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[PMID]:28714084
[Au] Autor:Ji Z; LeBaron MJ
[Ad] Endereço:Toxicology and Environmental Research and Consulting, The Dow Chemical Company, Midland, Michigan, 48674.
[Ti] Título:Applying the erythrocyte Pig-a assay concept to rat epididymal sperm for germ cell mutagenicity evaluation.
[So] Source:Environ Mol Mutagen;58(7):485-493, 2017 Aug.
[Is] ISSN:1098-2280
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Pig-a assay, a recently developed in vivo somatic gene mutation assay, is based on the identification of mutant erythrocytes that have an altered repertoire of glycosylphosphatidylinositol (GPI)-anchored cell surface markers. We hypothesized that the erythrocyte Pig-a assay concept could be applied to rat cauda epididymal spermatozoa (sperm) for germ cell mutagenicity evaluation. We used GPI-anchored CD59 as the Pig-a mutation marker and examined the frequency of CD59-negative sperm using flow cytometry. A reconstruction experiment that spiked un-labeled sperm (mutant-mimic) into labeled sperm at specific ratios yielded good agreement between the detected and expected frequencies of mutant-mimic sperm, demonstrating the analytical ability for CD59-negative sperm detection. Furthermore, this methodology was assessed in F344/DuCrl rats administered N-ethyl-N-nitrosourea (ENU), a prototypical mutagen, or clofibrate, a lipid-lowering drug. Rats treated with 1, 10, or 20 mg/kg body weight/day (mkd) ENU via daily oral garage for five consecutive days showed a dose-dependent increase in the frequency of CD59-negative sperm on study day 63 (i.e., 58 days after the last ENU dose). This ENU dosing regimen also increased the frequency of CD59-negative erythrocytes. In rats treated with 300 mkd clofibrate via daily oral garage for consecutive 28 days, no treatment-related changes were detected in the frequency of CD59-negative sperm on study day 85 (i.e., 57 days after the last dose) or in the frequency of CD59-negative erythrocytes on study day 29. In conclusion, these data suggest that the epidiymal sperm Pig-a assay in rats is a promising method for evaluating germ cell mutagenicity. Environ. Mol. Mutagen. 58:485-493, 2017. © 2017 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Epididimo
Proteínas de Membrana/genética
Testes de Mutagenicidade/métodos
Mutagênicos/toxicidade
Espermatozoides/efeitos de drogas
[Mh] Termos MeSH secundário: Animais
Antígenos CD59/genética
Clofibrato/toxicidade
Eritrócitos/efeitos de drogas
Eritrócitos/metabolismo
Eritrócitos/patologia
Etilnitrosoureia/toxicidade
Citometria de Fluxo
Glicosilfosfatidilinositóis/biossíntese
Masculino
Ratos Endogâmicos F344
Espermatozoides/metabolismo
Espermatozoides/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD59); 0 (Glycosylphosphatidylinositols); 0 (Membrane Proteins); 0 (Mutagens); 0 (phosphatidylinositol glycan-class A protein); HPN91K7FU3 (Clofibrate); P8M1T4190R (Ethylnitrosourea)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170831
[Lr] Data última revisão:
170831
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170717
[St] Status:MEDLINE
[do] DOI:10.1002/em.22109


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[PMID]:27979168
[Au] Autor:Ji X; Li X; Ma Y; Li D
[Ad] Endereço:School of Chemical Engineering and Technology, Harbin Institute of Technology, Harbin, Heilongjiang 150090, China.
[Ti] Título:Differences in proteomic profiles of milk fat globule membrane in yak and cow milk.
[So] Source:Food Chem;221:1822-1827, 2017 Apr 15.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Milk fat globule membrane (MFGM) is an important milk component which is rich in bioactive proteins. In this work, the isobaric tags for relative and absolute quantitation (iTRAQ) proteomic approach was used to investigate the differences in the MFGM proteins between yak and cow milk. Over 450 proteins were identified between the yak and cow MFGM. The MFGM proteins with significant differences were compared based on the relative abundance. Proteins such as Glycosylation-dependent cell adhesion molecule 1 (GlyCAM1), CD59 molecule and lactadherin, were identified having a much higher abundance (4.6-10.1 fold) in yak MFGM than cow MFGM. These proteins are thought to have biological functions such as the antimicrobial and antitumor effects. This may be due to the need that yak produces high nutritive milk including high levels of bioactive compounds in order to resist the extreme high altitude environment.
[Mh] Termos MeSH primário: Glicolipídeos/química
Glicoproteínas/química
Leite/química
Proteômica
[Mh] Termos MeSH secundário: Animais
Antígenos CD59/química
Bovinos/classificação
Feminino
Proteínas do Leite/química
Mucinas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD59); 0 (Glycolipids); 0 (Glycoproteins); 0 (Milk Proteins); 0 (Mucins); 0 (milk fat globule); 145895-89-2 (sulfated glycoprotein p50)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161216
[St] Status:MEDLINE


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[PMID]:28533125
[Au] Autor:Hoffman WH; Artlett CM; Boodhoo D; Gilliland MGF; Ortiz L; Mulder D; Tjan DHT; Martin A; Tatomir A; Rus H
[Ad] Endereço:Department of Pediatrics, Medical College of Georgia, Augusta University, Augusta, GA 30912, United States. Electronic address: whoffman@augusta.edu.
[Ti] Título:Markers of immune-mediated inflammation in the brains of young adults and adolescents with type 1 diabetes and fatal diabetic ketoacidosis. Is there a difference?
[So] Source:Exp Mol Pathol;102(3):505-514, 2017 Jun.
[Is] ISSN:1096-0945
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Due to the limited data on diabetic ketoacidosis and brain edema (DKA/BE) in children/adolescents and the lack of recent data on adults with type 1 diabetes (T1D), we addressed the question of whether neuroinflammation was present in the fatal DKA of adults. We performed immunohistochemistry (IHC) studies on the brains of two young adults with T1D and fatal DKA and compared them with two teenagers with poorly controlled diabetes and fatal DKA. C5b-9, the membrane attack complex (MAC) had significantly greater deposits in the grey and white matter of the teenagers than the young adults (p=0.03). CD59, a MAC assembly inhibitory protein was absent, possibly suppressed by the hyperglycemia in the teenagers but was expressed in the young adults despite comparable average levels of hyperglycemia. The receptor for advanced glycation end products (RAGE) had an average expression in the young adults significantly greater than in the teenagers (p=0.02). The autophagy marker Light Chain 3 (LC3) A/B was the predominant form of programmed cell death (PCD) in the teenage brains. The young adults had high expressions of both LC3A/B and TUNEL, an apoptotic cell marker for DNA fragmentation. BE was present in the newly diagnosed young adult with hyperglycemic hyperosmolar DKA and also in the two teenagers. Our data indicate that significant differences in neuroinflammatory components, initiated by the dysregulation of DKA and interrelated metabolic and immunologic milieu, are likely present in the brains of fatal DKA of teenagers when compared with young adults.
[Mh] Termos MeSH primário: Biomarcadores/metabolismo
Diabetes Mellitus Tipo 1/genética
Cetoacidose Diabética/genética
Inflamação Neurogênica/genética
[Mh] Termos MeSH secundário: Adolescente
Adulto
Antígenos CD59/genética
Antígenos CD59/metabolismo
Autofagia
Encéfalo/fisiopatologia
Edema Encefálico/diagnóstico
Edema Encefálico/etiologia
Edema Encefálico/genética
Fragmentação do DNA
Diabetes Mellitus Tipo 1/complicações
Cetoacidose Diabética/complicações
Regulação da Expressão Gênica
Humanos
Imuno-Histoquímica
Marcação In Situ das Extremidades Cortadas
Mediadores da Inflamação/metabolismo
Proteínas Associadas aos Microtúbulos/genética
Proteínas Associadas aos Microtúbulos/metabolismo
Inflamação Neurogênica/etiologia
Adulto Jovem
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD59); 0 (Biomarkers); 0 (Inflammation Mediators); 0 (Microtubule-Associated Proteins); 0 (light chain 3, human); 101754-01-2 (CD59 protein, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170523
[St] Status:MEDLINE


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[PMID]:28345259
[Au] Autor:Blom AM
[Ad] Endereço:Division of Medical Protein Chemistry, Department of Translational Medicine, Lund University, Malmö, Sweden.
[Ti] Título:The role of complement inhibitors beyond controlling inflammation.
[So] Source:J Intern Med;282(2):116-128, 2017 Aug.
[Is] ISSN:1365-2796
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The complement system is an arm of innate immunity that aids in the removal of pathogens and dying cells. Due to its harmful, pro-inflammatory potential, complement is controlled by several soluble and membrane-bound inhibitors. This family of complement regulators has been recently extended by the discovery of several new members, and it is becoming apparent that these proteins harbour additional functions. In this review, the current state of knowledge of the physiological functions of four complement regulators will be described: cartilage oligomeric matrix protein (COMP), CUB and sushi multiple domains 1 (CSMD1), sushi domain-containing protein 4 (SUSD4) and CD59. Complement activation is involved in both the development of and defence against cancer. COMP expression is pro-oncogenic, whereas CSMD1 and SUSD4 act as tumour suppressors. These effects may be related in part to the complex influence of complement on cancer but also depend on unrelated functions such as the protection of cells from endoplasmic reticulum stress conveyed by intracellular COMP. CD59 is the main inhibitor of the membrane attack complex, and its deficiency leads to complement attack on erythrocytes and severe haemolytic anaemia, which is now amenable to treatment with an inhibitor of C5 cleavage. Unexpectedly, the intracellular pool of CD59 is crucial for insulin secretion from pancreatic ß-cells. This finding is one of several relating to the intracellular functions of complement proteins, which until recently were only considered to be present in the extracellular space. Understanding the alternative functions of complement inhibitors may unravel unexpected links between complement and other physiological systems, but is also important for better design of therapeutic complement inhibition.
[Mh] Termos MeSH primário: Proteínas do Sistema Complemento/fisiologia
[Mh] Termos MeSH secundário: Animais
Antígenos CD59/fisiologia
Proteína de Matriz Oligomérica de Cartilagem/fisiologia
Ativação do Complemento/fisiologia
Proteínas Inativadoras do Complemento/fisiologia
Humanos
Infecção/fisiopatologia
Inflamação/fisiopatologia
Artropatias/fisiopatologia
Proteínas de Membrana/fisiologia
Neoplasias/fisiopatologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antigens, CD59); 0 (COMP protein, human); 0 (CSMD1 protein, human); 0 (Cartilage Oligomeric Matrix Protein); 0 (Complement Inactivator Proteins); 0 (Membrane Proteins); 0 (SUSD4 protein, human); 9007-36-7 (Complement System Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170327
[St] Status:MEDLINE
[do] DOI:10.1111/joim.12606


  5 / 1455 MEDLINE  
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[PMID]:28516949
[Au] Autor:Hill A; DeZern AE; Kinoshita T; Brodsky RA
[Ad] Endereço:Department of Haematology, St. James' University Hospital, Leeds, UK.
[Ti] Título:Paroxysmal nocturnal haemoglobinuria.
[So] Source:Nat Rev Dis Primers;3:17028, 2017 May 18.
[Is] ISSN:2056-676X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Paroxysmal nocturnal haemoglobinuria (PNH) is a clonal haematopoietic stem cell (HSC) disease that presents with haemolytic anaemia, thrombosis and smooth muscle dystonias, as well as bone marrow failure in some cases. PNH is caused by somatic mutations in PIGA (which encodes phosphatidylinositol N-acetylglucosaminyltransferase subunit A) in one or more HSC clones. The gene product of PIGA is required for the biosynthesis of glycosylphosphatidylinositol (GPI) anchors; thus, PIGA mutations lead to a deficiency of GPI-anchored proteins, such as complement decay-accelerating factor (also known as CD55) and CD59 glycoprotein (CD59), which are both complement inhibitors. Clinical manifestations of PNH occur when a HSC clone carrying somatic PIGA mutations acquires a growth advantage and differentiates, generating mature blood cells that are deficient of GPI-anchored proteins. The loss of CD55 and CD59 renders PNH erythrocytes susceptible to intravascular haemolysis, which can lead to thrombosis and to much of the morbidity and mortality of PNH. The accumulation of anaphylatoxins (such as C5a) from complement activation might also have a role. The natural history of PNH is highly variable, ranging from quiescent to life-threatening. Therapeutic strategies include terminal complement blockade and bone marrow transplantation. Eculizumab, a monoclonal antibody complement inhibitor, is highly effective and the only licensed therapy for PNH.
[Mh] Termos MeSH primário: Hemoglobinúria Paroxística/patologia
Hemoglobinúria Paroxística/terapia
Proteínas de Membrana/genética
[Mh] Termos MeSH secundário: Anticorpos Monoclonais Humanizados/uso terapêutico
Antígenos CD55/metabolismo
Antígenos CD59/metabolismo
Transplante de Medula Óssea
Proteínas Inativadoras do Complemento/metabolismo
Hemoglobinúria Paroxística/genética
Hemoglobinúria Paroxística/metabolismo
Humanos
Mutação
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antibodies, Monoclonal, Humanized); 0 (Antigens, CD55); 0 (Antigens, CD59); 0 (Complement Inactivator Proteins); 0 (Membrane Proteins); 0 (phosphatidylinositol glycan-class A protein); 101754-01-2 (CD59 protein, human); A3ULP0F556 (eculizumab)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170518
[St] Status:MEDLINE
[do] DOI:10.1038/nrdp.2017.28


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[PMID]:27770464
[Au] Autor:Raschke M; Igl BW; Kenny J; Collins J; Dertinger SD; Labash C; Bhalli JA; Tebbe CC; McNeil KM; Sutter A
[Ad] Endereço:Bayer Pharma AG, Muellerstrasse 178, Berlin, 13353, Germany.
[Ti] Título:In Vivo Pig-a gene mutation assay: Guidance for 3Rs-friendly implementation.
[So] Source:Environ Mol Mutagen;57(9):678-686, 2016 Dec.
[Is] ISSN:1098-2280
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The rodent Pig-a assay is an in vivo method for the detection of gene mutation, where lack of glycosylphosphatidylinositol-anchored proteins on the surface of circulating red blood cells (RBCs) serves as a reporter for Pig-a gene mutation. In the case of rats, the frequency of mutant phenotype RBCs is measured via fluorescent anti-CD59 antibodies and flow cytometry. The Pig-a assay meets the growing expectations for novel approaches in animal experimentation not only focusing on the scientific value of the assay but also on animal welfare aspects (3Rs principles), for example, amenable to integration into pivotal rodent 28-day general toxicology studies. However, as recommended in the Organisation for Economic Co-operation and Development Test Guidelines for genotoxicity testing, laboratories are expected to demonstrate their proficiency. While this has historically involved the extensive use of animals, here we describe an alternative approach based on a series of blood dilutions covering a range of mutant frequencies. The experiments described herein utilized either non-fluorescent anti-CD59 antibodies to provide elevated numbers of mutant-like cells, or a low volume blood sample from a single N-ethyl-N-nitrosourea treated animal. Results from these so-called reconstruction experiments from four independent laboratories showed good overall precision (correlation coefficients: 0.9979-0.9999) and accuracy (estimated slope: 0.71-1.09) of mutant cell scoring, which was further confirmed by Bland-Altman analysis. These data strongly support the use of reconstruction experiments for training purposes and demonstrating laboratory proficiency with very few animals, an ideal situation given the typically conflicting goals of demonstrating laboratory proficiency and reducing the use of animals. Environ. Mol. Mutagen. 57:678-686, 2016. © 2016 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Alternativas ao Uso de Animais
Etilnitrosoureia/toxicidade
Proteínas de Membrana/genética
Testes de Mutagenicidade/métodos
Mutagênicos/toxicidade
Mutação
[Mh] Termos MeSH secundário: Bem-Estar do Animal
Animais
Antígenos CD59/análise
Eritrócitos/efeitos de drogas
Eritrócitos/metabolismo
Citometria de Fluxo
Guias como Assunto
Laboratórios/normas
Masculino
Ratos Endogâmicos
Reticulócitos/efeitos de drogas
Reticulócitos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD59); 0 (Membrane Proteins); 0 (Mutagens); 0 (phosphatidylinositol glycan-class A protein); P8M1T4190R (Ethylnitrosourea)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170609
[Lr] Data última revisão:
170609
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161022
[St] Status:MEDLINE
[do] DOI:10.1002/em.22060


  7 / 1455 MEDLINE  
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[PMID]:28330937
[Au] Autor:Kinoshita M; Suzuki KG; Matsumori N; Takada M; Ano H; Morigaki K; Abe M; Makino A; Kobayashi T; Hirosawa KM; Fujiwara TK; Kusumi A; Murata M
[Ad] Endereço:Lipid Active Structure Project, Exploratory Research for Advanced Technology Organization, Japan Science and Technology Agency, Osaka University, Osaka 560-0043, Japan.
[Ti] Título:Raft-based sphingomyelin interactions revealed by new fluorescent sphingomyelin analogs.
[So] Source:J Cell Biol;216(4):1183-1204, 2017 Apr 03.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sphingomyelin (SM) has been proposed to form cholesterol-dependent raft domains and sphingolipid domains in the plasma membrane (PM). How SM contributes to the formation and function of these domains remains unknown, primarily because of the scarcity of suitable fluorescent SM analogs. We developed new fluorescent SM analogs by conjugating a hydrophilic fluorophore to the SM choline headgroup without eliminating its positive charge, via a hydrophilic nonaethylene glycol linker. The new analogs behaved similarly to the native SM in terms of their partitioning behaviors in artificial liquid order-disorder phase-separated membranes and detergent-resistant PM preparations. Single fluorescent molecule tracking in the live-cell PM revealed that they indirectly interact with each other in cholesterol- and sphingosine backbone-dependent manners, and that, for ∼10-50 ms, they undergo transient colocalization-codiffusion with a glycosylphosphatidylinositol (GPI)-anchored protein, CD59 (in monomers, transient-dimer rafts, and clusters), in CD59-oligomer size-, cholesterol-, and GPI anchoring-dependent manners. These results suggest that SM continually and rapidly exchanges between CD59-associated raft domains and the bulk PM.
[Mh] Termos MeSH primário: Corantes Fluorescentes/metabolismo
Esfingomielinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Antígenos CD59/metabolismo
Células CHO
Linhagem Celular
Membrana Celular/metabolismo
Colesterol/metabolismo
Cricetulus
Detergentes/metabolismo
Glicosilfosfatidilinositóis/metabolismo
Interações Hidrofóbicas e Hidrofílicas
Microdomínios da Membrana/metabolismo
Esfingolipídeos/metabolismo
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD59); 0 (Detergents); 0 (Fluorescent Dyes); 0 (Glycosylphosphatidylinositols); 0 (Sphingolipids); 0 (Sphingomyelins); 101754-01-2 (CD59 protein, human); 97C5T2UQ7J (Cholesterol)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170531
[Lr] Data última revisão:
170531
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170323
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201607086


  8 / 1455 MEDLINE  
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[PMID]:28347253
[Au] Autor:Yang P; Li B; Yin QF; Wang YJ
[Ad] Endereço:Department of Biology, Medical College of Qingdao University, Qingdao, People's Republic of China.
[Ti] Título:Carboxymethyl chitosan nanoparticles coupled with CD59-specific ligand peptide for targeted delivery of C-phycocyanin to HeLa cells.
[So] Source:Tumour Biol;39(3):1010428317692267, 2017 Mar.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The combination of nanotechnology and medicine will be the next generation of vehicles for targeted drug delivery. Carboxymethyl chitosan loaded with the anticancer drug C-phycocyanin and the CD59-specific ligand peptide for cancer cell targeting were used to create C-phycocyanin/carboxymethyl chitosan-CD59-specific ligand peptide nanoparticles using the ionic-gelation method. Optimal synthesis conditions, selected by response surface methodology, comprised the ratio carboxymethyl chitosan:C-phycocyanin = 3:1, and carboxymethyl chitosan and CaCl concentrations of 2.0 and 1.0 mg/mL, respectively. The resulting nanoparticles were spherical, with diameters of approximately 200 nm; the entrapment efficient was about 65%; and the drug loading was about 20%. The release of C-phycocyanin from C-phycocyanin/carboxymethyl chitosan nanoparticles was pH sensitive and had a sustainable effect in vitro. Guided by the CD59-specific ligand peptide, the nanoparticles efficiently targeted the surface of HeLa cells and had an obvious inhibitory effect on HeLa cell proliferation as determined by methyl thiazolyl tetrazolium assays. The nanoparticles were hemocompatible and induced apoptosis by upregulation of cleaved caspase-3 and cleaved polyADP-ribose polymerase proteins, and downregulation of Bcl-2 proteins. Our study provides a novel approach to the research and development of marine drugs, and support for targeted therapy using anticancer drugs.
[Mh] Termos MeSH primário: Quitosana/análogos & derivados
Nanopartículas/administração & dosagem
Peptídeos/administração & dosagem
Ficocianina/administração & dosagem
[Mh] Termos MeSH secundário: Antígenos CD59/imunologia
Caspase 3/biossíntese
Quitosana/administração & dosagem
Quitosana/química
Sistemas de Liberação de Medicamentos
Liberação Controlada de Fármacos
Epitopos
Células HeLa
Humanos
Nanopartículas/química
Peptídeos/química
Peptídeos/imunologia
Ficocianina/química
Proteínas Proto-Oncogênicas c-bcl-2/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD59); 0 (Epitopes); 0 (Peptides); 0 (Proto-Oncogene Proteins c-bcl-2); 0 (carboxymethyl-chitosan); 101754-01-2 (CD59 protein, human); 11016-15-2 (Phycocyanin); 9012-76-4 (Chitosan); EC 3.4.22.- (Caspase 3)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170407
[Lr] Data última revisão:
170407
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170328
[St] Status:MEDLINE
[do] DOI:10.1177/1010428317692267


  9 / 1455 MEDLINE  
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[PMID]:27688119
[Au] Autor:Sui ZH; Li MF; Sun L
[Ad] Endereço:Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao, China; Laboratory for Marine Biology and Biotechnology, Qingdao National Laboratory for Marine Science and Technology, Qingdao, China; University of Chinese Academy of Sciences, Beijing, China.
[Ti] Título:Tongue sole (Cynoglossus semilaevis) CD59: A complement inhibitor that binds bacterial cells and promotes bacterial escape from the killing of fish serum.
[So] Source:Fish Shellfish Immunol;58:442-448, 2016 Nov.
[Is] ISSN:1095-9947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:CD59 is a complement regulatory protein that inhibits the formation of membrane attack complex of complement. In this study, we examined the expression and activity of tongue sole (Cynoglossus semilaevis) CD59 (CsCD59). CsCD59 possesses the conserved structural features of CD59 and shares 33%-46% sequence identities with other fish CD59. Expression of CsCD59 was high in liver, spleen, and muscle, and was stimulated by infection of bacterial pathogens. Recombinant CsCD59 (rCsCD59) exhibited an apparent inhibition effect on the activation of tongue sole serum complement. ELISA and microscopy detected binding of rCsCD59 to a number of Gram-negative and Gram-positive bacteria. Interaction with rCsCD59 did not affect bacterial viability but significantly enhanced bacterial resistance against the killing effect of fish serum. Together these results indicate that fish CD59 may to some degrees facilitate a general escape of bacteria from complement-mediated immunity.
[Mh] Termos MeSH primário: Antígenos CD59/genética
Proteínas Inativadoras do Complemento/genética
Doenças dos Peixes/genética
Proteínas de Peixes/genética
Linguados
Infecções por Bactérias Gram-Negativas/veterinária
Infecções por Bactérias Gram-Positivas/veterinária
[Mh] Termos MeSH secundário: Animais
Antígenos CD59/metabolismo
Sequência de Bases
Proteínas Inativadoras do Complemento/metabolismo
Doenças dos Peixes/imunologia
Doenças dos Peixes/microbiologia
Proteínas de Peixes/metabolismo
Regulação da Expressão Gênica
Bactérias Gram-Negativas/fisiologia
Infecções por Bactérias Gram-Negativas/genética
Infecções por Bactérias Gram-Negativas/imunologia
Infecções por Bactérias Gram-Negativas/microbiologia
Bactérias Gram-Positivas/fisiologia
Infecções por Bactérias Gram-Positivas/genética
Infecções por Bactérias Gram-Positivas/imunologia
Infecções por Bactérias Gram-Positivas/microbiologia
Alinhamento de Sequência/veterinária
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD59); 0 (Complement Inactivator Proteins); 0 (Fish Proteins)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170302
[Lr] Data última revisão:
170302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160930
[St] Status:MEDLINE


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[PMID]:27667587
[Au] Autor:Al-Faris L; Al-Rukhayes M; Al-Humood S
[Ad] Endereço:a Department of Pathology, Faculty of Medicine , Kuwait University , Safat , Kuwait.
[Ti] Título:Expression pattern of CD55 and CD59 on red blood cells in sickle cell disease.
[So] Source:Hematology;22(2):105-113, 2017 Mar.
[Is] ISSN:1607-8454
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVES: To investigate the pattern of CD55 and CD59 expression on RBCs of SCD patients, and its association with anemia, biochemical parameters of hemolysis, level of erythropoietin, and pro-inflammatory markers. METHODS: Flow cytometric analysis was performed on RBCs from 71 adult SCD patients and 53 healthy controls, using the commercial REDQUANT kit. RESULTS: CD59 deficiency was significantly higher among SCD patients than among healthy controls. The proportions of CD55-deficient and CD59-deficient RBCs from SCD patients were significantly higher when compared with those from healthy controls (0.17 vs. 0.09 and 2.1 vs. 1.2, respectively). The MFI of CD55 and CD59 expression on RBCs in SCD was significantly reduced when compared to the expression in healthy controls (5.2 vs. 6.4 and 19.4 vs 20.3, respectively). The pattern of CD55 and CD59 expression was not correlated with anemia, biomarkers of hemolysis, erythropoietin level, or other pro-inflammatory markers. DISCUSSION: There is an altered pattern of CD55 and CD59 expression on RBCs of SCD Patients; however, it does not seem to play a causal role in the pathophysiology of anemia, and is unlikely to be influenced by the level of erythropoietin or other inflammatory mediators.
[Mh] Termos MeSH primário: Anemia Falciforme/sangue
Anemia Falciforme/genética
Antígenos CD55/biossíntese
Antígenos CD59/biossíntese
Eritrócitos/metabolismo
[Mh] Termos MeSH secundário: Adulto
Antígenos CD55/sangue
Antígenos CD59/sangue
Eritropoetina/sangue
Feminino
Citometria de Fluxo
Humanos
Masculino
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD55); 0 (Antigens, CD59); 101754-01-2 (CD59 protein, human); 11096-26-7 (Erythropoietin)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170411
[Lr] Data última revisão:
170411
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160926
[St] Status:MEDLINE
[do] DOI:10.1080/10245332.2016.1231988



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