDLINE  
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[PMID]:28417205
[Au] Autor:Zhou L; Li S; Wang Z; Li F; Xiang J
[Ad] Endereço:Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao, 266071, China.
[Ti] Título:An eclosion hormone-like gene participates in the molting process of Palaemonid shrimp Exopalaemon carinicauda.
[So] Source:Dev Genes Evol;227(3):189-199, 2017 Jun.
[Is] ISSN:1432-041X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Molting behavior is an important physiological process related to metamorphosis, growth, and reproduction in crustaceans. Previous studies indicated that the molting process was controlled by 20-hydroxyecdysone (20E) and upstream hormones, peptides, and environmental factors, which regulate 20E function. Eclosion hormone (EH) in insect is a kind of neuropeptide that is regulated by 20E and triggers ecdysis behavior at the end of molting process. However, the function of eclosion hormone gene during the molting process in crustaceans is still largely unknown. In the present study, an eclosion hormone-like gene EcEHL was identified from Exopalaemon carinicauda. The deduced amino acid sequence of EcEHL contained a signal peptide, a typical eclosion domain, and six conserved cysteine residues forming three putative disulfide bonds. EcEHL was predominantly expressed in the epidermis, gill, and eyestalk of shrimp. In situ hybridization analysis showed that EcEHL transcripts were localized in gill cells and in medulla externa X-organ, medulla terminalis X-organ, sinus gland, and lamina ganglionaris of eyestalks. During the molting process of shrimp, EcEHL showed the highest expression level in shrimp at the premolt stage. The expression level of EcEHL in shrimp at mid premolt stage was up-regulated by injection of exogenous 20E. Silencing of EcEHL using double-stranded RNA delayed both the molting process and ecdysis rate of E. carinicauda. Furthermore, injection of exogenous 20E to shrimp at mid premolt stage (D2) could remarkably speed up the molting process and also raise the ecdysis rate of E. carinicauda. The results revealed that EcEHL might participate in the molting process of shrimp and its expression was regulated by 20E. These data will help us to understand the molecular mechanism of molting in crustacean.
[Mh] Termos MeSH primário: Hormônios de Invertebrado/genética
Muda
Palaemonidae/crescimento & desenvolvimento
Palaemonidae/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sequência de Bases
Clonagem Molecular
Perfilação da Expressão Gênica
Especificidade de Órgãos
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Invertebrate Hormones)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170419
[St] Status:MEDLINE
[do] DOI:10.1007/s00427-017-0580-9


  3 / 1804 MEDLINE  
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[PMID]:28369112
[Au] Autor:Loredo-Ranjel R; Fanjul-Moles ML; Escamilla-Chimal EG
[Ad] Endereço:Laboratorio de Neurofisiología y Ritmos Biológicos, Departamento de Ecología y Recursos Naturales, Facultad de Ciencias, Universidad Nacional Autónoma de México, Mexico City, Mexico.
[Ti] Título:Crustacean hyperglycemic hormone is synthesized in the eyestalk and brain of the crayfish Procambarus clarkii.
[So] Source:PLoS One;12(4):e0175046, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Crustacean hyperglycemic hormone (CHH) is a neuropeptide that is synthesized, stored, and released by brain and eyestalk structures in decapods. CHH participates in the regulation of several mechanisms, including increasing the level of glucose in hemolymph. Although CHH mRNA levels have been quantified and the CHH protein has been localized in various structures of the crayfish P. clarkii, CHH synthesis has only been reported in the X-organ-sinus gland (XO-SG). Therefore, the aim of this study was to use in situ hybridization to determine whether CHH mRNA is located in other structures, including the putative pacemaker, eyestalk and brain, of crayfish P. clarkii at two times of day. CHH mRNA was observed in both the eyestalk and the brain of P. clarkii, indicating that CHH is synthesized in several structures in common with other crustaceans, possibly to provide metabolic support for these regions by increasing glucose levels.
[Mh] Termos MeSH primário: Proteínas de Artrópodes/metabolismo
Astacoidea/metabolismo
Encéfalo/metabolismo
Olho/metabolismo
Hormônios de Invertebrado/metabolismo
Proteínas do Tecido Nervoso/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas de Artrópodes/genética
Relógios Circadianos/fisiologia
Ritmo Circadiano/fisiologia
Glucose/metabolismo
Hemolinfa/metabolismo
Hibridização In Situ
Hormônios de Invertebrado/genética
Proteínas do Tecido Nervoso/genética
Reação em Cadeia da Polimerase
RNA Mensageiro/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arthropod Proteins); 0 (Invertebrate Hormones); 0 (Nerve Tissue Proteins); 0 (RNA, Messenger); 0 (hyperglycemic hormone, crustacean); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170404
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0175046


  4 / 1804 MEDLINE  
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[PMID]:28207859
[Au] Autor:Li W; Chiu KH; Tien YC; Tsai SF; Shih LJ; Lee CH; Toullec JY; Lee CY
[Ad] Endereço:Department of Biology, National Changhua University of Education, Changhua, Taiwan.
[Ti] Título:Differential effects of silencing crustacean hyperglycemic hormone gene expression on the metabolic profiles of the muscle and hepatopancreas in the crayfish Procambarus clarkii.
[So] Source:PLoS One;12(2):e0172557, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In order to functionally characterize the metabolic roles of crustacean hyperglycemic hormone (CHH), gene expression of CHH in the crayfish (Procambarus clarkii) was knocked down by in vivo injection of CHH double-stranded RNA (dsRNA), followed by metabolomic analysis of 2 CHH target tissues (the muscle and hepatopancreas) using nuclear magnetic resonance spectroscopy. Compared to the levels in untreated and saline-injected (SAI) animals, levels of CHH transcript, but not those of molt-inhibiting hormone (a CHH-family peptide), in the eyestalk ganglia of CHH dsRNA-injected (DSI) animals were significantly decreased at 24, 48, and 72 hour post injection (hpi), with concomitant changes in levels of CHH peptide in the sinus gland (a neurohemal organ) and hemolymph. Green fluorescence protein (GFP) dsRNA failed to affect levels of CHH transcript in the eyestalk ganglia of GFP DSI animals. Number of metabolites whose levels were significantly changed by CHH dsRNA was 149 and 181 in the muscle and 24 and 12 in the hepatopancreas, at 24 and 48 hpi, respectively. Principal component analysis of these metabolites show that metabolic effects of silencing CHH gene expression were more pronounced in the muscle (with the cluster of CHH DSI group clearly being separated from that of SAI group at 24 hpi) than in the hepatopancreas. Moreover, pathway analysis of the metabolites closely related to carbohydrate and energy metabolism indicate that, for CHH DSI animals at 24 hpi, metabolic profile of the muscle was characterized by reduced synthesis of NAD+ and adenine ribonucleotides, diminished levels of ATP, lower rate of utilization of carbohydrates through glycolysis, and a partially rescued TCA cycle, whereas that of the hepatopancreas by unaffected levels of ATP, lower rate of utilization of carbohydrates, and increased levels of ketone bodies. The combined results of metabolic changes in response to silenced CHH gene expression reveal that metabolic functions of CHH on the muscle and hepatopancreas are more diverse than previously thought and are differential between the two tissues.
[Mh] Termos MeSH primário: Proteínas de Artrópodes/antagonistas & inibidores
Astacoidea/metabolismo
Inativação Gênica
Hepatopâncreas/metabolismo
Hormônios de Invertebrado/antagonistas & inibidores
Metaboloma
Músculos/metabolismo
Proteínas do Tecido Nervoso/antagonistas & inibidores
[Mh] Termos MeSH secundário: Animais
Proteínas de Artrópodes/genética
Astacoidea/genética
Metabolismo Energético
Regulação da Expressão Gênica
Hemolinfa/metabolismo
Hormônios de Invertebrado/genética
Proteínas do Tecido Nervoso/genética
RNA de Cadeia Dupla/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arthropod Proteins); 0 (Invertebrate Hormones); 0 (Nerve Tissue Proteins); 0 (RNA, Double-Stranded); 0 (hyperglycemic hormone, crustacean)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170901
[Lr] Data última revisão:
170901
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170217
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0172557


  5 / 1804 MEDLINE  
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[PMID]:28089897
[Au] Autor:Wang L; Chen H; Xu J; Xu Q; Wang M; Zhao D; Wang L; Song L
[Ad] Endereço:Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266071, China; University of Chinese Academy of Sciences, Beijing 100049, China.
[Ti] Título:Crustacean hyperglycemic hormones directly modulate the immune response of hemocytes in shrimp Litopenaeus vannamei.
[So] Source:Fish Shellfish Immunol;62:164-174, 2017 Mar.
[Is] ISSN:1095-9947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A robust immune response against invading pathogens is crucial for host to survive, which depends greatly on the well balance of metabolism. Increasing evidence has indicated that some metabolic hormones, such as insulin, could modulate immune responses directly. Crustacean hyperglycemic hormone (CHH) family is a group of ecdysozoans-specific peptide hormone involved in glucose metabolism and other biological events. In the present study, two members of CHH family (designated as LvCHH I and LvCHH II) in shrimp Litopenaeus vannamei with one and two crustacean neurohormone domains respectively were chosen to investigate their putative modulatory roles in both glucose metabolism and immune response. LvCHH I and LvCHH II were both expressed in the sinus gland and lamina ganglionalis of eyestalks and were significantly induced after white spot syndrome virus (WSSV) infection. Meanwhile, significant increases of hemolymph glucose levels were observed in shrimp at 12 and 24 h after WSSV infection while the glucose inside the hemocytes decreased at 6 h and then increased at 12 h. Gain-of-function of rLvCHHs was subsequently conducted in vivo by injecting the recombinant proteins (rLvCHH I and rLvCHH II). The hemolymph glucose increased significantly from 0.5 h to 3 h after the shrimps received an injection of rLvCHH I, while it decreased at 0.5 h and increased afterward at 3 h post rLvCHH II injection. At the meantime, significant decreases of reactive oxygen species level in hemocytes were observed at 3 h and 6 h post rLvCHH I injection, while it remained unchanged in rLvCHH II injection group. rLvCHH I and rLvCHH II could bind to the cytomembrane of primary shrimp hemocytes in vitro, and the expressions of superoxide dismutase and LvRelish increased when the hemocytes were incubated with rLvCHH I for 3 h. Meanwhile, the expression of antimicrobial peptides, crustin and penaeidin-4, were also induced by rLvCHH I and rLvCHH II. These results demonstrated that host immune response, in addition to glucose metabolism, could be directly modulated by LvCHH family, and the present study provided new insights into the immunomodulation role of metabolic hormones in invertebrate.
[Mh] Termos MeSH primário: Proteínas de Artrópodes/genética
Expressão Gênica
Imunidade Inata
Hormônios de Invertebrado/genética
Proteínas do Tecido Nervoso/genética
Penaeidae/genética
Penaeidae/imunologia
Vírus 1 da Síndrome da Mancha Branca/fisiologia
[Mh] Termos MeSH secundário: Animais
Proteínas de Artrópodes/metabolismo
Glucose/metabolismo
Hemócitos/imunologia
Hemócitos/virologia
Imunomodulação
Hormônios de Invertebrado/metabolismo
Proteínas do Tecido Nervoso/metabolismo
Penaeidae/virologia
Distribuição Aleatória
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arthropod Proteins); 0 (Invertebrate Hormones); 0 (Nerve Tissue Proteins); 0 (hyperglycemic hormone, crustacean); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170410
[Lr] Data última revisão:
170410
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170117
[St] Status:MEDLINE


  6 / 1804 MEDLINE  
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[PMID]:27989866
[Au] Autor:Pitts NL; Mykles DL
[Ad] Endereço:Department of Biology, Colorado State University, Fort Collins, CO 80523, USA.
[Ti] Título:Localization and expression of molt-inhibiting hormone and nitric oxide synthase in the central nervous system of the green shore crab, Carcinus maenas, and the blackback land crab, Gecarcinus lateralis.
[So] Source:Comp Biochem Physiol A Mol Integr Physiol;203:328-340, 2017 Jan.
[Is] ISSN:1531-4332
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In decapod crustaceans, molting is controlled by the pulsatile release of molt-inhibiting hormone (MIH) from neurosecretory cells in the X-organ/sinus gland (XO/SG) complex in the eyestalk ganglia (ESG). A drop in MIH release triggers molting by activating the molting gland or Y-organ (YO). Post-transcriptional mechanisms ultimately control MIH levels in the hemolymph. Neurotransmitter-mediated electrical activity controls Ca -dependent vesicular release of MIH from the SG axon terminals, which may be modulated by nitric oxide (NO). In green shore crab, Carcinus maenas, nitric oxide synthase (NOS) protein and NO are present in the SG. Moreover, C. maenas are refractory to eyestalk ablation (ESA), suggesting other regions of the nervous system secrete sufficient amounts of MIH to prevent molting. By contrast, ESA induces molting in the blackback land crab, Gecarcinus lateralis. Double-label immunofluorescence microscopy and quantitative polymerase chain reaction were used to localize and quantify MIH and NOS proteins and transcripts, respectively, in the ESG, brain, and thoracic ganglion (TG) of C. maenas and G. lateralis. In ESG, MIH- and NOS-immunopositive cells were closely associated in the SG of both species; confocal microscopy showed that NOS was localized in cells adjacent to MIH-positive axon terminals. In brain, MIH-positive cells were located in a small number of cells in the olfactory lobe; no NOS immunofluorescence was detected. In TG, MIH and NOS were localized in cell clusters between the segmental nerves. In G. lateralis, Gl-MIH and Gl-crustacean hyperglycemic hormone (CHH) mRNA levels were ~10 -fold higher in ESG than in brain or TG of intermolt animals, indicating that the ESG is the primary source of these neuropeptides. Gl-NOS and Gl-elongation factor (EF2) mRNA levels were also higher in the ESG. Molt stage had little or no effect on CHH, NOS, NOS-interacting protein (NOS-IP), membrane Guanylyl Cyclase-II (GC-II), and NO-independent GC-III expression in the ESG of both species. By contrast, MIH and NO receptor GC-I beta subunit (GC-Iß) transcripts were increased during premolt and postmolt stages in G. lateralis, but not in C. maenas. MIH immunopositive cells in the brain and TG may be a secondary source of MIH; the release of MIH from these sources may contribute to the difference between the two species in response to ESA. The MIH-immunopositive cells in the TG may be the source of an MIH-like factor that mediates molt inhibition by limb bud autotomy. The association of MIH- and NOS-labeled cells in the ESG and TG suggests that NO may modulate MIH release. A model is proposed in which NO-dependent activation of GC-I inhibits Ca -dependent fusion of MIH vesicles with the nerve terminal membrane; the resulting decrease in MIH activates the YO and the animal enters premolt.
[Mh] Termos MeSH primário: Proteínas de Artrópodes/metabolismo
Braquiúros/fisiologia
Sistema Nervoso Central/metabolismo
Regulação da Expressão Gênica no Desenvolvimento
Hormônios de Invertebrado/metabolismo
Neurônios/metabolismo
Óxido Nítrico Sintase/metabolismo
[Mh] Termos MeSH secundário: Animais
Aquicultura
Proteínas de Artrópodes/genética
Oceano Atlântico
Braquiúros/crescimento & desenvolvimento
California
Sistema Nervoso Central/citologia
Sistema Nervoso Central/enzimologia
República Dominicana
Olho
Gânglios dos Invertebrados/citologia
Gânglios dos Invertebrados/enzimologia
Gânglios dos Invertebrados/metabolismo
Hormônios de Invertebrado/genética
Masculino
Muda
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/metabolismo
Neurônios/citologia
Neurônios/enzimologia
Óxido Nítrico Sintase/genética
Córtex Olfatório/citologia
Córtex Olfatório/enzimologia
Córtex Olfatório/metabolismo
Especificidade de Órgãos
Oceano Pacífico
Especificidade da Espécie
Tórax
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arthropod Proteins); 0 (Invertebrate Hormones); 0 (Nerve Tissue Proteins); 0 (molt-inhibiting hormone); EC 1.14.13.39 (Nitric Oxide Synthase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161220
[St] Status:MEDLINE


  7 / 1804 MEDLINE  
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[PMID]:27838378
[Au] Autor:Yamamoto K; Kiyomoto M; Katayama H; Mita M
[Ad] Endereço:Department of Biology, Faculty of Education and Integrated Sciences, Center for Advanced Biomedical Sciences, Waseda University, Wakamatsucho 2-2, Shinjuku-ku, Tokyo 162-8480, Japan.
[Ti] Título:Radioimmunoassay of relaxin-like gonad-stimulating peptide in the starfish Patiria (=Asterina) pectinifera.
[So] Source:Gen Comp Endocrinol;243:84-88, 2017 Mar 01.
[Is] ISSN:1095-6840
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A relaxin-like gonad-stimulating peptide (RGP) from starfish Patiria (=Asterina) pectinifera is the first identified invertebrate gonadotropin for final gamete maturation. An antiserum against P. pectinifera RGP (PpeRGP) was produced by immunizing rabbits with a PpeRGP sulfanyl-polyethylene glycol derivative conjugated with keyhole limpet hemocyanin (KLH) as the antigen. The antiserum was used for the development of a specific and sensitive radioimmunoassay (RIA) for the measurement of RGP. In binding experiments using radioiodinated PpeRGP and antiserum against PpeRGP, a displacement curve was obtained using radioinert PpeRGP. The sensitivity of the RIA, defined as the amount of PpeRGP that significantly decreased the counts by 2 SD from the 100% bound point, averaged 0.040±0.002pmol PpeRGP per 100µl assay buffer (0.40±0.02nM) in 10 assays. Intra-assay and inter-assay coefficients of variation were 6.1% and 2.7%, respectively. Serial dilution of whole homogenates from the radial nerve cords and circumoral nerve-rings of P. pectinifera produced displacement curves parallel to the PpeRGP standard. Thus, the amounts of PpeRGP were determined as 1.54±0.09pmol/mg wet weight of radial nerves and 0.87±0.04pmol/mg wet weight of nerve-rings, respectively. On contrary, pyloric stomach, pyloric caeca, tube-feet, ovaries, testes, and ovarian follicle cells did not react in the RIA system. Furthermore, the A- and B-chains of PpeRGP, Asterias amurensis RGP, bovine insulin, and human relaxin did not show cross-reactivity in the RIA. These results strongly suggest that the RIA system is a highly specific and sensitive with respect to PpeRGP.
[Mh] Termos MeSH primário: Asterina/metabolismo
Gônadas/metabolismo
Hormônios de Invertebrado/metabolismo
Fragmentos de Peptídeos/metabolismo
Radioimunoensaio/métodos
Relaxina/metabolismo
[Mh] Termos MeSH secundário: Animais
Asterina/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Invertebrate Hormones); 0 (Peptide Fragments); 9002-69-1 (Relaxin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170928
[Lr] Data última revisão:
170928
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161114
[St] Status:MEDLINE


  8 / 1804 MEDLINE  
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[PMID]:27806429
[Au] Autor:Lin M; Mita M; Egertová M; Zampronio CG; Jones AM; Elphick MR
[Ad] Endereço:Queen Mary University of London, School of Biological & Chemical Sciences, London, UK.
[Ti] Título:Cellular localization of relaxin-like gonad-stimulating peptide expression in Asterias rubens: New insights into neurohormonal control of spawning in starfish.
[So] Source:J Comp Neurol;525(7):1599-1617, 2017 May 01.
[Is] ISSN:1096-9861
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Gamete maturation and spawning in starfish is triggered by a gonad-stimulating substance (GSS), which is present in extracts of the radial nerve cords. Purification of GSS from the starfish Patiria pectinifera identified GSS as a relaxin-like polypeptide, which is now known as relaxin-like gonad-stimulating peptide (RGP). Cells expressing RGP in the radial nerve cord of P. pectinifera have been visualized, but the presence of RGP-expressing cells in other parts of the starfish body has not been investigated. Here we addressed this issue in the starfish Asterias rubens. An A. rubens RGP (AruRGP) precursor cDNA was sequenced and the A chain and B chain that form AruRGP were detected in A. rubens radial nerve cord extracts using mass spectrometry. Comparison of the bioactivity of AruRGP and P. pectinifera RGP (PpeRGP) revealed that both polypeptides induce oocyte maturation and ovulation in A. rubens ovarian fragments, but AruRGP is more potent than PpeRGP. Analysis of the expression of AruRGP in A. rubens using mRNA in situ hybridization revealed cells expressing RGP in the radial nerve cords, circumoral nerve ring, and tube feet. Furthermore, a band of RGP-expressing cells was identified in the body wall epithelium lining the cavity that surrounds the sensory terminal tentacle and optic cushion at the tips of the arms. Discovery of these RGP-expressing cells closely associated with sensory organs in the arm tips is an important finding because these cells are candidate physiological mediators for hormonal control of starfish spawning in response to environmental cues. J. Comp. Neurol. 525:1599-1617, 2017. © 2016 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Hormônios de Invertebrado/metabolismo
Relaxina/metabolismo
Comportamento Sexual Animal/fisiologia
Estrelas-do-Mar/fisiologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sequência de Bases
Hibridização In Situ
Espectrometria de Massas
Peptídeos/metabolismo
Filogenia
Reação em Cadeia da Polimerase
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Invertebrate Hormones); 0 (Peptides); 9002-69-1 (Relaxin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161103
[St] Status:MEDLINE
[do] DOI:10.1002/cne.24141


  9 / 1804 MEDLINE  
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[PMID]:27783925
[Au] Autor:Barriga-Montoya C; de la O-Martínez A; Fuentes-Pardo B; Gómez-Lagunas F
[Ad] Endereço:Departamento de Fisiología, Facultad de Medicina, Universidad Nacional Autónoma de México (UNAM), Circuito Interior S/N, Ciudad Universitaria, 04510 Ciudad de México, Mexico.
[Ti] Título:Desensitization and recovery of crayfish photoreceptors. Dependency on circadian time, and pigment-dispersing hormone.
[So] Source:Comp Biochem Physiol A Mol Integr Physiol;203:297-303, 2017 Jan.
[Is] ISSN:1531-4332
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this work, we studied the characteristics of recovery from desensitization of the light-elicited current of crayfish. Applying a two-flash protocol, we found that the first flash triggers a current that activates with a noticeable latency, reaches a peak value, and thereafter decays along a single exponential time course. In comparison with the first-elicited current, the current elicited by the second flash not only presents an expected smaller peak current, depending on the time between flashes, but it also displays a different latency and decay time constant. Recovery of the first flash values of these current parameters depends on the circadian time at which the experiments are conducted, and on the presence of pigment-dispersing hormone. Our data also suggest the existence of distinctive desensitized states, whose induction depends on circadian time and the presence of pigment-dispersing hormone.
[Mh] Termos MeSH primário: Astacoidea/fisiologia
Ritmo Circadiano
Hormônios de Invertebrado/metabolismo
Células Fotorreceptoras de Invertebrados/fisiologia
[Mh] Termos MeSH secundário: Algoritmos
Animais
Aquicultura
Astacoidea/crescimento & desenvolvimento
Fenômenos Eletrofisiológicos
Olho
Técnicas In Vitro/veterinária
Cinética
Muda
Tempo de Reação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Invertebrate Hormones); 56092-79-6 (black pigment dispersing hormone)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161107
[St] Status:MEDLINE


  10 / 1804 MEDLINE  
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Texto completo
[PMID]:27642094
[Au] Autor:S V; C J; K C S; Jose S; Jose B; Philip R; I S BS
[Ad] Endereço:National Centre for Aquatic Animal Health, Cochin University of Science and Technology, Cochin 682 016, India.
[Ti] Título:Regulating gonad inhibition and vitellogenin/vitellin induction in Penaeus monodon using mature GIH fusion protein and polyclonal antisera.
[So] Source:Comp Biochem Physiol A Mol Integr Physiol;203:167-178, 2017 Jan.
[Is] ISSN:1531-4332
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo: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.
[Mh] Termos MeSH primário: Proteínas de Artrópodes/farmacologia
Proteínas de Transporte/farmacologia
Desenho de Drogas
Hormônios de Invertebrado/farmacologia
Modelos Moleculares
Penaeidae/efeitos dos fármacos
Substâncias para o Controle da Reprodução/farmacologia
Vitelogênese/efeitos dos fármacos
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Anticorpos Neutralizantes/farmacologia
Aquicultura
Proteínas de Artrópodes/química
Proteínas de Artrópodes/genética
Proteínas de Artrópodes/metabolismo
Bioensaio
Proteínas de Transporte/química
Proteínas de Transporte/genética
Proteínas de Transporte/metabolismo
Sequência Conservada
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Proteínas de Escherichia coli/farmacologia
Olho
Feminino
Hormônios de Invertebrado/química
Hormônios de Invertebrado/genética
Hormônios de Invertebrado/metabolismo
Sistemas Neurossecretores/citologia
Sistemas Neurossecretores/efeitos dos fármacos
Sistemas Neurossecretores/fisiologia
Penaeidae/citologia
Penaeidae/fisiologia
Conformação Proteica
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes de Fusão/farmacologia
Substâncias para o Controle da Reprodução/antagonistas & inibidores
Substâncias para o Controle da Reprodução/química
Substâncias para o Controle da Reprodução/metabolismo
Alinhamento de Sequência
Homologia Estrutural de Proteína
Tiorredoxinas/química
Tiorredoxinas/genética
Tiorredoxinas/metabolismo
Tiorredoxinas/farmacologia
Vitelinas/antagonistas & inibidores
Vitelinas/genética
Vitelinas/metabolismo
Vitelogeninas/antagonistas & inibidores
Vitelogeninas/genética
Vitelogeninas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
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)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161107
[St] Status:MEDLINE



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