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Pesquisa : D12.776.220.980 [Categoria DeCS]
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[PMID]:29244882
[Au] Autor:Meissner JM; Sikorski AF; Nawara T; Grzesiak J; Marycz K; Boguslawska DM; Michalczyk I; Lecomte MC; Machnicka B
[Ad] Endereço:Laboratory of Cytobiochemistry, Biotechnology Faculty, University of Wroclaw, Wroclaw, Poland.
[Ti] Título:αII-spectrin in T cells is involved in the regulation of cell-cell contact leading to immunological synapse formation?
[So] Source:PLoS One;12(12):e0189545, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:T-lymphocyte activation after antigen presentation to the T-Cell Receptor (TCR) is a critical step in the development of proper immune responses to infection and inflammation. This dynamic process involves reorganization of the actin cytoskeleton and signaling molecules at the cell membrane, leading to the formation of the Immunological Synapse (IS). The mechanisms regulating the formation of the IS are not completely understood. Nonerythroid spectrin is a membrane skeletal protein involved in the regulation of many cellular processes, including cell adhesion, signaling and actin cytoskeleton remodeling. However, the role of spectrin in IS formation has not been explored. We used molecular, imaging and cellular approaches to show that nonerythroid αII-spectrin redistributes to the IS during T-cell activation. The redistribution of spectrin coincides with the relocation of CD45 and LFA-1, two components essential for IS formation and stability. We assessed the role of spectrin by shRNA-mediated depletion from Jurkat T cells and show that spectrin-depleted cells exhibit decreased adhesion and are defective in forming lamellipodia and filopodia. Importantly, IS formation is impaired in spectrin-depleted cells. Thus, spectrin may be engaged in regulation of distinct events necessary for the establishment and maturity of the IS: besides the involvement of spectrin in the control of CD45 and LFA-1 surface display, spectrin acts in the establishment of cell-cell contact and adhesion processes during the formation of the IS.
[Mh] Termos MeSH primário: Sinapses Imunológicas/fisiologia
Espectrina/fisiologia
[Mh] Termos MeSH secundário: Adesão Celular
Seres Humanos
Células Jurkat
Transporte Proteico
Pseudópodes/metabolismo
Pseudópodes/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
12634-43-4 (Spectrin)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180105
[Lr] Data última revisão:
180105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171216
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189545


  2 / 3247 MEDLINE  
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[PMID]:28991926
[Au] Autor:Fai TG; Leo-Macias A; Stokes DL; Peskin CS
[Ad] Endereço:John A. Paulson School of Engineering and Applied Sciences, Harvard University, Cambridge, Massachusetts, United States of America.
[Ti] Título:Image-based model of the spectrin cytoskeleton for red blood cell simulation.
[So] Source:PLoS Comput Biol;13(10):e1005790, 2017 Oct.
[Is] ISSN:1553-7358
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We simulate deformable red blood cells in the microcirculation using the immersed boundary method with a cytoskeletal model that incorporates structural details revealed by tomographic images. The elasticity of red blood cells is known to be supplied by both their lipid bilayer membranes, which resist bending and local changes in area, and their cytoskeletons, which resist in-plane shear. The cytoskeleton consists of spectrin tetramers that are tethered to the lipid bilayer by ankyrin and by actin-based junctional complexes. We model the cytoskeleton as a random geometric graph, with nodes corresponding to junctional complexes and with edges corresponding to spectrin tetramers such that the edge lengths are given by the end-to-end distances between nodes. The statistical properties of this graph are based on distributions gathered from three-dimensional tomographic images of the cytoskeleton by a segmentation algorithm. We show that the elastic response of our model cytoskeleton, in which the spectrin polymers are treated as entropic springs, is in good agreement with the experimentally measured shear modulus. By simulating red blood cells in flow with the immersed boundary method, we compare this discrete cytoskeletal model to an existing continuum model and predict the extent to which dynamic spectrin network connectivity can protect against failure in the case of a red cell subjected to an applied strain. The methods presented here could form the basis of disease- and patient-specific computational studies of hereditary diseases affecting the red cell cytoskeleton.
[Mh] Termos MeSH primário: Citoesqueleto/química
Eritrócitos/citologia
Processamento de Imagem Assistida por Computador/métodos
Modelos Biológicos
Espectrina/química
[Mh] Termos MeSH secundário: Algoritmos
Elasticidade
Deformação Eritrocítica
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
12634-43-4 (Spectrin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171110
[Lr] Data última revisão:
171110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171010
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pcbi.1005790


  3 / 3247 MEDLINE  
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[PMID]:28957326
[Au] Autor:Ebel ER; Telis N; Venkataram S; Petrov DA; Enard D
[Ad] Endereço:Department of Biology, Stanford University, Stanford, California, United States of America.
[Ti] Título:High rate of adaptation of mammalian proteins that interact with Plasmodium and related parasites.
[So] Source:PLoS Genet;13(9):e1007023, 2017 Sep.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Plasmodium parasites, along with their Piroplasm relatives, have caused malaria-like illnesses in terrestrial mammals for millions of years. Several Plasmodium-protective alleles have recently evolved in human populations, but little is known about host adaptation to blood parasites over deeper evolutionary timescales. In this work, we analyze mammalian adaptation in ~500 Plasmodium- or Piroplasm- interacting proteins (PPIPs) manually curated from the scientific literature. We show that (i) PPIPs are enriched for both immune functions and pleiotropy with other pathogens, and (ii) the rate of adaptation across mammals is significantly elevated in PPIPs, compared to carefully matched control proteins. PPIPs with high pathogen pleiotropy show the strongest signatures of adaptation, but this pattern is fully explained by their immune enrichment. Several pieces of evidence suggest that blood parasites specifically have imposed selection on PPIPs. First, even non-immune PPIPs that lack interactions with other pathogens have adapted at twice the rate of matched controls. Second, PPIP adaptation is linked to high expression in the liver, a critical organ in the parasite life cycle. Finally, our detailed investigation of alpha-spectrin, a major red blood cell membrane protein, shows that domains with particularly high rates of adaptation are those known to interact specifically with P. falciparum. Overall, we show that host proteins that interact with Plasmodium and Piroplasm parasites have experienced elevated rates of adaptation across mammals, and provide evidence that some of this adaptation has likely been driven by blood parasites.
[Mh] Termos MeSH primário: Adaptação Fisiológica/genética
Apicomplexa/patogenicidade
Interações Hospedeiro-Parasita/genética
Mamíferos/parasitologia
Plasmodium falciparum/patogenicidade
Espectrina/genética
[Mh] Termos MeSH secundário: Animais
Artiodáctilos/parasitologia
Evolução Molecular
Regulação da Expressão Gênica
Seres Humanos
Primatas/parasitologia
Roedores/parasitologia
Alinhamento de Sequência
Espectrina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
12634-43-4 (Spectrin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170929
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007023


  4 / 3247 MEDLINE  
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[PMID]:28902407
[Au] Autor:Qu Z; Wang Y; Li X; Wu L; Wang Y
[Ad] Endereço:Laboratory of Neural Signal Transduction, Institute of Neuroscience, Chinese Academy of Sciences, Shanghai, China.
[Ti] Título:TRPC6 expression in neurons is differentially regulated by NR2A- and NR2B-containing NMDA receptors.
[So] Source:J Neurochem;143(3):282-293, 2017 Nov.
[Is] ISSN:1471-4159
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The expression of transient receptor potential canonical 6 (TRPC6) in central nervous system (CNS) is important for neuronal functions and certain neural disorders. However, the regulatory mechanism of TRPC6 expression in neurons is still obscure. In this study, we show that TRPC6 expression in the primary cultured cortical neurons is bidirectionally regulated by glutamate. Activation of NR2A-containing NMDARs induces TRPC6 transcription through a calcineurin-dependent pathway. In contrast, activation of NR2B-containing NMDARs causes TRPC6 degradation through calpain. Thus, TRPC6 expression in neurons is regulated by glutamate in a bidirectional manner that is dependent on NR2A and NR2B.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica/genética
Neurônios/metabolismo
Receptores de N-Metil-D-Aspartato/metabolismo
Canais de Cátion TRPC/metabolismo
[Mh] Termos MeSH secundário: Animais
Animais Recém-Nascidos
Astrócitos/efeitos dos fármacos
Astrócitos/metabolismo
Células Cultivadas
Córtex Cerebral/citologia
Ciclosporina/farmacologia
Dipeptídeos/farmacologia
Embrião de Mamíferos
Inibidores Enzimáticos/farmacologia
Fármacos atuantes sobre Aminoácidos Excitatórios/farmacologia
Regulação da Expressão Gênica/efeitos dos fármacos
Neurônios/efeitos dos fármacos
RNA Interferente Pequeno/genética
RNA Interferente Pequeno/metabolismo
Ratos
Ratos Sprague-Dawley
Receptores de N-Metil-D-Aspartato/genética
Espectrina/genética
Espectrina/metabolismo
Canais de Cátion TRPC/genética
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dipeptides); 0 (Enzyme Inhibitors); 0 (Excitatory Amino Acid Agents); 0 (NR2A NMDA receptor); 0 (NR2B NMDA receptor); 0 (RNA, Small Interfering); 0 (Receptors, N-Methyl-D-Aspartate); 0 (TRPC Cation Channels); 0 (Trpc6 protein, rat); 12634-43-4 (Spectrin); 18X9FR245W (calpeptin); 83HN0GTJ6D (Cyclosporine)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170914
[St] Status:MEDLINE
[do] DOI:10.1111/jnc.14215


  5 / 3247 MEDLINE  
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[PMID]:28855121
[Au] Autor:Nigra AD; Santander VS; Dircio-Maldonado R; Amaiden MR; Monesterolo NE; Flores-Guzmán P; Muhlberger T; Rivelli JF; Campetelli AN; Mayani H; Casale CH
[Ad] Endereço:Departamento de Biología Molecular, Facultad de Ciencias Exactas Físico-Químicas y Naturales, Universidad Nacional de Río Cuarto, Río Cuarto, Córdoba 5800, Argentina.
[Ti] Título:Tubulin is retained throughout the human hematopoietic/erythroid cell differentiation process and plays a structural role in sedimentable fraction of mature erythrocytes.
[So] Source:Int J Biochem Cell Biol;91(Pt A):29-36, 2017 Oct.
[Is] ISSN:1878-5875
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:We investigated the properties of tubulin present in the sedimentable fraction ("Sed-tub") of human erythrocytes, and tracked the location and organization of tubulin in various types of cells during the process of hematopoietic/erythroid differentiation. Sed-tub was sensitive to taxol/nocodazole (drugs that modify microtubule assembly/disassembly), but was organized as part of a protein network rather than in typical microtubule form. This network had a non-uniform "connected-ring" structure, with tubulin localized in the connection areas and associated with other proteins. When tubulin was eliminated from Sed-tub fraction, this connected-ring structure disappeared. Spectrin, a major protein component in Sed-tub fraction, formed a complex with tubulin. During hematopoietic differentiation, tubulin shifts from typical microtubule structure (in pro-erythroblasts) to a disorganized structure (in later stages), and is retained in reticulocytes following enucleation. Thus, tubulin is not completely lost when erythrocytes mature; it continues to play a structural role in the Sed-tub fraction.
[Mh] Termos MeSH primário: Eritrócitos/citologia
Eritrócitos/metabolismo
Hematopoese
Tubulina (Proteína)/metabolismo
[Mh] Termos MeSH secundário: Adulto
Sedimentação Sanguínea/efeitos dos fármacos
Eritrócitos/efeitos dos fármacos
Feminino
Hematopoese/efeitos dos fármacos
Seres Humanos
Masculino
Nocodazol/farmacologia
Paclitaxel/farmacologia
Espectrina/metabolismo
Tubulina (Proteína)/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Tubulin); 12634-43-4 (Spectrin); P88XT4IS4D (Paclitaxel); SH1WY3R615 (Nocodazole)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170901
[St] Status:MEDLINE


  6 / 3247 MEDLINE  
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[PMID]:28806784
[Au] Autor:Cutts EE; Laasch N; Reiter DM; Trenker R; Slater LM; Stansfeld PJ; Vakonakis I
[Ad] Endereço:Department of Biochemistry, University of Oxford, Oxford, United Kingdom.
[Ti] Título:Structural analysis of P. falciparum KAHRP and PfEMP1 complexes with host erythrocyte spectrin suggests a model for cytoadherent knob protrusions.
[So] Source:PLoS Pathog;13(8):e1006552, 2017 Aug.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Plasmodium falciparum Erythrocyte Membrane Protein 1 (PfEMP1) and Knob-associated Histidine-rich Protein (KAHRP) are directly linked to malaria pathology. PfEMP1 and KAHRP cluster on protrusions (knobs) on the P. falciparum-infected erythrocyte surface and enable pathogenic cytoadherence of infected erythrocytes to the host microvasculature, leading to restricted blood flow, oxygen deprivation and damage of tissues. Here we characterize the interactions of PfEMP1 and KAHRP with host erythrocyte spectrin using biophysical, structural and computational approaches. These interactions assist knob formation and, thus, promote cytoadherence. We show that the folded core of the PfEMP1 cytosolic domain interacts broadly with erythrocyte spectrin but shows weak, residue-specific preference for domain 17 of α spectrin, which is proximal to the erythrocyte cytoskeletal junction. In contrast, a protein sequence repeat region in KAHRP preferentially associates with domains 10-14 of ß spectrin, proximal to the spectrin-ankyrin complex. Structural models of PfEMP1 and KAHRP with spectrin combined with previous microscopy and protein interaction data suggest a model for knob architecture.
[Mh] Termos MeSH primário: Eritrócitos/parasitologia
Interações Hospedeiro-Parasita/fisiologia
Malária Falciparum/metabolismo
Peptídeos/metabolismo
Proteínas de Protozoários/metabolismo
Espectrina/metabolismo
[Mh] Termos MeSH secundário: Cristalografia por Raios X
Seres Humanos
Simulação de Acoplamento Molecular
Ressonância Magnética Nuclear Biomolecular
Peptídeos/química
Plasmodium falciparum
Proteínas de Protozoários/química
Espectrina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptides); 0 (Protozoan Proteins); 0 (erythrocyte membrane protein 1, Plasmodium falciparum); 0 (knob protein, Plasmodium falciparum); 12634-43-4 (Spectrin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170815
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006552


  7 / 3247 MEDLINE  
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[PMID]:28759231
[Au] Autor:Kling A; Jantos K; Mack H; Hornberger W; Drescher K; Nimmrich V; Relo A; Wicke K; Hutchins CW; Lao Y; Marsh K; Moeller A
[Ad] Endereço:Neuroscience Research, AbbVie Deutschland GmbH & Co. KG , Knollstrasse, 67061 Ludwigshafen, Germany.
[Ti] Título:Discovery of Novel and Highly Selective Inhibitors of Calpain for the Treatment of Alzheimer's Disease: 2-(3-Phenyl-1H-pyrazol-1-yl)-nicotinamides.
[So] Source:J Med Chem;60(16):7123-7138, 2017 Aug 24.
[Is] ISSN:1520-4804
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Calpain overactivation has been implicated in a variety of pathological disorders including ischemia/reperfusion injury, cataract formation, and neurodegenerative diseases such as Alzheimer's disease (AD). Herein we describe our efforts leading to the identification of ketoamide-based 2-(3-phenyl-1H-pyrazol-1-yl)nicotinamides as potent and reversible inhibitors of calpain with high selectivity versus related cysteine protease cathepsins, other proteases, and receptors. Broad efficacy in a set of preclinical models relevant to AD suggests that inhibition of calpain represents an attractive approach with potential benefit for the treatment of AD.
[Mh] Termos MeSH primário: Doença de Alzheimer/tratamento farmacológico
Aminobutiratos/farmacologia
Calpaína/antagonistas & inibidores
Inibidores de Cisteína Proteinase/farmacologia
Niacinamida/análogos & derivados
Niacinamida/farmacologia
Pirazóis/farmacologia
[Mh] Termos MeSH secundário: Aminobutiratos/síntese química
Aminobutiratos/farmacocinética
Animais
Catepsinas
Inibidores de Cisteína Proteinase/síntese química
Inibidores de Cisteína Proteinase/farmacocinética
Cães
Hipocampo/metabolismo
Seres Humanos
Concentração Inibidora 50
Macaca fascicularis
Masculino
Microssomos Hepáticos/metabolismo
Niacinamida/síntese química
Niacinamida/farmacocinética
Pirazóis/síntese química
Pirazóis/farmacocinética
Ratos Endogâmicos F344
Ratos Sprague-Dawley
Ratos Wistar
Sono REM/efeitos dos fármacos
Espectrina/metabolismo
Estereoisomerismo
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (A-933548); 0 (Aminobutyrates); 0 (Cysteine Proteinase Inhibitors); 0 (Pyrazoles); 12634-43-4 (Spectrin); 25X51I8RD4 (Niacinamide); EC 3.4.- (Cathepsins); EC 3.4.22.- (Calpain); EC 3.4.22.52 (CAPN1 protein, human)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170801
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jmedchem.7b00731


  8 / 3247 MEDLINE  
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[PMID]:28694211
[Au] Autor:He Y; Jia S; Dewan RK; Liao N
[Ad] Endereço:Department of Pediatrics, The First Affiliated Hospital of Guangxi Medical University, N0.6, Shuangyong Road, Qingxiu District, Nanning, Guangxi Province 530021, PR China.
[Ti] Título:Novel mutations in patients with hereditary red blood cell membrane disorders using next-generation sequencing.
[So] Source:Gene;627:556-562, 2017 Sep 05.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:To diagnose and investigate the genotype-phenotype relationship in intractable hereditary red blood cell (RBC) membrane cases, we have utilized next-generation sequencing (NGS) to develop a high-throughput, highly sensitive assay. Three unrelated families including 15 individuals were analysed with a panel interrogating 600 genes related to haematopathy disorders. Where possible, inheritance patterns of pathogenic mutations were determined by sequencing the relatives. We identified 2 novel mutations in ANK1 (Y216X and E142X) responsible for hereditary spherocytosis (HS) that were stop-gain single nucleotide variants (SNVs). Furthermore, a novel SPTA1 mutation (H54P) was identified; it is a nonsynonymous SNV and is associated with hereditary elliptocytosis (HE). In addition, patients who also carried erythropoiesis gene mutations showed more severe disease phenotype. The NGS panel provides a fast and accurate method for molecular diagnosis in patients with intractable hereditary RBC membrane disorders. An approach integrating medical history, clinical and molecular testing, and pedigree analysis is beneficial for these patients and families.
[Mh] Termos MeSH primário: Anquirinas/genética
Eliptocitose Hereditária/genética
Mutação de Sentido Incorreto
Espectrina/genética
Esferocitose Hereditária/genética
[Mh] Termos MeSH secundário: Adulto
Criança
Eritropoese
Feminino
Seres Humanos
Lactente
Masculino
Linhagem
Fenótipo
Polimorfismo de Nucleotídeo Único
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ANK1 protein, human); 0 (Ankyrins); 12634-43-4 (Spectrin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170712
[St] Status:MEDLINE


  9 / 3247 MEDLINE  
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[PMID]:28668965
[Au] Autor:Ciana A; Achilli C; Gaur A; Minetti G
[Ti] Título:Membrane Remodelling and Vesicle Formation During Ageing of Human Red Blood Cells.
[So] Source:Cell Physiol Biochem;42(3):1127-1138, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: A high surface-to-volume ratio and a spectrin membrane-skeleton (MS) confer to the mammalian red blood cells (RBCs) their characteristic deformability, mechanical strength and structural stability. During their 120 days of circulatory life in humans, RBCs decrease in size, while remaining biconcave disks, owing to a coordinated decrease in membrane surface area and cell water. It is generally believed that part of the membrane is lost with the shedding of spectrin-free vesicles of the same type that can be obtained in vitro by different treatments. If this were true, an excess of MS would arise in old RBCs, with respect to the lipid bilayer. Aim of this paper was to investigate this aspect. METHODS: Quantification of spectrin by electrophoretic methods was carried out in RBCs of different age. RESULTS: Spectrin decreases, on a per cell basis, with RBC ageing. On the other hand, the membrane raft protein marker flotillin-2, while decreasing in the membrane of old cells, was found to be strongly depleted in the membrane of in vitro-induced vesicles. CONCLUSION: Part of the membrane-skeleton is probably lost together with part of the lipid bilayer in a balanced way. These findings point to a mechanism for the in vivo release of membrane that is different from that which is known to occur in vitro.
[Mh] Termos MeSH primário: Senescência Celular
Membrana Eritrocítica/metabolismo
Eritrócitos/citologia
[Mh] Termos MeSH secundário: Micropartículas Derivadas de Células/metabolismo
Eritrócitos/metabolismo
Seres Humanos
Proteínas de Membrana/análise
Proteínas de Membrana/metabolismo
Espectrina/análise
Espectrina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (flotillins); 12634-43-4 (Spectrin)
[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:170703
[St] Status:MEDLINE
[do] DOI:10.1159/000478768


  10 / 3247 MEDLINE  
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[PMID]:28668958
[Au] Autor:Ciana A; Achilli C; Minetti G
[Ti] Título:Spectrin and Other Membrane-Skeletal Components in Human Red Blood Cells of Different Age.
[So] Source:Cell Physiol Biochem;42(3):1139-1152, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Old human red blood cells (RBCs) have a reduced surface area with respect to young RBCs. If this decrease occurred through the release of vesicles similar to the spectrin-free vesicles that are shed in vitro under different experimental conditions or during storage, there would be no decrease of membrane-skeleton, but only of lipid bilayer surface area, during RBC ageing in vivo. However, we observed a decrease in spectrin and other membrane-skeletal proteins in old RBCs. Because RBCs contain components of the ubiquitin-proteasome system and other hydrolytic systems for protein degradation, we asked whether increased membrane-skeleton fragments could be detected in older RBCs. METHODS: Four different anti-spectrin antibodies and an antibody anti-ubiquitin conjugates were used to analyse, by Western blotting, fragments of spectrin and other proteins in RBCs of different age separated in density gradients and characterized for their protein 4.1a/4.1b ratio as a cell age parameter. RESULTS: spectrin fragments do exist in RBCs of all ages, they represent a minute fraction of all spectrin, are membrane-bound and not cytoplasmic and do not increase with cell age. Besides spectrin, other membrane-skeletal components decrease with cell age. CONCLUSION: Observed results challenge the commonly accepted view that decrease in cell membrane throughout RBC life in vivo occurs via the release of spectrin-free vesicles.
[Mh] Termos MeSH primário: Senescência Celular
Eritrócitos/citologia
Espectrina/análise
[Mh] Termos MeSH secundário: Citoesqueleto/metabolismo
Membrana Eritrocítica/metabolismo
Eritrócitos/metabolismo
Exossomos/metabolismo
Seres Humanos
Proteínas de Membrana/metabolismo
Multimerização Proteica
Espectrina/metabolismo
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membrane Proteins); 12634-43-4 (Spectrin)
[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:170703
[St] Status:MEDLINE
[do] DOI:10.1159/000478769



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