Base de dados : MEDLINE
Pesquisa : D12.644.136 [Categoria DeCS]
Referências encontradas : 544 [refinar]
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[PMID]:28870810
[Au] Autor:Kwon HS; Kawaguchi K; Kikuma T; Takegawa K; Kitamoto K; Higuchi Y
[Ad] Endereço:Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, Fukuoka 812-8581, Japan.
[Ti] Título:Analysis of an acyl-CoA binding protein in Aspergillus oryzae that undergoes unconventional secretion.
[So] Source:Biochem Biophys Res Commun;493(1):481-486, 2017 Nov 04.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acyl-CoA binding protein (ACBP) plays important roles in the metabolism of lipids in eukaryotic cells. In the industrially important filamentous fungus Aspergillus oryzae, although we have previously demonstrated that the A. oryzae ACBP (AoACBP) localizes to punctate structures and exhibits long-range motility, which is dependent on autophagy-related proteins, the physiological role of AoACBP remains elusive. Here, we describe identification and characterization of another ACBP from A. oryzae; we named this ACBP as AoAcb2 and accordingly renamed AoACBP as AoAcb1. The deduced amino acid sequence of AoAcb2 lacked a signal peptide. Phylogenetic analysis classified AoAcb2 into a clade that was same as the ACBP Acb1 of the model yeast Saccharomyces cerevisiae, but was different from that of AoAcb1. In contrast to punctate localization of AoAcb1, AoAcb2 was found to be dispersedly distributed in the cytoplasm, as was previously observed for the S. cerevisiae Acb1. Since we could not generate an Aoacb2 disruptant, we created an Aoacb2 conditional mutant that exhibited less growth under Aoacb2-repressed condition, suggesting that Aoacb2 is an essential gene for growth. Moreover, we observed that A. oryzae AoAcb2, but not A. oryzae AoAcb1, was secreted under carbon-starved condition, suggesting that AoAcb2 might be secreted via the unconventional protein secretion (UPS) pathway, just like S. cerevisiae Acb1. We also demonstrated that the unconventional secretion of AoAcb2 was dependent on the t-SNARE AoSso1, but was independent of the autophagy-related protein AoAtg1, suggesting that the unconventional secretion of AoAcb2, unlike that of S. cerevisiae Acb1, via the UPS pathway, is not regulated by the autophagy machinery. Thus, the filamentous fungus A. oryzae harbors two types of ACBPs, one of which appears to be essential for growth and undergoes unconventional secretion.
[Mh] Termos MeSH primário: Aspergillus oryzae/metabolismo
Proliferação Celular/fisiologia
Inibidor da Ligação a Diazepam/química
Inibidor da Ligação a Diazepam/secreção
[Mh] Termos MeSH secundário: Inibidor da Ligação a Diazepam/classificação
Especificidade da Espécie
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Diazepam Binding Inhibitor)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170906
[St] Status:MEDLINE


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[PMID]:28343864
[Au] Autor:Dumitru I; Neitz A; Alfonso J; Monyer H
[Ad] Endereço:Department of Clinical Neurobiology at the German Cancer Research Center (DKFZ) and the Medical Faculty of the Heidelberg University, Im Neuenheimer Feld 280, 69120 Heidelberg, Germany.
[Ti] Título:Diazepam Binding Inhibitor Promotes Stem Cell Expansion Controlling Environment-Dependent Neurogenesis.
[So] Source:Neuron;94(1):125-137.e5, 2017 Apr 05.
[Is] ISSN:1097-4199
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Plasticity of adult neurogenesis supports adaptation to environmental changes. The identification of molecular mediators that signal these changes to neural progenitors in the niche has remained elusive. Here we report that diazepam binding inhibitor (DBI) is crucial in supporting an adaptive mechanism in response to changes in the environment. We provide evidence that DBI is expressed in stem cells in all neurogenic niches of the postnatal brain. Focusing on the hippocampal subgranular zone (SGZ) and employing multiple genetic manipulations in vivo, we demonstrate that DBI regulates the balance between preserving the stem cell pool and neurogenesis. Specifically, DBI dampens GABA activity in stem cells, thereby sustaining the proproliferative effect of physical exercise and enriched environment. Our data lend credence to the notion that the modulatory effect of DBI constitutes a general mechanism that regulates postnatal neurogenesis.
[Mh] Termos MeSH primário: Proliferação Celular/genética
Inibidor da Ligação a Diazepam/genética
Meio Ambiente
Hipocampo/metabolismo
Células-Tronco Neurais/metabolismo
Neurogênese/genética
[Mh] Termos MeSH secundário: Animais
Inibidor da Ligação a Diazepam/metabolismo
Hipocampo/citologia
Imuno-Histoquímica
Macaca mulatta
Camundongos
Camundongos Transgênicos
Células-Tronco Neurais/citologia
Técnicas de Patch-Clamp
Receptores de GABA-A/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Diazepam Binding Inhibitor); 0 (Receptors, GABA-A)
[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:170328
[St] Status:MEDLINE


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[PMID]:28320857
[Au] Autor:Ferreira NS; Engelsby H; Neess D; Kelly SL; Volpert G; Merrill AH; Futerman AH; Færgeman NJ
[Ad] Endereço:From the Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot 76100, Israel.
[Ti] Título:Regulation of very-long acyl chain ceramide synthesis by acyl-CoA-binding protein.
[So] Source:J Biol Chem;292(18):7588-7597, 2017 May 05.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ceramide and more complex sphingolipids constitute a diverse group of lipids that serve important roles as structural entities of biological membranes and as regulators of cellular growth, differentiation, and development. Thus, ceramides are vital players in numerous diseases including metabolic and cardiovascular diseases, as well as neurological disorders. Here we show that acyl-coenzyme A-binding protein (ACBP) potently facilitates very-long acyl chain ceramide synthesis. ACBP increases the activity of ceramide synthase 2 (CerS2) by more than 2-fold and CerS3 activity by 7-fold. ACBP binds very-long-chain acyl-CoA esters, which is required for its ability to stimulate CerS activity. We also show that high-speed liver cytosol from wild-type mice activates CerS3 activity, whereas cytosol from ACBP knock-out mice does not. Consistently, CerS2 and CerS3 activities are significantly reduced in the testes of ACBP mice, concomitant with a significant reduction in long- and very-long-chain ceramide levels. Importantly, we show that ACBP interacts with CerS2 and CerS3. Our data uncover a novel mode of regulation of very-long acyl chain ceramide synthesis by ACBP, which we anticipate is of crucial importance in understanding the regulation of ceramide metabolism in pathogenesis.
[Mh] Termos MeSH primário: Ceramidas/biossíntese
Inibidor da Ligação a Diazepam/metabolismo
Ácidos Graxos/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Ceramidas/genética
Inibidor da Ligação a Diazepam/genética
Ácidos Graxos/genética
Seres Humanos
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Camundongos
Camundongos Knockout
Esfingosina N-Aciltransferase/genética
Esfingosina N-Aciltransferase/metabolismo
Proteínas Supressoras de Tumor/genética
Proteínas Supressoras de Tumor/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ceramides); 0 (Diazepam Binding Inhibitor); 0 (Fatty Acids); 0 (Membrane Proteins); 0 (Tumor Suppressor Proteins); EC 2.3.1.24 (CERS2 protein, human); EC 2.3.1.24 (Cers2 protein, mouse); EC 2.3.1.24 (LASS3 protein, mouse); EC 2.3.1.24 (Sphingosine N-Acyltransferase); EC 2.3.1.24 (ceramide synthase 3, human)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170607
[Lr] Data última revisão:
170607
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.785345


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[PMID]:28242275
[Au] Autor:Chellan P; Sadler PJ; Land KM
[Ad] Endereço:Department of Chemistry, University of Warwick, Coventry, Warwickshire CV4 7AL, UK.
[Ti] Título:Recent developments in drug discovery against the protozoal parasites Cryptosporidium and Toxoplasma.
[So] Source:Bioorg Med Chem Lett;27(7):1491-1501, 2017 04 01.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Apicomplexan parasites cause some of the most devastating human diseases, including malaria, toxoplasmosis, and cryptosporidiosis. New drug discovery is imperative in light of increased resistance. In this digest article, we briefly explore some of the recent and promising developments in new drug discovery against two apicomplexan parasites, Cryptosporidium and Toxoplasma.
[Mh] Termos MeSH primário: Antiprotozoários/farmacologia
Cryptosporidium/efeitos dos fármacos
Toxoplasma/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Antiprotozoários/uso terapêutico
Apoptose/efeitos dos fármacos
Criptosporidiose/tratamento farmacológico
Criptosporidiose/parasitologia
Cryptosporidium/enzimologia
Inibidor da Ligação a Diazepam/antagonistas & inibidores
Descoberta de Drogas
Inibidores Enzimáticos/farmacologia
Inibidores Enzimáticos/uso terapêutico
Seres Humanos
Camundongos
Toxoplasma/enzimologia
Toxoplasmose/tratamento farmacológico
Toxoplasmose/parasitologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antiprotozoal Agents); 0 (Diazepam Binding Inhibitor); 0 (Enzyme Inhibitors)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171124
[Lr] Data última revisão:
171124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170301
[St] Status:MEDLINE


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[PMID]:27815223
[Au] Autor:Gallego SF; Sprenger RR; Neess D; Pauling JK; Færgeman NJ; Ejsing CS
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Villum Center for Bioanalytical Sciences, University of Southern Denmark, DK-5230 Odense, Denmark.
[Ti] Título:Quantitative lipidomics reveals age-dependent perturbations of whole-body lipid metabolism in ACBP deficient mice.
[So] Source:Biochim Biophys Acta;1862(2):145-155, 2017 02.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The acyl-CoA binding protein (ACBP) plays a key role in chaperoning long-chain acyl-CoAs into lipid metabolic processes and acts as an important regulatory hub in mammalian physiology. This is highlighted by the recent finding that mice devoid of ACBP suffer from a compromised epidermal barrier and delayed weaning, the physiological process where newborns transit from a fat-based milk diet to a carbohydrate-rich diet. To gain insights into how ACBP impinges on weaning and the concomitant remodeling of whole-body lipid metabolism we performed a comparative lipidomics analysis charting the absolute abundance of 613 lipid molecules in liver, muscle and plasma from weaning and adult Acbp knockout and wild type mice. Our results reveal that ACBP deficiency affects primarily lipid metabolism of liver and plasma during weaning. Specifically, we show that ACBP deficient mice have elevated levels of hepatic cholesteryl esters, and that lipids featuring an 18:1 fatty acid moiety are increased in Acbp depleted mice across all tissues investigated. Our results also show that the perturbation of systemic lipid metabolism in Acbp knockout mice is transient and becomes normalized and similar to that of wild type as mice grow older. These findings demonstrate that ACBP serves crucial functions in maintaining lipid metabolic homeostasis in mice during weaning.
[Mh] Termos MeSH primário: Inibidor da Ligação a Diazepam/deficiência
Metabolismo dos Lipídeos/fisiologia
[Mh] Termos MeSH secundário: Animais
Ésteres do Colesterol/metabolismo
Ácidos Graxos/metabolismo
Lipídeos/fisiologia
Fígado/metabolismo
Masculino
Camundongos
Camundongos Knockout
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cholesterol Esters); 0 (Diazepam Binding Inhibitor); 0 (Fatty Acids); 0 (Lipids)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161106
[St] Status:MEDLINE


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[PMID]:27452861
[Au] Autor:Dlamini Z; Mbele M; McCabe M; Rees J; Naicker S; Mbita Z
[Ad] Endereço:Research, Innovation and Engagements Portfolio, Mangosuthu University of Technology, Durban, South Africa. dlaminiz@mut.ac.za.
[Ti] Título:Significant up-regulation of 1-ACBP, B-ACBP and PBR genes in immune cells within the oesophageal malignant tissue and a possible link in carcinogenic angiogenesis.
[So] Source:Histol Histopathol;32(6):561-570, 2017 Jun.
[Is] ISSN:1699-5848
[Cp] País de publicação:Spain
[La] Idioma:eng
[Ab] Resumo:Oesophageal cancer ranks as the sixth most common malignancy in the world, and recent evidence has shown that its incidence is increasing. ACBPs (Acyl-coA binding proteins) act as intracellular carrier-proteins for medium to long chain acyl-coA, mediating fatty acid transport to the mitochondrion for ß-oxidation. ACBPs are also believed to be putative ligands of PBR (peripheral benzodiazepine receptor), and once they bind to this receptor they facilitate mitochondrial membrane permeabilization, presumably favouring apoptosis. The main aim of the study was to establish the expression patterns of 1- Acyl-coA binding proteins (1-ACBP), B- Acyl-coA binding proteins (B-ACBP), and peripheral bezodiazepine receptor (PBR) in oesophageal cancer, and to link their roles with the disease. In situ hybridization and quantitative real-time PCR methods were performed to determine localization and the expression levels of the three genes in oesophageal cancer. All three genes illustrated substantial up-regulation within the malignant tissue sections as compared to normal oesophageal sections, all three transcripts localized specifically to mast cells, plasma cells and lymphocytes in diseased and normal tissue section. In the diseased tissue B-ACBP and 1-ACBP mRNA localized to endothelial cells of blood vessels in the submucosa. B-ACBP also localized to the nucleus of squamous epithelial cells. PBR localization was indicated in tumour islands of invasive tissue sections. Quantitative RT-PCR also indicated that the expression levels of PBR were higher as compared to the ACBP genes expression in tumours. These results show that 1-ACBP, B-ACBP and PBR play a role in the pathogenesis of oesophageal tumours and possibly in carcinogenic angiogenesis.
[Mh] Termos MeSH primário: Carcinoma de Células Escamosas/patologia
Inibidor da Ligação a Diazepam/biossíntese
Neoplasias Esofágicas/patologia
Neovascularização Patológica/patologia
Receptores de GABA-A/biossíntese
[Mh] Termos MeSH secundário: Biomarcadores Tumorais/análise
Carcinoma de Células Escamosas/genética
Carcinoma de Células Escamosas/imunologia
Inibidor da Ligação a Diazepam/genética
Neoplasias Esofágicas/genética
Neoplasias Esofágicas/imunologia
Seres Humanos
Hibridização In Situ
Linfócitos/metabolismo
Mastócitos/metabolismo
Plasmócitos/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Receptores de GABA-A/genética
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (Diazepam Binding Inhibitor); 0 (Receptors, GABA-A)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170815
[Lr] Data última revisão:
170815
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160726
[St] Status:MEDLINE
[do] DOI:10.14670/HH-11-805


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[PMID]:27725156
[Au] Autor:Kawaguchi K; Kikuma T; Higuchi Y; Takegawa K; Kitamoto K
[Ad] Endereço:Department of Biotechnology, The University of Tokyo, 1-1-1 Bunkyo-ku, Tokyo 113-8657, Japan.
[Ti] Título:Subcellular localization of acyl-CoA binding protein in Aspergillus oryzae is regulated by autophagy machinery.
[So] Source:Biochem Biophys Res Commun;480(1):8-12, 2016 Nov 04.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In eukaryotic cells, acyl-CoA binding protein (ACBP) is important for cellular activities, such as in lipid metabolism. In the industrially important fungus Aspergillus oryzae, the ACBP, known as AoACBP, has been biochemically characterized, but its physiological function is not known. In the present study, although we could not find any phenotype of AoACBP disruptants in the normal growth conditions, we examined the subcellular localization of AoACBP to understand its physiological function. Using an enhanced green fluorescent protein (EGFP)-tagged AoACBP construct we showed that AoACBP localized to punctate structures in the cytoplasm, some of which moved inside the cells in a microtubule-dependent manner. Further microscopic analyses showed that AoACBP-EGFP co-localized with the autophagy marker protein AoAtg8 tagged with red fluorescent protein (mDsRed). Expression of AoACBP-EGFP in disruptants of autophagy-related genes revealed aggregation of AoACBP-EGFP fluorescence in the cytoplasm of Aoatg1, Aoatg4 and Aoatg8 disruptant cells. However, in cells harboring disruption of Aoatg15, which encodes a lipase for autophagic body, puncta of AoACBP-EGFP fluorescence accumulated in vacuoles, indicating that AoACBP is transported to vacuoles via the autophagy machinery. Collectively, these results suggest the existence of a regulatory mechanism between AoACBP localization and autophagy.
[Mh] Termos MeSH primário: Aspergillus oryzae/metabolismo
Autofagia/fisiologia
Inibidor da Ligação a Diazepam/metabolismo
Proteínas Fúngicas/metabolismo
[Mh] Termos MeSH secundário: Aspergillus oryzae/citologia
Família da Proteína 8 Relacionada à Autofagia/genética
Família da Proteína 8 Relacionada à Autofagia/metabolismo
Citoplasma/metabolismo
Inibidor da Ligação a Diazepam/genética
Proteínas Fúngicas/genética
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Proteínas Luminescentes/genética
Proteínas Luminescentes/metabolismo
Microtúbulos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Autophagy-Related Protein 8 Family); 0 (Diazepam Binding Inhibitor); 0 (Fungal Proteins); 0 (Luminescent Proteins); 0 (enhanced green fluorescent protein); 0 (red fluorescent protein); 147336-22-9 (Green Fluorescent Proteins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170606
[Lr] Data última revisão:
170606
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161012
[St] Status:MEDLINE


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[PMID]:27368137
[Au] Autor:Du ZY; Arias T; Meng W; Chye ML
[Ad] Endereço:School of Biological Sciences, The University of Hong Kong, Pokfulam, Hong Kong.
[Ti] Título:Plant acyl-CoA-binding proteins: An emerging family involved in plant development and stress responses.
[So] Source:Prog Lipid Res;63:165-81, 2016 07.
[Is] ISSN:1873-2194
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Acyl-CoA-binding protein (ACBP) was first identified in mammals as a neuropeptide, and was demonstrated to belong to an important house-keeping protein family that extends across eukaryotes and some prokaryotes. In plants, the Arabidopsis ACBP family consists of six AtACBPs (AtACBP1 to AtACBP6), and has been investigated using gene knock-out mutants and overexpression lines. Herein, recent findings on the AtACBPs are examined to provide an insight on their functions in various plant developmental processes, such as embryo and seed development, seed dormancy and germination, seedling development and cuticle formation, as well as their roles under various environmental stresses. The significance of the AtACBPs in acyl-CoA/lipid metabolism, with focus on their interaction with long to very-long-chain (VLC) acyl-CoA esters and their potential role in the formation of lipid droplets in seeds and vegetative tissues are discussed. In addition, recent findings on the rice ACBP family are presented. The similarities and differences between ACBPs from Arabidopsis and rice, that represent eudicot and monocot model plants, respectively, are analyzed and the evolution of plant ACBPs by phylogenetic analysis reviewed. Finally, we propose potential uses of plant ACBPs in phytoremediation and in agriculture related to the improvement of environmental stress tolerance and seed oil production.
[Mh] Termos MeSH primário: Inibidor da Ligação a Diazepam/metabolismo
Plantas/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/crescimento & desenvolvimento
Arabidopsis/metabolismo
Inibidor da Ligação a Diazepam/classificação
Oryza/crescimento & desenvolvimento
Oryza/metabolismo
Estresse Oxidativo
Filogenia
Desenvolvimento Vegetal
Sementes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Diazepam Binding Inhibitor)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170420
[Lr] Data última revisão:
170420
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160703
[St] Status:MEDLINE


  9 / 544 MEDLINE  
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[PMID]:27023243
[Au] Autor:Lung SC; Chye ML
[Ad] Endereço:School of Biological Sciences, The University of Hong Kong, Pokfulam, Hong Kong, China.
[Ti] Título:Acyl-CoA-Binding Proteins (ACBPs) in Plant Development.
[So] Source:Subcell Biochem;86:363-404, 2016.
[Is] ISSN:0306-0225
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acyl-CoA-binding proteins (ACBPs) play a pivotal role in fatty acid metabolism because they can transport medium- and long-chain acyl-CoA esters. In eukaryotic cells, ACBPs are involved in intracellular trafficking of acyl-CoA esters and formation of a cytosolic acyl-CoA pool. In addition to these ubiquitous functions, more specific non-redundant roles of plant ACBP subclasses are implicated by the existence of multigene families with variable molecular masses, ligand specificities, functional domains (e.g. protein-protein interaction domains), subcellular locations and gene expression patterns. In this chapter, recent progress in the characterization of ACBPs from the model dicot plant, Arabidopsis thaliana, and the model monocot, Oryza sativa, and their emerging roles in plant growth and development are discussed. The functional significance of respective members of the plant ACBP families in various developmental and physiological processes such as seed development and germination, stem cuticle formation, pollen development, leaf senescence, peroxisomal fatty acid ß-oxidation and phloem-mediated lipid transport is highlighted.
[Mh] Termos MeSH primário: Inibidor da Ligação a Diazepam/fisiologia
Desenvolvimento Vegetal/fisiologia
[Mh] Termos MeSH secundário: Arabidopsis/embriologia
Arabidopsis/crescimento & desenvolvimento
Arabidopsis/fisiologia
Oryza/embriologia
Oryza/crescimento & desenvolvimento
Oryza/fisiologia
Folhas de Planta/metabolismo
Óleos Vegetais/metabolismo
Pólen/metabolismo
Sementes/crescimento & desenvolvimento
Sementes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Diazepam Binding Inhibitor); 0 (Plant Oils)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:160330
[Lr] Data última revisão:
160330
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160330
[St] Status:MEDLINE
[do] DOI:10.1007/978-3-319-25979-6_15


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[PMID]:27001070
[Au] Autor:Majerowicz D; Hannibal-Bach HK; Castro RSC; Bozaquel-Morais BL; Alves-Bezerra M; Grillo LAM; Masuda CA; Færgeman NJ; Knudsen J; Gondim KC
[Ad] Endereço:Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil; Institut for Biokemi og Molekylær Biologi, Syddansk Universitet, Odense, Denmark.
[Ti] Título:The ACBP gene family in Rhodnius prolixus: Expression, characterization and function of RpACBP-1.
[So] Source:Insect Biochem Mol Biol;72:41-52, 2016 May.
[Is] ISSN:1879-0240
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The acyl-CoA-binding proteins (ACBP) constitute a family of conserved proteins that bind acyl-CoA with high affinity and protect it from hydrolysis. Thus, ACBPs may have essential roles in basal cellular lipid metabolism. The genome of the insect Rhodnius prolixus encodes five ACBP genes similar to those described for other insect species. The qPCR analysis revealed that these genes have characteristic expression profiles in insect organs, suggesting that they have specific roles in insect physiology. Recombinant RpACBP-1 was able to bind acyl-CoA in an in vitro gel-shift assay. Moreover, heterologous RpACBP-1 expression in acb1Δ mutant yeast rescued the multi-lobed vacuole phenotype, indicating that RpACBP-1 acts as a bona fide acyl-CoA-binding protein. RpACBP-1 knockdown using RNAi caused triacylglycerol accumulation in the insect posterior midgut and a reduction in the number of deposited eggs. The amount of stored triacylglycerol was reduced in flight muscle, and the incorporation of fatty acids in cholesteryl esters was increased in the fat body. These results showed that RpACBP-1 participates in several lipid metabolism steps in R. prolixus.
[Mh] Termos MeSH primário: Inibidor da Ligação a Diazepam/metabolismo
Proteínas de Insetos/metabolismo
Rhodnius/metabolismo
[Mh] Termos MeSH secundário: Acil Coenzima A/metabolismo
Animais
Corpo Adiposo/metabolismo
Feminino
Fertilidade
Regulação da Expressão Gênica
Proteínas de Insetos/genética
Metabolismo dos Lipídeos
Masculino
Oviposição
Interferência de RNA
Rhodnius/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Diazepam Binding Inhibitor); 0 (Insect Proteins)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170805
[Lr] Data última revisão:
170805
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160323
[St] Status:MEDLINE



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