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[PMID]:29083052
[Au] Autor:Erazo-Borrás LV; Álvarez-Álvarez JA; Perez-Romero CA; Orrego-Arango JC; Franco-Restrepo JL; Trujillo-Vargas CM
[Ad] Endereço:Grupo de Inmunodeficiencias Primarias, Facultad de Medicina, Universidad de Antioquia, Medellín, Colombia.
[Ti] Título:Skewed Invariant Natural Killer T (iNKT) Cells, Impaired iNKT:B Cell Help and Decreased SAP Expression in Blood Lymphocytes from Patients with Common Variable Immunodeficiency.
[So] Source:Scand J Immunol;86(3):171-178, 2017 Sep.
[Is] ISSN:1365-3083
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Common variable immunodeficiency (CVID) is a syndrome with predominantly defective B cell function. However, abnormalities in the number and function of other lymphocyte subpopulations in peripheral blood (PB) have been described in most patients. We have analysed the distribution of iNKT cell subpopulations in the PB of CVID patients and the ability of these cells to provide in vitro cognate B cell help. The total of iNKT cells was reduced in the PB of CVID patients, especially CD4+, CD4-/CD8- and CCR5+/CXCR3+. These findings were associated with an enrichment of memory-like and a tendency towards a reduction in TNF-α-expressing effector iNKT cells in the peripheral blood mononuclear cells (PBMC) of CVID patients. Moreover, an accumulation of follicular helper iNKT cells in the PB of CVID patients was demonstrated. CVID αGalCer-pulsed iNKT cells are not able to induce autologous B cell proliferation although they do induce proliferation to healthy donor B cells. Interestingly, autologous and heterologous co-cultures did not differ in the amount of immunoglobulin secreted by B cells in vitro. Finally, reduced intracellular SAP expression in iNKT cells and other lymphocytes in the blood from CVID patients was observed. These results provide further insights into the immunological mechanisms underlying the iNKT cell defects and the potential targets to improve B cell help in CVID.
[Mh] Termos MeSH primário: Linfócitos B/imunologia
Comunicação Celular
Imunodeficiência de Variável Comum/imunologia
Células T Matadoras Naturais/imunologia
Saposinas/metabolismo
[Mh] Termos MeSH secundário: Adolescente
Adulto
Antígenos CD4/metabolismo
Antígenos CD8/metabolismo
Proliferação Celular
Células Cultivadas
Técnicas de Cocultura
Feminino
Galactosilceramidas/imunologia
Seres Humanos
Imunoglobulinas/metabolismo
Memória Imunológica
Ativação Linfocitária
Masculino
Meia-Idade
Receptores CCR5/metabolismo
Receptores CXCR3/metabolismo
Fator de Necrose Tumoral alfa/metabolismo
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CCR5 protein, human); 0 (CD4 Antigens); 0 (CD8 Antigens); 0 (CXCR3 protein, human); 0 (Galactosylceramides); 0 (Immunoglobulins); 0 (PSAP protein, human); 0 (Receptors, CCR5); 0 (Receptors, CXCR3); 0 (Saposins); 0 (Tumor Necrosis Factor-alpha)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171031
[St] Status:MEDLINE
[do] DOI:10.1111/sji.12576


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[PMID]:28776681
[Au] Autor:Van Damme P
[Ad] Endereço:Department of Neurosciences, Experimental Neurology and Leuven Institute for Neuroscience and Disease (LIND), KU Leuven - University of Leuven, Leuven, Belgium.
[Ti] Título:Another piece in the progranulin puzzle: special binding between progranulin and prosaposin creates additional lysosomal access: An Editorial Comment for 'The interaction between progranulin and prosaposin is mediated by granulins and the linker region between saposin B and C' on page 236.
[So] Source:J Neurochem;143(2):154-157, 2017 Oct.
[Is] ISSN:1471-4159
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Loss-of-function mutations in the gene encoding the growth factor progranulin cause degeneration of the ageing brain in a dose-dependent manner. While heterozygous mutations result in adult onset frontotemporal dementia, the much rarer homozygous null mutations cause an early onset lysosomal storage disorder. A better understanding of the biology of progranulin in the central nervous system is needed to find solutions for these incurable diseases. This Editorial highlights a study by Zhou et al. in the current issue of the Journal of Neurochemistry, in which the authors provide data that are a step towards this goal. Progranulin is mainly expressed by neurons and microglia and, although it is a secreted protein, it also ends up in lysosomes. Recently, the trafficking of progranulin and the molecular players involved have become better understood. A special interaction between progranulin and its travelling companion, prosaposin, explains how both proteins can use each other's transport receptors to gain access to lysosomes.
[Mh] Termos MeSH primário: Peptídeos e Proteínas de Sinalização Intercelular/metabolismo
Lisossomos/metabolismo
Saposinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Peptídeos e Proteínas de Sinalização Intercelular/genética
Lisossomos/genética
Ligação Proteica/fisiologia
Transporte Proteico/fisiologia
Saposinas/genética
[Pt] Tipo de publicação:EDITORIAL
[Nm] Nome de substância:
0 (GRN protein, human); 0 (Intercellular Signaling Peptides and Proteins); 0 (PSAP protein, human); 0 (Saposins); 134710-81-9 (granulin precursor protein)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170805
[St] Status:MEDLINE
[do] DOI:10.1111/jnc.14125


  3 / 623 MEDLINE  
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[PMID]:28640985
[Au] Autor:Zhou X; Sullivan PM; Sun L; Hu F
[Ad] Endereço:Department of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, New York, USA.
[Ti] Título:The interaction between progranulin and prosaposin is mediated by granulins and the linker region between saposin B and C.
[So] Source:J Neurochem;143(2):236-243, 2017 Oct.
[Is] ISSN:1471-4159
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The frontotemporal lobar degeneration (FTLD) protein progranulin (PGRN) is essential for proper lysosomal function. PGRN localizes in the lysosomal compartment within the cell. Prosaposin (PSAP), the precursor of lysosomal saposin activators (saposin A, B, C, D), physically interacts with PGRN. Previously, we have shown that PGRN and PSAP facilitate each other's lysosomal trafficking. Here, we report that the interaction between PSAP and PGRN requires the linker region of saposin B and C (BC linker). PSAP protein with the BC linker mutated, fails to interact with PGRN and deliver PGRN to lysosomes in the biosynthetic and endocytic pathways. On the other hand, PGRN interacts with PSAP through multiple granulin motifs. Granulin D and E bind to PSAP with similar affinity as full-length PGRN. Read the Editorial Comment for this article on page 154.
[Mh] Termos MeSH primário: Peptídeos e Proteínas de Sinalização Intercelular/genética
Peptídeos e Proteínas de Sinalização Intercelular/metabolismo
Precursores de Proteínas/genética
Precursores de Proteínas/metabolismo
Saposinas/genética
Saposinas/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Animais Recém-Nascidos
Células COS
Cercopithecus aethiops
Células HEK293
Seres Humanos
Camundongos
Camundongos Knockout
Ligação Proteica/fisiologia
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GRN protein, human); 0 (Intercellular Signaling Peptides and Proteins); 0 (PSAP protein, human); 0 (Protein Precursors); 0 (Saposins); 134710-81-9 (granulin precursor protein)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170623
[St] Status:MEDLINE
[do] DOI:10.1111/jnc.14110


  4 / 623 MEDLINE  
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[PMID]:28212860
[Au] Autor:Bryksa BC; Grahame DA; Yada RY
[Ad] Endereço:Department of Food Science, Ontario Agricultural College, University of Guelph, Guelph, ON N1G 2W1, Canada.
[Ti] Título:Comparative structure-function characterization of the saposin-like domains from potato, barley, cardoon and Arabidopsis aspartic proteases.
[So] Source:Biochim Biophys Acta;1859(5):1008-1018, 2017 05.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The present study characterized the aspartic protease saposin-like domains of four plant species, Solanum tuberosum (potato), Hordeum vulgare L. (barley), Cynara cardunculus L. (cardoon; artichoke thistle) and Arabidopsis thaliana, in terms of bilayer disruption and fusion, and structure pH-dependence. Comparison of the recombinant saposin-like domains revealed that each induced leakage of bilayer vesicles composed of a simple phospholipid mixture with relative rates Arabidopsis>barley>cardoon>potato. When compared for leakage of bilayer composed of a vacuole-like phospholipid mixture, leakage was approximately five times higher for potato saposin-like domain compared to the others. In terms of fusogenic activity, distinctions between particle size profiles were noted among the four proteins, particularly for potato saposin-like domain. Bilayer fusion assays in reducing conditions resulted in altered fusion profiles except in the case of cardoon saposin-like domain which was virtually unchanged. Secondary structure profiles were similar across all four proteins under different pH conditions, although cardoon saposin-like domain appeared to have higher overall helix structure. Furthermore, increases in Trp emission upon protein-bilayer interactions suggested that protein structure rearrangements equilibrated with half-times ranging from 52 to 120s, with cardoon saposin-like domain significantly slower than the other three species. Overall, the present findings serve as a foundation for future studies seeking to delineate protein structural features and motifs in protein-bilayer interactions based upon variability in plant aspartic protease saposin-like domain structures.
[Mh] Termos MeSH primário: Arabidopsis/enzimologia
Ácido Aspártico Proteases/química
Cynara/enzimologia
Hordeum/enzimologia
Domínios Proteicos
Saposinas/química
Solanum tuberosum/enzimologia
[Mh] Termos MeSH secundário: Ácido Aspártico Proteases/fisiologia
Concentração de Íons de Hidrogênio
Bicamadas Lipídicas/química
Estrutura Secundária de Proteína
Saposinas/fisiologia
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Lipid Bilayers); 0 (Saposins); EC 3.4.- (Aspartic Acid Proteases)
[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:170219
[St] Status:MEDLINE


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[PMID]:28126847
[Au] Autor:Abdul-Hammed M; Breiden B; Schwarzmann G; Sandhoff K
[Ad] Endereço:Life and Medical Sciences (LIMES) Institut, Membrane Biology and Lipid Biochemistry Unit, Kekulé-Institut für Organische Chemie und Biochemie, Universität Bonn, Bonn, Germany.
[Ti] Título:Lipids regulate the hydrolysis of membrane bound glucosylceramide by lysosomal ß-glucocerebrosidase.
[So] Source:J Lipid Res;58(3):563-577, 2017 Mar.
[Is] ISSN:1539-7262
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Glucosylceramide (GlcCer) is the primary storage lipid in the lysosomes of Gaucher patients and a secondary one in Niemann-Pick disease types A, B, and C. The regulatory roles of lipids on the hydrolysis of membrane bound GlcCer by lysosomal ß-glucocerebrosidase (GBA1) was probed using a detergent-free liposomal assay. The degradation rarely occurs at uncharged liposomal surfaces in the absence of saposin (Sap) C. However, anionic lipids stimulate GlcCer hydrolysis at low pH by up to 1,000-fold depending on the nature and position of the negative charges in their head groups while cationic lipids inhibit the degradation, thus showing the importance of electrostatic interactions between the polycationic GBA1 and the negatively charged vesicle surfaces at low pH. Ceramide, fatty acids, monoacylglycerol, and diacylglycerol also stimulate GlcCer hydrolysis while SM, sphingosine, and sphinganine play strong inhibitory roles, thereby explaining the secondary storage of GlcCer in Niemann-Pick diseases. Surprisingly, cholesterol stimulates GlcCer degradation in the presence of bis(monoacylglycero)phosphate (BMP). Sap C strongly stimulates GlcCer hydrolysis even in the absence of BMP and the regulatory roles of the intraendolysosomal lipids on its activity is discussed. Our data suggest that these strong modifiers of GlcCer hydrolysis affect the genotype-phenotype correlation in several cases of Gaucher patients independent of the types.
[Mh] Termos MeSH primário: Doença de Gaucher/metabolismo
Glucosilceramidase/genética
Glucosilceramidas/metabolismo
Doenças de Niemann-Pick/metabolismo
[Mh] Termos MeSH secundário: Colesterol/metabolismo
Doença de Gaucher/genética
Doença de Gaucher/patologia
Estudos de Associação Genética
Glucosilceramidase/metabolismo
Seres Humanos
Hidrólise
Metabolismo dos Lipídeos/genética
Lisofosfolipídeos/metabolismo
Lisossomos/enzimologia
Monoglicerídeos/metabolismo
Doenças de Niemann-Pick/genética
Doenças de Niemann-Pick/patologia
Saposinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glucosylceramides); 0 (Lysophospholipids); 0 (Monoglycerides); 0 (Saposins); 0 (bis(monoacylglyceryl)phosphate); 97C5T2UQ7J (Cholesterol); EC 3.2.1.45 (Glucosylceramidase)
[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:170128
[St] Status:MEDLINE
[do] DOI:10.1194/jlr.M073510


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[PMID]:26965692
[Au] Autor:Vilageliu L; Grinberg D
[Ad] Endereço:Department of Genetics, Faculty of Biology, Universitat de Barcelona, IBUB, CIBERER, Barcelona, Spain.
[Ti] Título:Involvement of Gaucher Disease Mutations in Parkinson Disease.
[So] Source:Curr Protein Pept Sci;18(7):758-764, 2017.
[Is] ISSN:1875-5550
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Gaucher disease is an autosomal recessive lysosomal storage disorder, caused by mutations in the GBA gene. The frequency of Gaucher disease patients and heterozygote carriers that developed Parkinson disease has been found to be above that of the control population. This fact suggests that mutations in the GBA gene can be involved in Parkison's etiology. Analysis of large cohorts of patients with Parkinson disease has shown that there are significantly more cases bearing GBA mutations than those found among healthy individuals. Functional studies have proven an interaction between α-synuclein and GBA, the levels of which presented an inverse correlation. Mutant GBA proteins cause increases in α-synuclein levels, while an inhibition of GBA by α-synuclein has been also demonstrated. Saposin C, a coactivator of GBA, has been shown to protect GBA from this inhibition. Among the GBA variants associated with Parkinson disease, E326K seems to be one of the most prevalent. Interestingly, it is involved in Gaucher disease only when it forms part of a double-mutant allele, usually with the L444P mutation. Structural analyses have revealed that both residues (E326 and L444) interact with Saposin C and, probably, also with α-synuclein. This could explain the antagonistic role of these two proteins in relation to GBA.
[Mh] Termos MeSH primário: Doença de Gaucher/genética
Glucosilceramidase/genética
Mutação
Doença de Parkinson/genética
alfa-Sinucleína/genética
[Mh] Termos MeSH secundário: Alelos
Doença de Gaucher/complicações
Doença de Gaucher/metabolismo
Doença de Gaucher/patologia
Expressão Gênica
Frequência do Gene
Glucosilceramidase/metabolismo
Seres Humanos
Lisossomos/efeitos dos fármacos
Lisossomos/metabolismo
Lisossomos/patologia
Doença de Parkinson/complicações
Doença de Parkinson/metabolismo
Doença de Parkinson/patologia
Saposinas/farmacologia
alfa-Sinucleína/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Saposins); 0 (alpha-Synuclein); EC 3.2.1.45 (Glucosylceramidase)
[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:160312
[St] Status:MEDLINE
[do] DOI:10.2174/1389203717666160311115956


  7 / 623 MEDLINE  
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[PMID]:27349982
[Au] Autor:Xiong ZJ; Huang J; Poda G; Pomès R; Privé GG
[Ad] Endereço:Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada.
[Ti] Título:Structure of Human Acid Sphingomyelinase Reveals the Role of the Saposin Domain in Activating Substrate Hydrolysis.
[So] Source:J Mol Biol;428(15):3026-42, 2016 Jul 31.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Acid sphingomyelinase (ASM) is a lysosomal phosphodiesterase that catalyzes the hydrolysis of sphingomyelin to produce ceramide and phosphocholine. While other lysosomal sphingolipid hydrolases require a saposin activator protein for full activity, the ASM polypeptide incorporates a built-in N-terminal saposin domain and does not require an external activator protein. Here, we report the crystal structure of human ASM and describe the organization of the three main regions of the enzyme: the N-terminal saposin domain, the proline-rich connector, and the catalytic domain. The saposin domain is tightly associated along an edge of the large, bowl-shaped catalytic domain and adopts an open form that exposes a hydrophobic concave surface approximately 30Å from the catalytic center. The calculated electrostatic potential of the enzyme is electropositive at the acidic pH of the lysosome, consistent with the strict requirement for the presence of acidic lipids in target membranes. Docking studies indicate that sphingomyelin binds with the ceramide-phosphate group positioned at the binuclear zinc center and molecular dynamic simulations indicate that the intrinsic flexibility of the saposin domain is important for monomer-dimer exchange and for membrane interactions. Overall, ASM uses a combination of electrostatic and hydrophobic interactions to cause local disruptions of target bilayers in order to bring the lipid headgroup to the catalytic center in a membrane-bound reaction.
[Mh] Termos MeSH primário: Saposinas/metabolismo
Esfingomielina Fosfodiesterase/metabolismo
[Mh] Termos MeSH secundário: Domínio Catalítico/fisiologia
Seres Humanos
Hidrólise
Lipídeos/fisiologia
Lisossomos/metabolismo
Membranas/metabolismo
Prolina/metabolismo
Eletricidade Estática
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lipids); 0 (Saposins); 9DLQ4CIU6V (Proline); EC 3.1.4.12 (Sphingomyelin Phosphodiesterase)
[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:160629
[St] Status:MEDLINE


  8 / 623 MEDLINE  
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[PMID]:27305744
[Au] Autor:Becze E
[Ti] Título:Proteins Targeting Tumor Microenvironment May Block Metastatic Cancer Growth.
[So] Source:ONS Connect;31(5):40, 2016 May.
[Is] ISSN:1935-1623
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Proliferação Celular/efeitos dos fármacos
Drogas em Investigação/uso terapêutico
Neoplasias/tratamento farmacológico
Neoplasias/fisiopatologia
Saposinas/farmacologia
Microambiente Tumoral/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Modelos Animais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drugs, Investigational); 0 (Saposins)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:160616
[Lr] Data última revisão:
160616
[Sb] Subgrupo de revista:N
[Da] Data de entrada para processamento:160617
[St] Status:MEDLINE


  9 / 623 MEDLINE  
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[PMID]:27190177
[Au] Autor:Liu S; Zhou X; Piao X; Hou N; Shen Y; Zou Y; Li S; Cao J; Chen Q
[Ad] Endereço:MOH Key Laboratory of Systems Biology of Pathogens, Institute of Pathogen Biology, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing.
[Ti] Título:Saposin-like Proteins, a Multigene Family of Schistosoma Species, are Biomarkers for the Immunodiagnosis of Schistosomiasis Japonica.
[So] Source:J Infect Dis;214(8):1225-34, 2016 Oct 15.
[Is] ISSN:1537-6613
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: One major obstacle to schistosomiasis prevention and control is the lack of accurate and sensitive diagnostic approaches, which are essential for planning, targeting, and evaluating disease control efforts. METHODS: Based on bioinformatics analysis, we identified a multigene family of saposin-like protein (SAPLP) in the schistosome genomes. Schistosoma japonicum SAPLPs (SjSAPLPs), including recently reported promising biomarker SjSP-13, were systematically and comparatively assessed as immunodiagnostic antigens for schistosomiasis japonica. RESULTS: Two novel antigens (SjSAPLP4 and SjSAPLP5) could specifically react to serum samples from both S. japonicum-infected laboratory animals and patients. The sensitivities of SjSAPLP4, SjSAPLP5, and SjSP-13 for immunodiagnosis were 98% (95% confidence interval, 88.0%-99.9%), 96% (85.1%-99.3%), and 88% (75.0%-95.0%), respectively, and 100% (91.1%-100%) specificity was observed for the 3 antigens with enzyme-linked immunosorbent assay; there was no cross-reaction with clonorchiosis (0 of 19 patients), echinococcosis (0 of 20 patients), or trichinellosis (0 of 18 patients) for the 3 antigens. Antibodies to the 3 antigens could be detected in the serum samples of rabbits infected with 1000 cercariae as early as 3-4 weeks after infection. CONCLUSIONS: These results suggest that SjSAPLP4 and SjSAPLP5 could serve as novel biomarkers for the immunodiagnosis of schistosomiasis japonica, which will further improve diagnostic sensitivity and specificity.
[Mh] Termos MeSH primário: Biomarcadores/sangue
Família Multigênica/genética
Saposinas/sangue
Saposinas/imunologia
Esquistossomose Japônica/diagnóstico
Esquistossomose Japônica/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Anti-Helmínticos/imunologia
Antígenos de Helmintos/imunologia
Feminino
Seres Humanos
Testes Imunológicos/métodos
Masculino
Camundongos
Camundongos Endogâmicos BALB C
Família Multigênica/imunologia
Coelhos
Schistosoma japonicum/genética
Esquistossomose Japônica/sangue
Esquistossomose Japônica/parasitologia
Sensibilidade e Especificidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Helminth); 0 (Antigens, Helminth); 0 (Biomarkers); 0 (Saposins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170601
[Lr] Data última revisão:
170601
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:160519
[St] Status:MEDLINE
[do] DOI:10.1093/infdis/jiw188


  10 / 623 MEDLINE  
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[PMID]:27160923
[Au] Autor:Davis HW; Hussain N; Qi X
[Ad] Endereço:Division of Hematology/Oncology, Translational Medicine Laboratory, Department of Internal Medicine, University of Cincinnati College of Medicine, and Brain Tumor Center at UC Neuroscience Institute, 3512 Eden Avenue, Cincinnati, OH, 45267-0508, USA.
[Ti] Título:Detection of cancer cells using SapC-DOPS nanovesicles.
[So] Source:Mol Cancer;15(1):33, 2016 May 10.
[Is] ISSN:1476-4598
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Unlike normal cells, cancer cells express high levels of phosphatidylserine on the extracellular leaflet of their cell membrane. Exploiting this characteristic, our lab developed a therapeutic agent that consists of the fusogenic protein, saposin C (SapC) which is embedded in dioleoylphosphatidylserine (DOPS) vesicles. These nanovesicles selectively target cancer cells and induce apoptosis. Here we review the data supporting use of SapC-DOPS to locate tumors for surgical resection or for treatment. In addition, there is important evidence suggesting that SapC-DOPS may also prove to be an effective novel cancer therapeutic reagent. Given that SapC-DOPS is easily labeled with lipophilic dyes, it has been combined with the far-red fluorescent dye, CellVue Maroon (CVM), for tumor targeting studies. We also have used contrast agents incorporated in the SapC-DOPS nanovesicles for computed tomography and magnetic resonance imaging, and review that data here. Administered intravenously, the fluorescently labeled SapC-DOPS traversed the blood-brain tumor barrier enabling identification of brain tumors. SapC-DOPS-CVM also detected a variety of other mouse tumors in vivo, rendering them observable by optical imaging using IVIS and multi-angle rotational optical imaging. Dye is detected within 30 min and remains within tumor for at least 7 days, whereas non-tumor tissues were unstained (some dye observed in the liver was transient, likely representing degradation products). Additionally, labeled SapC-DOPS ex vivo delineated tumors in human histological specimens. SapC-DOPS can also be labeled with contrast reagents for computed tomography or magnetic resonance imaging. In conclusion, labeled SapC-DOPS provides a convenient, specific, and nontoxic method for detecting tumors while concurrently offering a therapeutic benefit.
[Mh] Termos MeSH primário: Nanopartículas
Neoplasias/diagnóstico
Neoplasias/metabolismo
Fosfatidilserinas/metabolismo
Saposinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Membrana Celular/metabolismo
Meios de Contraste
Corantes Fluorescentes
Seres Humanos
Modelos Animais
Imagem Molecular/métodos
Imagem Multimodal/métodos
Neoplasias/terapia
Fosfatidilserinas/química
Ligação Proteica
Saposinas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Contrast Media); 0 (Fluorescent Dyes); 0 (Phosphatidylserines); 0 (Saposins); 70614-14-1 (1,2-dioleoylphosphatidylserine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170629
[Lr] Data última revisão:
170629
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160511
[St] Status:MEDLINE
[do] DOI:10.1186/s12943-016-0519-1



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