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[PMID]:28449718
[Au] Autor:Wang M; Zhao X; Zhu D; Liu T; Liang X; Liu F; Zhang Y; Dong X; Sun B
[Ad] Endereço:Department of Pathology, Tianjin Medical University, Tianjin, 300070, China.
[Ti] Título:HIF-1α promoted vasculogenic mimicry formation in hepatocellular carcinoma through LOXL2 up-regulation in hypoxic tumor microenvironment.
[So] Source:J Exp Clin Cancer Res;36(1):60, 2017 Apr 27.
[Is] ISSN:1756-9966
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The incidence and mortality rates of hepatocellular carcinoma (HCC) have steadily increased in recent years. A hypoxic microenvironment is one of the most important characteristics of solid tumors which has been shown to promote tumor metastasis, epithelial-mesenchymal transition and angiogenesis. Epithelial-mesenchymal transition and vasculogenic mimicry have been regarded as crucial contributing factors to cancer progression. HIF-1α functions as a master transcriptional regulator in the adaptive response to hypoxia. Lysyl oxidases like 2 (LOXL2) is a member of the lysyl oxidase family, which main function is to catalyze the covalent cross-linkages of collagen and elastin in the extracellular matrix. Recent work has demonstrated that HIF-1α promotes the expression of LOXL2, which is believed to amplify tumor aggressiveness. LOXL2 has shown to promote metastasis and is correlated with poor prognosis in hepatocellular carcinoma. The purpose of our study is to explore the role of HIF-1α in progression and metastasis of hepatocellular carcinoma by promoting the expression of LOXL2 as well as the potential regulatory mechanism. METHODS: HIF-1α, LOXL2 expression and CD31/periodic acid-Schiff double staining in HCC patient samples were examined by immunohistochemical staining. shRNA plasmids against HIF-1α was used to determine whether LOXL2 been increased by HIF-1α. We monitored a series of rescue assays to demonstrate our hypothesis that LOXL2 is required and sufficient for HIF-1α induced EMT and VM formation, which mediates cellular transformation and takes effect in cellular invasion. Then we performed GeneChip® Human Transcriptome Array (HTA) 2.0 in HepG2 cells, HepG2 cells overexpressed LOXL2 and HepG2 cells treated with CoCl . RESULTS: In clinical HCC tissues, it confirmed a positive relationship between HIF-1α and LOXL2 protein. Importantly, HIF-1α and LOXL2 high expression and the presence of vasculogenic mimicry were correlated to poor prognosis. HIF-1α was found to induce EMT, HCC cell migration, invasion and VM formation by regulating LOXL2. The results of microarray assays were analyzed. CONCLUSION: HIF-1α plays an important role in the development of HCC by promoting HCC metastasis, EMT and VM through up-regulating LOXL2. This study highlights the potential therapeutic value of targeting LOXL2 for suppression of HCC metastasis and progression.
[Mh] Termos MeSH primário: Aminoácido Oxirredutases/genética
Carcinoma Hepatocelular/genética
Carcinoma Hepatocelular/metabolismo
Regulação Neoplásica da Expressão Gênica
Subunidade alfa do Fator 1 Induzível por Hipóxia/metabolismo
Neoplasias Hepáticas/genética
Neoplasias Hepáticas/metabolismo
[Mh] Termos MeSH secundário: Adulto
Idoso
Biomarcadores
Carcinoma Hepatocelular/mortalidade
Carcinoma Hepatocelular/patologia
Linhagem Celular Tumoral
Biologia Computacional/métodos
Progressão da Doença
Feminino
Perfilação da Expressão Gênica
Ontologia Genética
Estudo de Associação Genômica Ampla
Seres Humanos
Hipóxia
Estimativa de Kaplan-Meier
Neoplasias Hepáticas/mortalidade
Neoplasias Hepáticas/patologia
Masculino
Meia-Idade
Gradação de Tumores
Metástase Neoplásica
Neovascularização Patológica
Prognóstico
Carga Tumoral
Microambiente Tumoral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Hypoxia-Inducible Factor 1, alpha Subunit); EC 1.4.- (Amino Acid Oxidoreductases); EC 1.4.3.- (LOXL2 protein, human)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1186/s13046-017-0533-1


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[PMID]:29273565
[Au] Autor:Maier MY; Luks L; Baudendistel OR; Wittmann V; Dietrich DR
[Ad] Endereço:Human and Environmental Toxicology, Department of Biology, University of Konstanz, Germany; Konstanz Research School Chemical Biology (KoRS-CB), University of Konstanz, Germany.
[Ti] Título:Identification of d-amino acid oxidase and propiverine interaction partners and their potential role in the propiverine-mediated nephropathy.
[So] Source:Chem Biol Interact;281:69-80, 2018 Feb 01.
[Is] ISSN:1872-7786
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Propiverine, a frequently-prescribed pharmaceutical for the treatment of symptoms associated with overactive bladder syndrome, provoked massive intranuclear and cytosolic protein inclusions in rat proximal tubule epithelium, primarily consisting of the peroxisomal targeting signal 1 (PTS1) containing protein d-amino acid oxidase (DAAO). As this type of nephropathy was also observed for other drugs, the aim was to determine whether propiverine interferes with trafficking and/or import of peroxisomal proteins. To elucidate this, DAAO- and propiverine-specific interaction partners from human HEK293 and rat WKPT cell lines and rat kidney and liver homogenate were determined using co-immunoprecipitation with subsequent nano-ESI-LC-MS/MS analyses. Corroboration of the role of DAAO- and/or propiverine-specific interaction partners in the drug-induced DAAO accumulation was sought via specific immunofluorescence staining of rat kidney sections from control and propiverine-treated rats. Above analyses demonstrated the interaction of propiverine with several protein classes, foremost peroxisomal proteins (DAAO, MFE2, HAOX2) and proteins of the protein quality control system, i.e. chaperones (HSP70 and DnaJ co-chaperones), proteases and proteasomal proteins (regulatory subunits of the 26S proteasome; Rpn1/2). The immunofluorescence analysis revealed mislocalization of many PTS1-proteins (DAAO, CAT, MFE2, ACOX1, EHHADH) in rat renal sections, strongly suggesting that propiverine primarily binds to PTS1 proteins resulting in the formation of PTS1 but not PTS2 or peroxisomal membrane protein (PMP) accumulations. Moreover, chaperones involved in peroxisomal trafficking (HSC70, DnaJB1) and peroxisomal biogenesis factor proteins (PEX3, PEX5, PEX7), also presented with distinct mislocalization patterns. Concomitantly, an increased number of peroxisomes was observed, suggestive of a compensatory mechanism for the presumably suboptimally functioning peroxisomes. Overall, the data presented suggested that propiverine interacts exclusively with DAAO or with a selected number of PTS1 proteins. The consequence of this interaction is the abrogated trafficking and peroxisomal import of PTS1 proteins concomitant with their nuclear and cytosolic accumulation due to inhibited degradation and imbalanced protein homeostasis.
[Mh] Termos MeSH primário: Aminoácido Oxirredutases/metabolismo
Benzilatos/metabolismo
Nefropatias Diabéticas/etiologia
[Mh] Termos MeSH secundário: 17-Hidroxiesteroide Desidrogenases/metabolismo
Oxirredutases do Álcool/metabolismo
Aminoácido Oxirredutases/química
Aminoácido Oxirredutases/genética
Animais
Benzilatos/química
Benzilatos/toxicidade
Linhagem Celular
Cromatografia Líquida de Alta Pressão
Células HEK293
Seres Humanos
Imunoprecipitação
Rim/metabolismo
Rim/patologia
Fígado/metabolismo
Microscopia Confocal
Chaperonas Moleculares/metabolismo
Proteína Multifuncional do Peroxissomo-2/metabolismo
Receptor 1 de Sinal de Orientação para Peroxissomos/química
Receptor 1 de Sinal de Orientação para Peroxissomos/metabolismo
Transporte Proteico/efeitos dos fármacos
Ratos
Proteínas Recombinantes de Fusão/biossíntese
Proteínas Recombinantes de Fusão/química
Espectrometria de Massas por Ionização por Electrospray
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzilates); 0 (Molecular Chaperones); 0 (Peroxisome-Targeting Signal 1 Receptor); 0 (Recombinant Fusion Proteins); 468GE2241L (propiverine); EC 1.1.- (17-Hydroxysteroid Dehydrogenases); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.119 (Hsd17b4 protein, rat); EC 1.4.- (Amino Acid Oxidoreductases); EC 4.2.1.107 (Peroxisomal Multifunctional Protein-2)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171224
[St] Status:MEDLINE


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[PMID]:28957411
[Au] Autor:Hodge-Hanson KM; Downs DM
[Ad] Endereço:Department of Microbiology, University of Georgia, Athens, Georgia, United States of America.
[Ti] Título:Members of the Rid protein family have broad imine deaminase activity and can accelerate the Pseudomonas aeruginosa D-arginine dehydrogenase (DauA) reaction in vitro.
[So] Source:PLoS One;12(9):e0185544, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Rid (YjgF/YER057c/UK114) protein family is a group of small, sequence diverse proteins that consists of eight subfamilies. The archetypal RidA subfamily is found in all domains, while the Rid1-7 subfamilies are present only in prokaryotes. Bacterial genomes often encode multiple members of the Rid superfamily. The best characterized member of this protein family, RidA from Salmonella enterica, is a deaminase that quenches the reactive metabolite 2-aminoacrylate generated by pyridoxal 5'-phosphate-dependent enzymes and ultimately spares certain enzymes from damage. The accumulation of 2-aminoacrylate can damage enzymes and lead to growth defects in bacteria, plants, and yeast. While all subfamily members have been annotated as imine deaminases based on the RidA characterization, experimental evidence to support this annotation exists for a single protein outside the RidA subfamily. Here we report that six proteins, spanning Rid subfamilies 1-3, deaminate a variety of imine/enamine substrates with differing specific activities. Proteins from the Rid2 and Rid3 subfamilies, but not from the RidA and Rid1 subfamilies deaminated iminoarginine, generated in situ by the Pseudomonas aeruginosa D-arginine dehydrogenase DauA. These data biochemically distinguished the subfamilies and showed Rid proteins have activity on a metabolite that is physiologically relevant in Pseudomonas and other bacteria.
[Mh] Termos MeSH primário: Aminoácido Oxirredutases/metabolismo
Aminoidrolases/metabolismo
Proteínas de Bactérias/metabolismo
Pseudomonas aeruginosa/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Aminoidrolases/química
Aminoidrolases/genética
Mutação
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 1.4.- (Amino Acid Oxidoreductases); EC 1.4.3.- (arginine oxidase); EC 3.5.4.- (Aminohydrolases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170929
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185544


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[PMID]:28872461
[Au] Autor:Wei Y; Kim TJ; Peng DH; Duan D; Gibbons DL; Yamauchi M; Jackson JR; Le Saux CJ; Calhoun C; Peters J; Derynck R; Backes BJ; Chapman HA
[Ad] Endereço:Department of Medicine, UCSF Cardiovascular Research Institute, San Francisco, California, USA.
[Ti] Título:Fibroblast-specific inhibition of TGF-ß1 signaling attenuates lung and tumor fibrosis.
[So] Source:J Clin Invest;127(10):3675-3688, 2017 Oct 02.
[Is] ISSN:1558-8238
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:TGF-ß1 signaling is a critical driver of collagen accumulation and fibrotic disease but also a vital suppressor of inflammation and epithelial cell proliferation. The nature of this multifunctional cytokine has limited the development of global TGF-ß1 signaling inhibitors as therapeutic agents. We conducted phenotypic screens for small molecules that inhibit TGF-ß1-induced epithelial-mesenchymal transition without immediate TGF-ß1 receptor (TßR) kinase inhibition. We identified trihydroxyphenolic compounds as potent blockers of TGF-ß1 responses (IC50 ~50 nM), Snail1 expression, and collagen deposition in vivo in models of pulmonary fibrosis and collagen-dependent lung cancer metastasis. Remarkably, the functional effects of trihydroxyphenolics required the presence of active lysyl oxidase-like 2 (LOXL2), thereby limiting effects to fibroblasts or cancer cells, the major LOXL2 producers. Mechanistic studies revealed that trihydroxyphenolics induce auto-oxidation of a LOXL2/3-specific lysine (K731) in a time-dependent reaction that irreversibly inhibits LOXL2 and converts the trihydrophenolic to a previously undescribed metabolite that directly inhibits TßRI kinase. Combined inhibition of LOXL2 and TßRI activities by trihydrophenolics resulted in potent blockade of pathological collagen accumulation in vivo without the toxicities associated with global inhibitors. These findings elucidate a therapeutic approach to attenuate fibrosis and the disease-promoting effects of tissue stiffness by specifically targeting TßRI kinase in LOXL2-expressing cells.
[Mh] Termos MeSH primário: Inibidores Enzimáticos
Transição Epitelial-Mesenquimal
Fibroblastos/metabolismo
Neoplasias Pulmonares
Proteínas de Neoplasias/antagonistas & inibidores
Proteínas de Neoplasias/metabolismo
Proteínas Serina-Treonina Quinases/antagonistas & inibidores
Fibrose Pulmonar
Receptores de Fatores de Crescimento Transformadores beta/antagonistas & inibidores
Transdução de Sinais/efeitos dos fármacos
Fator de Crescimento Transformador beta1/metabolismo
[Mh] Termos MeSH secundário: Células A549
Aminoácido Oxirredutases/genética
Aminoácido Oxirredutases/metabolismo
Animais
Ensaios de Seleção de Medicamentos Antitumorais
Inibidores Enzimáticos/química
Inibidores Enzimáticos/farmacologia
Fibroblastos/patologia
Seres Humanos
Neoplasias Pulmonares/tratamento farmacológico
Neoplasias Pulmonares/genética
Neoplasias Pulmonares/metabolismo
Camundongos
Metástase Neoplásica
Proteínas de Neoplasias/genética
Fenóis/química
Fenóis/farmacologia
Inibidores de Proteínas Quinases/farmacologia
Proteínas Serina-Treonina Quinases/genética
Proteínas Serina-Treonina Quinases/metabolismo
Fibrose Pulmonar/tratamento farmacológico
Fibrose Pulmonar/genética
Fibrose Pulmonar/metabolismo
Fibrose Pulmonar/patologia
Receptores de Fatores de Crescimento Transformadores beta/genética
Receptores de Fatores de Crescimento Transformadores beta/metabolismo
Fator de Crescimento Transformador beta1/antagonistas & inibidores
Fator de Crescimento Transformador beta1/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Neoplasm Proteins); 0 (Phenols); 0 (Protein Kinase Inhibitors); 0 (Receptors, Transforming Growth Factor beta); 0 (TGFB1 protein, human); 0 (Tgfb1 protein, mouse); 0 (Transforming Growth Factor beta1); EC 1.4.- (Amino Acid Oxidoreductases); EC 1.4.3.- (LOXL2 protein, human); EC 1.4.3.- (Loxl2 protein, mouse); EC 2.7.1.11 (TGF-beta type I receptor); EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171021
[Lr] Data última revisão:
171021
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170906
[St] Status:MEDLINE


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[PMID]:28864775
[Au] Autor:López-Jiménez AJ; Basak T; Vanacore RM
[Ad] Endereço:From the Department of Medicine, Division of Nephrology and Hypertension and.
[Ti] Título:Proteolytic processing of lysyl oxidase-like-2 in the extracellular matrix is required for crosslinking of basement membrane collagen IV.
[So] Source:J Biol Chem;292(41):16970-16982, 2017 Oct 13.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lysyl oxidase-like-2 (LOXL2) is an enzyme secreted into the extracellular matrix that crosslinks collagens by mediating oxidative deamination of lysine residues. Our previous work demonstrated that this enzyme crosslinks the 7S domain, a structural domain that stabilizes collagen IV scaffolds in the basement membrane. Despite its relevant role in extracellular matrix biosynthesis, little is known about the structural requirements of LOXL2 that enable collagen IV crosslinking. In this study, we demonstrate that LOXL2 is processed extracellularly by serine proteases, generating a 65-kDa form lacking the first two scavenger receptor cysteine-rich domains. Site-specific mutagenesis to prevent proteolytic processing generated a full-length enzyme that is active toward a soluble substrate, but fails to crosslink insoluble collagen IV within the extracellular matrix. In contrast, the processed form of LOXL2 binds to collagen IV and crosslinks the 7S domain. Together, our data demonstrate that proteolytic processing is an important event that allows LOXL2-mediated crosslinking of basement membrane collagen IV.
[Mh] Termos MeSH primário: Aminoácido Oxirredutases/secreção
Membrana Basal/metabolismo
Colágeno Tipo IV/metabolismo
Matriz Extracelular/metabolismo
Processamento de Proteína Pós-Traducional/fisiologia
Proteólise
[Mh] Termos MeSH secundário: Aminoácido Oxirredutases/genética
Colágeno Tipo IV/genética
Matriz Extracelular/genética
Células HEK293
Seres Humanos
Mutagênese Sítio-Dirigida
Domínios Proteicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Collagen Type IV); EC 1.4.- (Amino Acid Oxidoreductases); EC 1.4.3.- (LOXL2 protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170903
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.798603


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[PMID]:28859141
[Au] Autor:Maccarana M; Svensson RB; Knutsson A; Giannopoulos A; Pelkonen M; Weis M; Eyre D; Warman M; Kalamajski S
[Ad] Endereço:Department of Experimental Medical Sciences, Lund University, Lund, Sweden.
[Ti] Título:Asporin-deficient mice have tougher skin and altered skin glycosaminoglycan content and structure.
[So] Source:PLoS One;12(8):e0184028, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The main structural component of connective tissues is fibrillar, cross-linked collagen whose fibrillogenesis can be modulated by Small Leucine-Rich Proteins/Proteoglycans (SLRPs). Not all SLRPs' effects on collagen and extracellular matrix in vivo have been elucidated; one of the less investigated SLRPs is asporin. Here we describe the successful generation of an Aspn-/- mouse model and the investigation of the Aspn-/- skin phenotype. Functionally, Aspn-/- mice had an increased skin mechanical toughness, although there were no structural changes present on histology or immunohistochemistry. Electron microscopy analyses showed 7% thinner collagen fibrils in Aspn-/- mice (not statistically significant). Several matrix genes were upregulated, including collagens (Col1a1, Col1a2, Col3a1), matrix metalloproteinases (Mmp2, Mmp3) and lysyl oxidases (Lox, Loxl2), while lysyl hydroxylase (Plod2) was downregulated. Intriguingly no differences were observed in collagen protein content or in collagen cross-linking-related lysine oxidation or hydroxylation. The glycosaminoglycan content and structure in Aspn-/- skin was profoundly altered: chondroitin/dermatan sulfate was more than doubled and had an altered composition, while heparan sulfate was halved and had a decreased sulfation. Also, decorin and biglycan were doubled in Aspn-/- skin. Overall, asporin deficiency changes skin glycosaminoglycan composition, and decorin and biglycan content, which may explain the changes in skin mechanical properties.
[Mh] Termos MeSH primário: Biglicano/genética
Decorina/genética
Proteínas da Matriz Extracelular/deficiência
Efeito Fundador
Regulação da Expressão Gênica
Pele/metabolismo
[Mh] Termos MeSH secundário: Aminoácido Oxirredutases/genética
Aminoácido Oxirredutases/metabolismo
Animais
Biglicano/metabolismo
Sulfatos de Condroitina/genética
Sulfatos de Condroitina/metabolismo
Colágeno Tipo I/genética
Colágeno Tipo I/metabolismo
Colágeno Tipo III/genética
Colágeno Tipo III/metabolismo
Decorina/metabolismo
Dermatan Sulfato/análogos & derivados
Dermatan Sulfato/genética
Dermatan Sulfato/metabolismo
Matriz Extracelular/genética
Matriz Extracelular/metabolismo
Proteínas da Matriz Extracelular/genética
Feminino
Heparitina Sulfato/genética
Heparitina Sulfato/metabolismo
Sulfato de Ceratano/genética
Sulfato de Ceratano/metabolismo
Masculino
Metaloproteinase 2 da Matriz/genética
Metaloproteinase 2 da Matriz/metabolismo
Metaloproteinase 3 da Matriz/genética
Metaloproteinase 3 da Matriz/metabolismo
Camundongos
Camundongos Knockout
Fenótipo
Pró-Colágeno-Lisina 2-Oxoglutarato 5-Dioxigenase/genética
Pró-Colágeno-Lisina 2-Oxoglutarato 5-Dioxigenase/metabolismo
Pele/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aspn protein, mouse); 0 (Biglycan); 0 (COL3A1 protein, mouse); 0 (Col1a2 protein, mouse); 0 (Collagen Type I); 0 (Collagen Type III); 0 (Dcn protein, mouse); 0 (Decorin); 0 (Extracellular Matrix Proteins); 0 (collagen type I, alpha 1 chain); 0 (dermatan sulfate chondroitin sulfate); 24967-94-0 (Dermatan Sulfate); 9007-28-7 (Chondroitin Sulfates); 9050-30-0 (Heparitin Sulfate); 9056-36-4 (Keratan Sulfate); EC 1.14.11.4 (Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase); EC 1.14.11.4 (lysyl hydroxylase 2, mouse); EC 1.4.- (Amino Acid Oxidoreductases); EC 1.4.3.- (Loxl2 protein, mouse); EC 3.4.24.17 (Matrix Metalloproteinase 3); EC 3.4.24.17 (Mmp3 protein, mouse); EC 3.4.24.24 (Matrix Metalloproteinase 2); EC 3.4.24.24 (Mmp2 protein, mouse)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170901
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184028


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[PMID]:28845540
[Au] Autor:Brown KL; Cummings CF; Vanacore RM; Hudson BG
[Ad] Endereço:Department of Medicine, Vanderbilt University Medical Center, Nashville, Tennessee, 37232.
[Ti] Título:Building collagen IV smart scaffolds on the outside of cells.
[So] Source:Protein Sci;26(11):2151-2161, 2017 Nov.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Collagen IV scaffolds assemble through an intricate pathway that begins intracellularly and is completed extracellularly. Multiple intracellular enzymes act in concert to assemble collagen IV protomers, the building blocks of collagen IV scaffolds. After being secreted from cells, protomers are activated to initiate oligomerization, forming insoluble networks that are structurally reinforced with covalent crosslinks. Within these networks, embedded binding sites along the length of the protomer lead to the "decoration" of collagen IV triple helix with numerous functional molecules. We refer to these networks as "smart" scaffolds, which as a component of the basement membrane enable the development and function of multicellular tissues in all animal phyla. In this review, we present key molecular mechanisms that drive the assembly of collagen IV smart scaffolds.
[Mh] Termos MeSH primário: Aminoácido Oxirredutases/genética
Antígenos de Neoplasias/genética
Colágeno Tipo IV/química
Matriz Extracelular/metabolismo
Subunidades Proteicas/química
Receptores de Interleucina-1/genética
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Aminoácido Oxirredutases/metabolismo
Animais
Antígenos de Neoplasias/metabolismo
Membrana Basal/metabolismo
Membrana Basal/ultraestrutura
Colágeno Tipo IV/genética
Colágeno Tipo IV/metabolismo
Células Eucarióticas/metabolismo
Células Eucarióticas/ultraestrutura
Matriz Extracelular/ultraestrutura
Regulação da Expressão Gênica
Seres Humanos
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Estrutura Secundária de Proteína
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
Receptores de Interleucina-1/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antigens, Neoplasm); 0 (Collagen Type IV); 0 (PXDN protein, human); 0 (Protein Subunits); 0 (Receptors, Interleukin-1); EC 1.4.- (Amino Acid Oxidoreductases); EC 1.4.3.- (LOXL2 protein, human)
[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:170829
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3283


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[PMID]:28829846
[Au] Autor:Park HL; Kim JH; Jung Y; Park CK
[Ad] Endereço:Department of Ophthalmology and Visual Science, College of Medicine, The Catholic University of Korea, Seoul St. Mary's Hospital, Seoul, Korea.
[Ti] Título:Racial Differences in the Extracellular Matrix and Histone Acetylation of the Lamina Cribrosa and Peripapillary Sclera.
[So] Source:Invest Ophthalmol Vis Sci;58(10):4143-4154, 2017 Aug 01.
[Is] ISSN:1552-5783
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Purpose: We investigated the extracellular matrix (ECM) of the lamina cribrosa (LC) and peripapillary sclera (PPS) and compared histone acetylation and related enzymes to identify racial differences between Korean and Caucasian donor eyes. Methods: Posterior segment tissues were obtained from 30 Caucasian donors and 42 age and axial length-matched Korean donors. Histone modification was assessed for histone deacetylase (HDAC) 2, HDAC3, and acetylated histone H3. The promoter regions of the major ECM in the LC and PPS including collagen type I and III, and elastic fiber components (elastin and fibrillin-1) and lysyl oxidase enzymes including lysyl oxidase-like 1 and 2 (LOXL2) were evaluated by chromatin immunoprecipitation (ChIP) assay. Protein and mRNA expression of major ECM components were assessed using real-time polymerase chain reaction analysis, western blot analysis, and immunohistochemical staining. Results: HDAC2 and HDAC3 expression levels were decreased and acetylated histone H3 was increased in the LC and PPS of Korean eyes than Caucasian eyes. The promoter regions of LOXL2, elastin, and fribrillin-1 genes were highly acetylated in Korean LC. Expression of LOXL2 and elastic fiber components (elastin and fibrillin-1) were significantly increased in Korean LC and PPS than Caucasians according to the real-time polymerase chain reaction, western blot analyses, and quantification of elastic fiber staining. Conclusions: Histone acetylation status differed in the promoter regions of the elastic fiber components and LOXL2 in the LC and PPS according to race. Further study to reveal the association with these findings to the pathogenesis of glaucoma in Korean eyes is needed.
[Mh] Termos MeSH primário: Grupo com Ancestrais do Continente Asiático
Grupo com Ancestrais do Continente Europeu
Matriz Extracelular/metabolismo
Histona Desacetilase 2/metabolismo
Histona Desacetilases/metabolismo
Disco Óptico/metabolismo
Esclera/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Adulto
Idoso
Aminoácido Oxirredutases/metabolismo
Western Blotting
Elastina/metabolismo
Feminino
Fibrilina-1/metabolismo
Seres Humanos
Masculino
Meia-Idade
Regiões Promotoras Genéticas/fisiologia
Reação em Cadeia da Polimerase em Tempo Real
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fibrillin-1); 9007-58-3 (Elastin); EC 1.4.- (Amino Acid Oxidoreductases); EC 1.4.3.- (LOXL2 protein, human); EC 3.5.1.98 (Histone Deacetylase 2); EC 3.5.1.98 (Histone Deacetylases); EC 3.5.1.98 (histone deacetylase 3)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170828
[Lr] Data última revisão:
170828
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170823
[St] Status:MEDLINE
[do] DOI:10.1167/iovs.17-21474


  9 / 5274 MEDLINE  
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[PMID]:28711799
[Au] Autor:Zheng J; Yang T; Zhou J; Xu M; Zhang X; Rao Z; Yang S
[Ad] Endereço:The Key Laboratory of Industrial Biotechnology of Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, China.
[Ti] Título:Efficient production of d-amino acid oxidase in Escherichia coli by a trade-off between its expression and biomass using N-terminal modification.
[So] Source:Bioresour Technol;243:716-723, 2017 Nov.
[Is] ISSN:1873-2976
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Native d-amino acid oxidase (DAAO) that is expressed mostly as inclusion body and its toxicity for E. coli hamper efficient heterologous expression. In this study, the soluble expression of DAAO from Rhodosporidium toruloides (RtDAAO) was improved in E. coli through N-terminal modification, but the cell biomass was decreased. Then a trade-off between DAAO expression and biomass was achieved to obtain the highest volumetric activity of DAAO through regulated the number of N-terminus histidine residues. When variant H G was fused with three N-terminus histidine residues, the volumetric activity was increased by 3.1 times and the biomass was not significant change compared with the wild type. Finally, the N-terminus disordered region of RtDAAO (HSQK) was replaced with HHHG and the variant enzyme activity reached 80.7U/mL (with a 40 percent of inactive DAAO reduced) in a 7.5L fermenter in 24h.
[Mh] Termos MeSH primário: Aminoácido Oxirredutases
Escherichia coli
[Mh] Termos MeSH secundário: Aminoácidos
Biomassa
Reatores Biológicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); EC 1.4.- (Amino Acid Oxidoreductases)
[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:170717
[St] Status:MEDLINE


  10 / 5274 MEDLINE  
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[PMID]:28700220
[Au] Autor:Chow C; Hegde S; Blanchard JS
[Ad] Endereço:Department of Biochemistry, Albert Einstein College of Medicine , 1300 Morris Park Avenue, Bronx, New York 10461, United States.
[Ti] Título:Mechanistic Characterization of Escherichia coli l-Aspartate Oxidase from Kinetic Isotope Effects.
[So] Source:Biochemistry;56(31):4044-4052, 2017 Aug 08.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:l-Aspartate oxidase, encoded by the nadB gene, is the first enzyme in the de novo synthesis of NAD in bacteria. This FAD-dependent enzyme catalyzes the oxidation of l-aspartate to generate iminoaspartate and reduced flavin. Distinct from most amino acid oxidases, it can use either molecular oxygen or fumarate to reoxidize the reduced enzyme. Sequence alignments and the three-dimensional crystal structure have revealed that the overall fold and catalytic residues of NadB closely resemble those of the succinate dehydrogenase/fumarate reductase family rather than those of the prototypical d-amino acid oxidases. This suggests that the enzyme can catalyze amino acid oxidation via typical amino acid oxidase chemistry, involving the removal of protons from the α-amino group and the transfer of the hydride from C2, or potentially deprotonation at C3 followed by transfer of the hydride from C2, similar to chemistry occurring during succinate oxidation. We have investigated this potential mechanistic ambiguity using a combination of primary, solvent, and multiple deuterium kinetic isotope effects in steady state experiments. Our results indicate that the chemistry is similar to that of typical amino acid oxidases in which the transfer of the hydride from C2 of l-aspartate to FAD is rate-limiting and occurs in a concerted manner with respect to deprotonation of the α-amine. Together with previous kinetic and structural data, we propose that NadB has structurally evolved from succinate dehydrogenase/fumarate reductase-type enzymes to gain the new functionality of oxidizing amino acids while retaining the ability to reduce fumarate.
[Mh] Termos MeSH primário: Aminoácido Oxirredutases/metabolismo
Ácido Aspártico/metabolismo
Coenzimas/metabolismo
Escherichia coli K12/enzimologia
Proteínas de Escherichia coli/metabolismo
Flavina-Adenina Dinucleotídeo/metabolismo
Modelos Moleculares
[Mh] Termos MeSH secundário: Algoritmos
Aminoácido Oxirredutases/química
Aminoácido Oxirredutases/genética
Animais
Ácido Aspártico/química
Sítios de Ligação
Biocatálise
Domínio Catalítico
Coenzimas/química
Medição da Troca de Deutério
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/genética
Flavina-Adenina Dinucleotídeo/química
Concentração de Íons de Hidrogênio
Cinética
Malato Desidrogenase/metabolismo
Oxirredução
Conformação Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Sus scrofa
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Coenzymes); 0 (Escherichia coli Proteins); 0 (Recombinant Proteins); 146-14-5 (Flavin-Adenine Dinucleotide); 30KYC7MIAI (Aspartic Acid); EC 1.1.1.37 (Malate Dehydrogenase); EC 1.4.- (Amino Acid Oxidoreductases); EC 1.4.3.16 (L-aspartate oxidase, E coli)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170713
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00307



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