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[PMID]:28774878
[Au] Autor:Luscieti S; Galy B; Gutierrez L; Reinke M; Couso J; Shvartsman M; Di Pascale A; Witke W; Hentze MW; Pilo Boyl P; Sanchez M
[Ad] Endereço:Program of Predictive and Personalized Medicine of Cancer, Germans Trias and Pujol Research Institute, Campus Can Ruti, Badalona, Spain.
[Ti] Título:The actin-binding protein profilin 2 is a novel regulator of iron homeostasis.
[So] Source:Blood;130(17):1934-1945, 2017 Oct 26.
[Is] ISSN:1528-0020
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cellular iron homeostasis is controlled by the iron regulatory proteins (IRPs) 1 and 2 that bind -regulatory iron-responsive elements (IRE) on target messenger RNAs (mRNA). We identified ( ) mRNA, which encodes an actin-binding protein involved in endocytosis and neurotransmitter release, as a novel IRP-interacting transcript, and studied its role in iron metabolism. A combination of electrophoretic mobility shift assay experiments and bioinformatic analyses led to the identification of an atypical and conserved IRE in the 3' untranslated region of mRNA. mRNA levels were significantly reduced in duodenal samples from mice with intestinal IRP ablation, suggesting that IRPs exert a positive effect on mRNA expression in vivo. Overexpression of Pfn2 in HeLa and Hepa1-6 cells reduced their metabolically active iron pool. Importantly, Pfn2-deficient mice showed iron accumulation in discrete areas of the brain (olfactory bulb, hippocampus, and midbrain) and reduction of the hepatic iron store without anemia. Despite low liver iron levels, hepatic hepcidin expression remained high, likely because of compensatory activation of by mild inflammation. Splenic ferroportin was increased probably to sustain hematopoiesis. Overall, our results indicate that Pfn2 expression is controlled by the IRPs in vivo and that Pfn2 contributes to maintaining iron homeostasis in cell lines and mice.
[Mh] Termos MeSH primário: Homeostase
Ferro/metabolismo
Profilinas/metabolismo
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas/genética
Animais
Sequência de Bases
Linhagem Celular
Duodeno/metabolismo
Células HeLa
Seres Humanos
Proteínas Reguladoras do Ferro/metabolismo
Camundongos Endogâmicos C57BL
Modelos Biológicos
Especificidade de Órgãos
Profilinas/genética
Ligação Proteica/genética
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Elementos de Resposta/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (Iron-Regulatory Proteins); 0 (Profilins); 0 (RNA, Messenger); 0 (Reactive Oxygen Species); E1UOL152H7 (Iron)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170805
[St] Status:MEDLINE
[do] DOI:10.1182/blood-2016-11-754382


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[PMID]:28671021
[Au] Autor:Jamnongkan W; Thanan R; Techasen A; Namwat N; Loilome W; Intarawichian P; Titapun A; Yongvanit P
[Ad] Endereço:1 Department of Biochemistry, Faculty of Medicine, Khon Kaen University, Khon Kaen, Thailand.
[Ti] Título:Upregulation of transferrin receptor-1 induces cholangiocarcinoma progression via induction of labile iron pool.
[So] Source:Tumour Biol;39(7):1010428317717655, 2017 Jul.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Labile iron pool is a cellular source of ions available for Fenton reactions resulting in oxidative stress. Living organisms avoid an excess of free irons by a tight control of iron homeostasis. We investigated the altered expression of iron regulatory proteins and iron discrimination in the development of liver fluke-associated cholangiocarcinoma. Additionally, the levels of labile iron pool and the functions of transferrin receptor-1 on cholangiocarcinoma development were also identified. Iron deposition was determined using the Prussian blue staining method in human cholangiocarcinoma tissues. We investigated the alteration of iron regulatory proteins including transferrin, transferrin receptor-1, ferritin, ferroportin, hepcidin, and divalent metal transporter-1 in cholangiocarcinoma tissues using immunohistochemistry. The clinicopathological data of cholangiocarcinoma patients and the expressions of proteins were analyzed. Moreover, the level of intracellular labile iron pool in cholangiocarcinoma cell lines was identified by the RhoNox-1 staining method. We further demonstrated transferrin receptor-1 functions on cell proliferation and migration upon small interfering RNA for human transferrin receptor 1 transfection. Results show that Iron was strongly stained in tumor tissues, whereas negative staining was observed in normal bile ducts of healthy donors. Interestingly, high iron accumulation was significantly correlated with poor prognosis of cholangiocarcinoma patients. The expressions of iron regulatory proteins in human cholangiocarcinoma tissues and normal liver from cadaveric donors revealed that transferrin receptor-1 expression was increased in the cancer cells of cholangiocarcinoma tissues when compared with the adjacent normal bile ducts and was significantly correlated with cholangiocarcinoma metastasis. Labile iron pool level and transferrin receptor-1 expression were significantly increased in KKU-214 and KKU-213 when compared with cholangiocyte cells (MMNK1). Additionally, the suppression of transferrin receptor-1 expression significantly decreased intracellular labile iron pool, cholangiocarcinoma migration, and cell proliferation when compared with control media and control small interfering RNA. In Conclusion, high expression of transferrin receptor-1 resulting in iron uptake contributes to increase in the labile iron pool which plays roles in cholangiocarcinoma progression with aggressive clinical outcomes.
[Mh] Termos MeSH primário: Antígenos CD/biossíntese
Colangiocarcinoma/genética
Proteínas Reguladoras do Ferro/genética
Ferro/metabolismo
Estresse Oxidativo/genética
Receptores da Transferrina/biossíntese
[Mh] Termos MeSH secundário: Adulto
Idoso
Antígenos CD/genética
Linhagem Celular Tumoral
Movimento Celular/genética
Proliferação Celular/genética
Colangiocarcinoma/metabolismo
Colangiocarcinoma/patologia
Progressão da Doença
Feminino
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Proteínas Reguladoras do Ferro/metabolismo
Masculino
Meia-Idade
Metástase Neoplásica
Estadiamento de Neoplasias
Receptores da Transferrina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD); 0 (CD71 antigen); 0 (Iron-Regulatory Proteins); 0 (Receptors, Transferrin); E1UOL152H7 (Iron)
[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:170704
[St] Status:MEDLINE
[do] DOI:10.1177/1010428317717655


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[PMID]:28615455
[Au] Autor:Guengerich FP
[Ad] Endereço:From the Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146 f.guengerich@vanderbilt.edu.
[Ti] Título:Introduction to Metals in Biology 2017: Iron transport, storage, and the ramifications.
[So] Source:J Biol Chem;292(31):12725-12726, 2017 Aug 04.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this tenth Thematic Series in Metals in Biology, six Minireviews deal with aspects of iron metabolism. A number of important proteins control iron homeostasis, including hepcidin and ferroportin, in various cells. Other aspects of iron dealt with here include biogenesis of iron-sulfur proteins and chaperones that deliver iron cofactors in cells. Additionally, an iron-regulated metastasis suppressor interacts with the epidermal growth factor receptor and mediates its downstream signaling activity.
[Mh] Termos MeSH primário: Homeostase
Ferro/fisiologia
[Mh] Termos MeSH secundário: Animais
Transporte Biológico
Seres Humanos
Proteínas Reguladoras do Ferro/fisiologia
Proteínas com Ferro-Enxofre/fisiologia
[Pt] Tipo de publicação:INTRODUCTORY JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Iron-Regulatory Proteins); 0 (Iron-Sulfur Proteins); E1UOL152H7 (Iron)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170616
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.R117.801332


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[PMID]:28615439
[Au] Autor:Rouault TA; Maio N
[Ad] Endereço:From the Molecular Medicine Branch, Eunice Kennedy Shriver NICHD, National Institutes of Health, Bethesda, Maryland 20892 rouault@mail.nih.gov.
[Ti] Título:Biogenesis and functions of mammalian iron-sulfur proteins in the regulation of iron homeostasis and pivotal metabolic pathways.
[So] Source:J Biol Chem;292(31):12744-12753, 2017 Aug 04.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fe-S cofactors are composed of iron and inorganic sulfur in various stoichiometries. A complex assembly pathway conducts their initial synthesis and subsequent binding to recipient proteins. In this minireview, we discuss how discovery of the role of the mammalian cytosolic aconitase, known as iron regulatory protein 1 (IRP1), led to the characterization of the function of its Fe-S cluster in sensing and regulating cellular iron homeostasis. Moreover, we present an overview of recent studies that have provided insights into the mechanism of Fe-S cluster transfer to recipient Fe-S proteins.
[Mh] Termos MeSH primário: Homeostase
Proteína 1 Reguladora do Ferro/fisiologia
Ferro/fisiologia
Modelos Moleculares
[Mh] Termos MeSH secundário: Animais
Apoenzimas/química
Apoenzimas/metabolismo
Liases de Carbono-Enxofre/biossíntese
Liases de Carbono-Enxofre/química
Liases de Carbono-Enxofre/fisiologia
Transporte de Elétrons
Regulação Enzimológica da Expressão Gênica
Proteínas de Choque Térmico HSP70/biossíntese
Proteínas de Choque Térmico HSP70/química
Proteínas de Choque Térmico HSP70/fisiologia
Seres Humanos
Proteína 1 Reguladora do Ferro/biossíntese
Proteína 1 Reguladora do Ferro/química
Proteínas de Ligação ao Ferro/biossíntese
Proteínas de Ligação ao Ferro/química
Proteínas de Ligação ao Ferro/fisiologia
Proteínas Reguladoras do Ferro/biossíntese
Proteínas Reguladoras do Ferro/química
Proteínas Reguladoras do Ferro/fisiologia
Proteínas com Ferro-Enxofre/biossíntese
Proteínas com Ferro-Enxofre/química
Proteínas com Ferro-Enxofre/fisiologia
Proteínas Mitocondriais/biossíntese
Proteínas Mitocondriais/química
Proteínas Mitocondriais/fisiologia
Chaperonas Moleculares/biossíntese
Chaperonas Moleculares/química
Chaperonas Moleculares/fisiologia
Dobramento de Proteína
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Elementos de Resposta
Succinato Desidrogenase/biossíntese
Succinato Desidrogenase/química
Succinato Desidrogenase/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Apoenzymes); 0 (HSCB protein, human); 0 (HSP70 Heat-Shock Proteins); 0 (HSPA9 protein, human); 0 (ISCU protein, human); 0 (ISD11 protein, human); 0 (Iron-Binding Proteins); 0 (Iron-Regulatory Proteins); 0 (Iron-Sulfur Proteins); 0 (Mitochondrial Proteins); 0 (Molecular Chaperones); 0 (frataxin); E1UOL152H7 (Iron); EC 1.3.5.1 (SDHB protein, human); EC 1.3.99.1 (Succinate Dehydrogenase); EC 4.2.1.3 (IRP1 protein, human); EC 4.2.1.3 (Iron Regulatory Protein 1); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.- (NFS1 protein, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170616
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.R117.789537


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[PMID]:28271877
[Au] Autor:Friemel M; Marelja Z; Li K; Leimkühler S
[Ad] Endereço:Institut für Biochemie und Biologie, Molekulare Enzymologie, Universität Potsdam , Karl-Liebknecht-Strasse 24-25, 14476 Potsdam, Germany.
[Ti] Título:The N-Terminus of Iron-Sulfur Cluster Assembly Factor ISD11 Is Crucial for Subcellular Targeting and Interaction with l-Cysteine Desulfurase NFS1.
[So] Source:Biochemistry;56(12):1797-1808, 2017 Mar 28.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Assembly of iron-sulfur (FeS) clusters is an important process in living cells. The initial sulfur mobilization step for FeS cluster biosynthesis is catalyzed by l-cysteine desulfurase NFS1, a reaction that is localized in mitochondria in humans. In humans, the function of NFS1 depends on the ISD11 protein, which is required to stabilize its structure. The NFS1/ISD11 complex further interacts with scaffold protein ISCU and regulator protein frataxin, thereby forming a quaternary complex for FeS cluster formation. It has been suggested that the role of ISD11 is not restricted to its role in stabilizing the structure of NFS1, because studies of single-amino acid variants of ISD11 additionally demonstrated its importance for the correct assembly of the quaternary complex. In this study, we are focusing on the N-terminal region of ISD11 to determine the role of N-terminal amino acids in the formation of the complex with NFS1 and to reveal the mitochondrial targeting sequence for subcellular localization. Our in vitro studies with the purified proteins and in vivo studies in a cellular system show that the first 10 N-terminal amino acids of ISD11 are indispensable for the activity of NFS1 and especially the conserved "LYR" motif is essential for the role of ISD11 in forming a stable and active complex with NFS1.
[Mh] Termos MeSH primário: Liases de Carbono-Enxofre/química
Proteínas de Ligação ao Ferro/química
Proteínas Reguladoras do Ferro/química
Proteínas com Ferro-Enxofre/química
Ferro/química
Mitocôndrias/metabolismo
Enxofre/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Liases de Carbono-Enxofre/genética
Liases de Carbono-Enxofre/metabolismo
Regulação da Expressão Gênica
Genes Reporter
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Células HeLa
Seres Humanos
Ferro/metabolismo
Proteínas de Ligação ao Ferro/genética
Proteínas de Ligação ao Ferro/metabolismo
Proteínas Reguladoras do Ferro/genética
Proteínas Reguladoras do Ferro/metabolismo
Proteínas com Ferro-Enxofre/genética
Proteínas com Ferro-Enxofre/metabolismo
Proteínas Luminescentes/genética
Proteínas Luminescentes/metabolismo
Mitocôndrias/genética
Modelos Moleculares
Domínios Proteicos
Multimerização Proteica
Estrutura Secundária de Proteína
Transporte Proteico
Transdução de Sinais
Enxofre/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (ISCU protein, human); 0 (ISD11 protein, human); 0 (Iron-Binding Proteins); 0 (Iron-Regulatory Proteins); 0 (Iron-Sulfur Proteins); 0 (Luminescent Proteins); 0 (frataxin); 0 (yellow fluorescent protein, Bacteria); 147336-22-9 (Green Fluorescent Proteins); 70FD1KFU70 (Sulfur); E1UOL152H7 (Iron); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.- (NFS1 protein, human)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170529
[Lr] Data última revisão:
170529
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170309
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b01239


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[PMID]:28233492
[Au] Autor:Cai K; Frederick RO; Tonelli M; Markley JL
[Ad] Endereço:Biochemistry Department, University of Wisconsin-Madison , 433 Babcock Drive, Madison, Wisconsin 53706, United States.
[Ti] Título:Mitochondrial Cysteine Desulfurase and ISD11 Coexpressed in Escherichia coli Yield Complex Containing Acyl Carrier Protein.
[So] Source:ACS Chem Biol;12(4):918-921, 2017 Apr 21.
[Is] ISSN:1554-8937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitochondrial cysteine desulfurase is an essential component of the machinery for iron-sulfur cluster biosynthesis. It has been known that human cysteine desulfurase that is catalytically active in vitro can be prepared by overexpressing in Escherichia coli cells two protein components of this system, the cysteine desulfurase protein NFS1 and the auxiliary protein ISD11. We report here that this active preparation contains, in addition, the holo-form of E. coli acyl carrier protein (Acp). We have determined the stoichiometry of the complex to be [Acp] :[ISD11] :[NFS1] . Acyl carrier protein recently has been found to be an essential component of the iron-sulfur protein biosynthesis machinery in mitochondria; thus, because of the activity of [Acp] :[ISD11] :[NFS1] in supporting iron-sulfur cluster assembly in vitro, it appears that E. coli Acp can substitute for its human homologue.
[Mh] Termos MeSH primário: Proteína de Transporte de Acila/metabolismo
Liases de Carbono-Enxofre/metabolismo
Escherichia coli/genética
Proteínas Reguladoras do Ferro/metabolismo
Mitocôndrias/enzimologia
[Mh] Termos MeSH secundário: Liases de Carbono-Enxofre/genética
Cromatografia em Gel
Eletroforese em Gel de Poliacrilamida
Proteínas Reguladoras do Ferro/genética
Mitocôndrias/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Espalhamento a Baixo Ângulo
Espectrometria de Massas em Tandem
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Carrier Protein); 0 (ISD11 protein, human); 0 (Iron-Regulatory Proteins); 0 (Recombinant Proteins); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.- (cysteine desulfurase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170802
[Lr] Data última revisão:
170802
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170225
[St] Status:MEDLINE
[do] DOI:10.1021/acschembio.6b01005


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[PMID]:28151915
[Au] Autor:Nikkari ST; Visto AL; Määttä KM; Kunnas TA
[Ad] Endereço:aDepartment of Medical Biochemistry, Faculty of Medicine and Life Sciences, University of Tampere, Finland bFimlab laboratories, Tampere, Finland.
[Ti] Título:Minor variant of rs 16827043 in the iron regulator hemojuvelin gene (HJV) contributes to hypertension: The TAMRISK study.
[So] Source:Medicine (Baltimore);96(5):e6052, 2017 Feb.
[Is] ISSN:1536-5964
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:It is known that iron overload may lead to an increased risk for many diseases. According to GWAS studies, iron regulatory protein HFE gene variant H63D (rs1799945) was associated with hypertension, an observation which we were able to confirm also in our TAMRISK cohort. Thus, it is possible that abnormalities in iron homeostasis may predispose to hypertension. This prompted us to study whether there is an association between hypertension and another iron overload-associated gene, hemojuvelin (HJV), which has 2 common polymorphic sites (rs 16827043, rs7536827).The study included 336 hypertensive cases and 480 controls. All participants were 50- year-old Finnish men and women, and the data was collected from the Tampere adult population cardiovascular risk study (TAMRISK). Genotypes were determined using Competitive Allelic Specific PCR (KASP).We found that the minor variant of the HJV polymorphic site rs16827043 (G-allele) is a statistically significant factor associated with hypertension among 50 year-old individuals compared with the AA genotype carriers (OR = 1.66, 95% CI: 1.06 - 2.60, P = 0.03). The risk was even higher when overweight subjects (BMI>30) were excluded from the analyses. For the other polymorphic variant rs7536827, association with hypertension was found only among normal or slightly overweight A-allele carriers.In conclusion, HJV genetic variants were associated with essential hypertension in Finnish subjects from the TAMRISK cohort. Previous studies together with the present one indicate that individuals with possible dysregulation of iron metabolism may have higher risk for hypertension than those with normal iron homeostasis.
[Mh] Termos MeSH primário: Proteínas Ligadas por GPI/genética
Predisposição Genética para Doença
Hipertensão/genética
Proteínas Reguladoras do Ferro/genética
[Mh] Termos MeSH secundário: Alelos
Estudos de Casos e Controles
Hipertensão Essencial
Feminino
Finlândia
Marcadores Genéticos
Variação Genética
Genótipo
Seres Humanos
Masculino
Meia-Idade
Sobrepeso/complicações
Sobrepeso/genética
Polimorfismo de Nucleotídeo Único
Fatores de Risco
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GPI-Linked Proteins); 0 (Genetic Markers); 0 (HFE2 protein, human); 0 (Iron-Regulatory Proteins)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170203
[St] Status:MEDLINE
[do] DOI:10.1097/MD.0000000000006052


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[PMID]:28131773
[Au] Autor:Wei Y; Yuan H; Xu P; Tan X
[Ad] Endereço:Department of Chemistry & Shanghai Key Laboratory of Chemical Biology for Protein Research, Institutes of Biomedical Sciences, Fudan University, Shanghai 200433, China.
[Ti] Título:Redox sensing molecular mechanism of an iron metabolism regulatory protein FBXL5.
[So] Source:Arch Biochem Biophys;616:30-39, 2017 Feb 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:FBXL5 is a subunit of the SCF ubiquitin ligase complex that targets the proteasomal degradation of iron regulatory protein IRP2, which is an important regulator in iron metabolism. The degradation of FBXL5 itself is regulated in an iron- and oxygen-responsive manner through its diiron center containing Hr-like domain. Although the crystal structure of the Hr-like domain of FBXL5 and its degradation based on iron/oxygen sensing has been reported, the redox sensing molecular mechanism is still not clear. Herein the redox properties of FBXL5 were investigated via EPR, direct electrochemistry, SRCD, fluorescence emission spectroscopy, and redox kinetics. The results indicated that the conformation and function of FBXL5 are tuned by the redox states of the diiron center. The redox reactions of the diiron center are accompanied with conformational changes and iron release, which are associated with FBXL5 stability and degradation. These results provide insights into the redox sensing mechanism by which FBXL5 can serve as an iron metabolism regulator within mammalian cells.
[Mh] Termos MeSH primário: Proteínas F-Box/química
Proteínas Reguladoras do Ferro/química
Oxirredução
Complexos Ubiquitina-Proteína Ligase/química
[Mh] Termos MeSH secundário: Dicroísmo Circular
Cristalografia por Raios X
Eletroquímica
Espectroscopia de Ressonância de Spin Eletrônica
Escherichia coli/metabolismo
Seres Humanos
Ferro/química
Cinética
Oxigênio/química
Domínios Proteicos
Espectrometria de Fluorescência
Espectrofotometria Ultravioleta
Síncrotrons
Triptofano/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (F-Box Proteins); 0 (FBXL5 protein, human); 0 (Iron-Regulatory Proteins); 8DUH1N11BX (Tryptophan); E1UOL152H7 (Iron); EC 2.3.2.23 (Ubiquitin-Protein Ligase Complexes); S88TT14065 (Oxygen)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170130
[St] Status:MEDLINE


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[PMID]:28001042
[Au] Autor:Cai K; Tonelli M; Frederick RO; Markley JL
[Ad] Endereço:Mitochondrial Protein Partnership, Center for Eukaryotic Structural Genomics, and ‡National Magnetic Resonance Facility at Madison, Biochemistry Department, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.
[Ti] Título:Human Mitochondrial Ferredoxin 1 (FDX1) and Ferredoxin 2 (FDX2) Both Bind Cysteine Desulfurase and Donate Electrons for Iron-Sulfur Cluster Biosynthesis.
[So] Source:Biochemistry;56(3):487-499, 2017 Jan 24.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ferredoxins play an important role as an electron donor in iron-sulfur (Fe-S) cluster biosynthesis. Two ferredoxins, human mitochondrial ferredoxin 1 (FDX1) and human mitochondrial ferredoxin 2 (FDX2), are present in the matrix of human mitochondria. Conflicting results have been reported regarding their respective function in mitochondrial iron-sulfur cluster biogenesis. We report here biophysical studies of the interaction of these two ferredoxins with other proteins involved in mitochondrial iron-sulfur cluster assembly. Results from nuclear magnetic resonance spectroscopy show that both FDX1 and FDX2 (in both their reduced and oxidized states) interact with the protein complex responsible for cluster assembly, which contains cysteine desulfurase (NFS1), ISD11 (also known as LYRM4), and acyl carrier protein (Acp). In all cases, ferredoxin residues close to the Fe-S cluster are involved in the interaction with this complex. Isothermal titration calorimetry results showed that FDX2 binds more tightly to the cysteine desulfurase complex than FDX1 does. The reduced form of each ferredoxin became oxidized in the presence of the cysteine desulfurase complex when l-cysteine was added, leading to its conversion to l-alanine and the generation of sulfide. In an in vitro reaction, the reduced form of each ferredoxin was found to support Fe-S cluster assembly on ISCU; the rate of cluster assembly was faster with FDX2 than with FDX1. Taken together, these results show that both FDX1 and FDX2 can function in Fe-S cluster assembly in vitro.
[Mh] Termos MeSH primário: Liases de Carbono-Enxofre/química
Ferredoxinas/química
Ferro/química
Enxofre/química
[Mh] Termos MeSH secundário: Proteína de Transporte de Acila/genética
Proteína de Transporte de Acila/metabolismo
Sequência de Aminoácidos
Animais
Liases de Carbono-Enxofre/genética
Liases de Carbono-Enxofre/metabolismo
Cisteína
Elétrons
Escherichia coli/genética
Escherichia coli/metabolismo
Ferredoxinas/genética
Ferredoxinas/metabolismo
Regulação da Expressão Gênica
Seres Humanos
Ferro/metabolismo
Proteínas de Ligação ao Ferro/genética
Proteínas de Ligação ao Ferro/metabolismo
Proteínas Reguladoras do Ferro/genética
Proteínas Reguladoras do Ferro/metabolismo
Proteínas com Ferro-Enxofre/genética
Proteínas com Ferro-Enxofre/metabolismo
Mitocôndrias/genética
Mitocôndrias/metabolismo
Modelos Moleculares
Oxirredução
Estrutura Secundária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Alinhamento de Sequência
Enxofre/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Carrier Protein); 0 (Ferredoxins); 0 (ISCU protein, human); 0 (ISD11 protein, human); 0 (Iron-Binding Proteins); 0 (Iron-Regulatory Proteins); 0 (Iron-Sulfur Proteins); 0 (Recombinant Proteins); 0 (frataxin); 70FD1KFU70 (Sulfur); E1UOL152H7 (Iron); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.- (NFS1 protein, human); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161222
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b00447


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[PMID]:27988301
[Au] Autor:Zaidi A; Singh KP; Ali V
[Ad] Endereço:Laboratory of Molecular Biochemistry and Cell Biology, Dept. of Biochemistry, Rajendra Memorial Research Institute of Medical Sciences (RMRIMS), Agamkuan, Patna, India.
[Ti] Título:Leishmania and its quest for iron: An update and overview.
[So] Source:Mol Biochem Parasitol;211:15-25, 2017 Jan.
[Is] ISSN:1872-9428
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Parasites of genus Leishmania are the causative agents of complex neglected diseases called leishmaniasis and continue to be a significant health concern globally. Iron is a vital nutritional requirement for virtually all organisms, including pathogenic trypanosomatid parasites, and plays a crucial role in many facets of cellular metabolism as a cofactor of several enzymes. Iron acquisition is essential for the survival of parasites. Yet parasites are also vulnerable to the toxicity of iron and reactive oxygen species. The aim of this review is to provide an update on the current knowledge about iron acquisition and usage by Leishmania species. We have also discussed about host strategy to modulate iron availability and the strategies deployed by Leishmania parasites to overcome iron withholding defences and thus favour parasite growth within host macrophages. Since iron plays central roles in the host's response and parasite metabolism, a comprehensive understanding of the iron metabolism is beneficial to identify potential viable therapeutic opportunities against leishmaniasis.
[Mh] Termos MeSH primário: Interações Hospedeiro-Parasita
Ferro/metabolismo
Leishmania/fisiologia
Leishmaniose/metabolismo
Leishmaniose/parasitologia
[Mh] Termos MeSH secundário: Animais
Transporte Biológico
Compostos Ferrosos/metabolismo
Seres Humanos
Imunomodulação
Quelantes de Ferro/farmacologia
Proteínas Reguladoras do Ferro/metabolismo
Leishmania/efeitos dos fármacos
Leishmaniose/imunologia
Macrófagos/metabolismo
Macrófagos/parasitologia
Oxirredução
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Ferrous Compounds); 0 (Iron Chelating Agents); 0 (Iron-Regulatory Proteins); E1UOL152H7 (Iron)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161219
[St] Status:MEDLINE



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