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[PMID]:26160559
[Au] Autor:Hnasko RM
[Ad] Endereço:Produce Safety and Microbiology Unit (PSM), Western Regional Research Center (WRRC), Pacific West Area (PWA), Agricultural Research Service (ARS), United States Department of Agriculture (USDA), 800 Buchanan St., Albany, CA, 94710, USA, Robert.hnasko@ars.usda.gov.
[Ti] Título:The Biochemical Properties of Antibodies and Their Fragments.
[So] Source:Methods Mol Biol;1318:1-14, 2015.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Immunoglobulins (Ig) or antibodies are powerful molecular recognition tools that can be used to identify minute quantities of a given target analyte. Their antigen-binding properties define both the sensitivity and selectivity of an immunoassay. Understanding the biochemical properties of this class of protein will provide users with the knowledge necessary to select the appropriate antibody composition to maximize immunoassay results. Here we define the general biochemical properties of antibodies and their similarities and differences, explain how these properties influence their functional relationship to an antigen target, and describe a method for the enzymatic fragmentation of antibodies into smaller functional parts.
[Mh] Termos MeSH primário: Anticorpos/isolamento & purificação
Cromatografia de Afinidade/métodos
Imunoensaio
Fragmentos Fab das Imunoglobulinas/isolamento & purificação
Fragmentos Fc das Imunoglobulinas/isolamento & purificação
[Mh] Termos MeSH secundário: Animais
Anticorpos/química
Afinidade de Anticorpos
Especificidade de Anticorpos
Reações Antígeno-Anticorpo
Antígenos/química
Epitopos/química
Seres Humanos
Fragmentos Fab das Imunoglobulinas/química
Fragmentos Fc das Imunoglobulinas/química
Isotipos de Imunoglobulinas/química
Isotipos de Imunoglobulinas/isolamento & purificação
Subunidades de Imunoglobulinas/química
Subunidades de Imunoglobulinas/isolamento & purificação
Modelos Moleculares
Papaína/química
Ligação Proteica
Sensibilidade e Especificidade
Proteína Estafilocócica A/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies); 0 (Antigens); 0 (Epitopes); 0 (Immunoglobulin Fab Fragments); 0 (Immunoglobulin Fc Fragments); 0 (Immunoglobulin Isotypes); 0 (Immunoglobulin Subunits); 0 (Staphylococcal Protein A); EC 3.4.22.2 (Papain)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:150710
[Lr] Data última revisão:
150710
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150711
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-2742-5_1


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[PMID]:25491494
[Au] Autor:Kim H; Jang W; Shin S; Park J; Kim M; Kim Y; Han K; Lee GD; Won H; Yang YJ
[Ad] Endereço:Department of Laboratory Medicine, College of Medicine, The Catholic University of Korea, Daejeon St. Mary's Hospital, Daejeon, 301-723, Korea (South).
[Ti] Título:Two cases of concurrent development of essential thrombocythemia with chronic lymphocytic leukemia, one related to clonal B-cell lymphocytosis, tested by array comparative genomic hybridization.
[So] Source:Int J Hematol;101(6):612-9, 2015 Jun.
[Is] ISSN:1865-3774
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:We present two cases of concurrent development of essential thrombocythemia (ET) with chronic lymphocytic leukemia (CLL) and one related to clonal B-cell lymphocytosis (CBL). Both patients were referred for lymphocytosis and thrombocytosis. A bone marrow biopsy revealed infiltration of small, mature lymphocytes and megakaryocytic hyperplasia. Flow cytometric immunophenotyping and immunoglobulin (IG) gene clonality tests revealed clonal B lymphocytes. Both patients were positive for the JAK2 V617F mutation in whole bone marrow aspirate. The JAK2 V617F mutation was present in isolated B lymphocytes of patient 1, but not patient 2. Cytogenetics were normal in both patients. An array comparative genomic hybridization (CGH) analyses of B cells revealed a gain of 4q28.3, which is reported in non-Hodgkin's lymphoma, in patient 1, and deletion 22q11.22, which is associated with CLL, and a gain of Xp22.31 in patient 2. In both patients, B cells showed no myeloproliferative neoplasm (MPN)-specific genetic abnormalities. These results suggest that different oncogenic mechanisms in each cell lineage may underlie the concurrent development of ET and CLL (or CBL). Array CGH may be helpful in identifying the pathogenic mechanism in cases of concurrent development of lymphoid neoplasm and MPN.
[Mh] Termos MeSH primário: Leucemia Linfocítica Crônica de Células B/complicações
Linfocitose/complicações
Trombocitemia Essencial/complicações
[Mh] Termos MeSH secundário: Idoso
Linfócitos B/metabolismo
Linfócitos B/patologia
Plaquetas/metabolismo
Plaquetas/patologia
Medula Óssea/patologia
Hibridização Genômica Comparativa
Feminino
Rearranjo Gênico do Linfócito B
Seres Humanos
Subunidades de Imunoglobulinas/genética
Janus Quinase 2/genética
Leucemia Linfocítica Crônica de Células B/genética
Leucemia Linfocítica Crônica de Células B/patologia
Linfocitose/genética
Linfocitose/patologia
Masculino
Mutação Puntual
Trombocitemia Essencial/genética
Trombocitemia Essencial/patologia
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Immunoglobulin Subunits); EC 2.7.10.2 (JAK2 protein, human); EC 2.7.10.2 (Janus Kinase 2)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141211
[St] Status:MEDLINE
[do] DOI:10.1007/s12185-014-1713-9


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[PMID]:25117628
[Au] Autor:Saha S; Pashov A; Siegel ER; Murali R; Kieber-Emmons T
[Ad] Endereço:Bioinformatics Graduate Program, University of Arkansas at Little Rock/University of Arkansas for Medical Sciences, Little Rock, Arkansas, United States of America.
[Ti] Título:Defining the recognition elements of Lewis Y-reactive antibodies.
[So] Source:PLoS One;9(8):e104208, 2014.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Antibody response to carbohydrate antigens is often independent of T cells and the process of affinity/specificity improvement is considered strictly dependent on the germinal centers. Antibodies induced during a T cell-independent type 2 (TI-2) response are less variable and less functionally versatile than those induced with T cell help. The antigen specificity consequences of accumulation of somatic mutations in antibodies during TI-2 responses of Marginal Zone (MZ) B cells is a fact that still needs explanation. Germline genes that define carbohydrate-reactive antibodies are known to sculpt antibody-combining sites containing innate, key side-chain contacts that define the antigen recognition step. However, substitutions associated with MZ B cell derived antibodies might affect the mobility and polyspecificity of the antibody. To examine this hypothesis, we analyzed antibodies reactive with the neolactoseries antigen Lewis Y (LeY) to define the residue subset required for the reactive repertoire for the LeY antigen. Our molecular simulation studies of crystallographically determined and modeled antibody-LeY complexes suggests that the heavy-chain germline gene VH7183.a13.20 and the light-chain Vκ cr1 germline gene are sufficient to account for the recognition of the trisaccharide-H determinant Types 1-4, while the specificity for LeY is driven by the CDR3 backbone conformation of the heavy chain and not the side chain interactions. These results confirm that these monoclonals use germline-encoded amino acids to recognize simple carbohydrate determinants like trisaccharide-H but relies on somatic mutations in the periphery of the combining site to modify affinity for LeY through electrostatic interactions that leads to their optimized binding. These observations bring further attention to the role of mutations in T-cell independent antibodies to distinguish self from non-self carbohydrate antigens.
[Mh] Termos MeSH primário: Anticorpos/imunologia
Sítios de Ligação de Anticorpos/imunologia
Sistema do Grupo Sanguíneo de Lewis/imunologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Anticorpos/química
Anticorpos/genética
Anticorpos Monoclonais/química
Anticorpos Monoclonais/genética
Anticorpos Monoclonais/imunologia
Configuração de Carboidratos
Subunidades de Imunoglobulinas/química
Subunidades de Imunoglobulinas/imunologia
Sistema do Grupo Sanguíneo de Lewis/química
Camundongos
Modelos Moleculares
Dados de Sequência Molecular
Mutação
Ligação Proteica/imunologia
Conformação Proteica
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Antibodies); 0 (Antibodies, Monoclonal); 0 (Immunoglobulin Subunits); 0 (Lewis Blood-Group System); 0 (Lewis Y antigen)
[Em] Mês de entrada:1504
[Cu] Atualização por classe:150805
[Lr] Data última revisão:
150805
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140814
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0104208


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[PMID]:24174674
[Au] Autor:Cameron S; Chang WT; Chen Y; Zhou Y; Taran S; Rao Y
[Ad] Endereço:Department of Neurology and Neurosurgery, McGill Centre for Research in Neuroscience and Departments of Medicine and Biology, McGill University Health Centre, Montreal, Quebec H3G 1A4, Canada.
[Ti] Título:Visual circuit assembly requires fine tuning of the novel Ig transmembrane protein Borderless.
[So] Source:J Neurosci;33(44):17413-21, 2013 Oct 30.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Establishment of synaptic connections in the neuropils of the developing nervous system requires the coordination of specific neurite-neurite interactions (i.e., axon-axon, dendrite-dendrite and axon-dendrite interactions). The molecular mechanisms underlying coordination of neurite-neurite interactions for circuit assembly are incompletely understood. In this report, we identify a novel Ig superfamily transmembrane protein that we named Borderless (Bdl), as a novel regulator of neurite-neurite interactions in Drosophila. Bdl induces homotypic cell-cell adhesion in vitro and mediates neurite-neurite interactions in the developing visual system. Bdl interacts physically and genetically with the Ig transmembrane protein Turtle, a key regulator of axonal tiling. Our results also show that the receptor tyrosine phosphatase leukocyte common antigen-related protein (LAR) negatively regulates Bdl to control synaptic-layer selection. We propose that precise regulation of Bdl action coordinates neurite-neurite interactions for circuit formation in Drosophila.
[Mh] Termos MeSH primário: Comunicação Celular/genética
Proteínas de Drosophila/fisiologia
Rede Nervosa/fisiologia
Vias Visuais/fisiologia
[Mh] Termos MeSH secundário: Animais
Regulação para Baixo/genética
Proteínas de Drosophila/genética
Drosophila melanogaster/enzimologia
Drosophila melanogaster/genética
Feminino
Subunidades de Imunoglobulinas/genética
Imunoglobulinas/genética
Imunoglobulinas/fisiologia
Masculino
Proteínas de Membrana/genética
Proteínas de Membrana/fisiologia
Mutação/genética
Rede Nervosa/enzimologia
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/fisiologia
Neuritos/fisiologia
Proteínas Tirosina Fosfatases Semelhantes a Receptores/genética
Proteínas Tirosina Fosfatases Semelhantes a Receptores/fisiologia
Vias Visuais/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (Immunoglobulin Subunits); 0 (Immunoglobulins); 0 (Membrane Proteins); 0 (Nerve Tissue Proteins); 0 (tutl protein, Drosophila); EC 3.1.3.48 (Lar protein, Drosophila); EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases)
[Em] Mês de entrada:1312
[Cu] Atualização por classe:131031
[Lr] Data última revisão:
131031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131101
[St] Status:MEDLINE
[do] DOI:10.1523/JNEUROSCI.1878-13.2013


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[PMID]:23029324
[Au] Autor:Wang X; Sharp AR; Miller RD
[Ad] Endereço:Center for Evolutionary and Theoretical Immunology, Department of Biology, University of New Mexico, Albuquerque, United States of America.
[Ti] Título:Early postnatal B cell ontogeny and antibody repertoire maturation in the opossum, Monodelphis domestica.
[So] Source:PLoS One;7(9):e45931, 2012.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Marsupials are a lineage of mammals noted for giving birth to highly altricial young, which complete much of their "fetal" development externally attached to a teat. Postnatal B cell ontogeny and diversity was investigated in a model marsupial species, the gray short-tailed opossum, Monodelphis domestica. The results support the initiation of B cell development late in gestation and progressing into the first two weeks of postnatal life. Transcription of CD79a and CD79b was detected in embryonic tissue prior to birth, while immunoglobulin heavy chain locus transcription was not detected until the first postnatal 24 hours. Transcription of the Ig light chains was not detected until postnatal day 7 at the earliest. The predicted timing of the earliest appearance of mature B cells and completion of gene rearrangements is consistent with previous analyses on the timing of endogenous antibody responses in newborn marsupials. The diversity of early B cell IgH chains is limited, as has been seen in fetal humans and mice, but lacks bias in the gene segments used to encode the variable domains. Newborn light chain diversity is, from the start, comparable to that of the adult, consistent with an earlier hypothesis that light chains contribute extensively to antibody diversity in this species.
[Mh] Termos MeSH primário: Linfócitos B/citologia
Regulação da Expressão Gênica no Desenvolvimento
Genes de Imunoglobulinas
Subunidades de Imunoglobulinas/genética
Monodelphis/crescimento & desenvolvimento
Monodelphis/imunologia
[Mh] Termos MeSH secundário: Animais
Diversidade de Anticorpos
Linfócitos B/imunologia
Linfócitos B/metabolismo
Sequência de Bases
Antígenos CD79/genética
Antígenos CD79/imunologia
Embrião de Mamíferos/citologia
Embrião de Mamíferos/imunologia
Embrião de Mamíferos/metabolismo
Rearranjo Gênico
Subunidades de Imunoglobulinas/imunologia
Monodelphis/embriologia
Monodelphis/genética
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (CD79 Antigens); 0 (Immunoglobulin Subunits)
[Em] Mês de entrada:1303
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121003
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0045931


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[PMID]:22661385
[Au] Autor:Kuroda D; Shirai H; Jacobson MP; Nakamura H
[Ad] Endereço:Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, Japan. dkuroda@protein.osaka-u.ac.jp
[Ti] Título:Computer-aided antibody design.
[So] Source:Protein Eng Des Sel;25(10):507-21, 2012 Oct.
[Is] ISSN:1741-0134
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Recent clinical trials using antibodies with low toxicity and high efficiency have raised expectations for the development of next-generation protein therapeutics. However, the process of obtaining therapeutic antibodies remains time consuming and empirical. This review summarizes recent progresses in the field of computer-aided antibody development mainly focusing on antibody modeling, which is divided essentially into two parts: (i) modeling the antigen-binding site, also called the complementarity determining regions (CDRs), and (ii) predicting the relative orientations of the variable heavy (V(H)) and light (V(L)) chains. Among the six CDR loops, the greatest challenge is predicting the conformation of CDR-H3, which is the most important in antigen recognition. Further computational methods could be used in drug development based on crystal structures or homology models, including antibody-antigen dockings and energy calculations with approximate potential functions. These methods should guide experimental studies to improve the affinities and physicochemical properties of antibodies. Finally, several successful examples of in silico structure-based antibody designs are reviewed. We also briefly review structure-based antigen or immunogen design, with application to rational vaccine development.
[Mh] Termos MeSH primário: Anticorpos/química
Anticorpos/imunologia
Projeto Auxiliado por Computador
[Mh] Termos MeSH secundário: Animais
Anticorpos/genética
Afinidade de Anticorpos
Sítios de Ligação de Anticorpos
Seres Humanos
Subunidades de Imunoglobulinas/química
Subunidades de Imunoglobulinas/genética
Subunidades de Imunoglobulinas/imunologia
Região Variável de Imunoglobulina/química
Região Variável de Imunoglobulina/genética
Região Variável de Imunoglobulina/imunologia
Modelos Moleculares
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Antibodies); 0 (Immunoglobulin Subunits); 0 (Immunoglobulin Variable Region)
[Em] Mês de entrada:1302
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120605
[St] Status:MEDLINE


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[PMID]:22558161
[Au] Autor:Ippolito GC; Hoi KH; Reddy ST; Carroll SM; Ge X; Rogosch T; Zemlin M; Shultz LD; Ellington AD; Vandenberg CL; Georgiou G
[Ad] Endereço:Section of Molecular Genetics and Microbiology, University of Texas at Austin, Austin, Texas, United States of America.
[Ti] Título:Antibody repertoires in humanized NOD-scid-IL2Rγ(null) mice and human B cells reveals human-like diversification and tolerance checkpoints in the mouse.
[So] Source:PLoS One;7(4):e35497, 2012.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Immunodeficient mice reconstituted with human hematopoietic stem cells enable the in vivo study of human hematopoiesis. In particular, NOD-scid-IL2Rγ(null) engrafted mice have been shown to have reasonable levels of T and B cell repopulation and can mount T-cell dependent responses; however, antigen-specific B-cell responses in this model are generally poor. We explored whether developmental defects in the immunoglobulin gene repertoire might be partly responsible for the low level of antibody responses in this model. Roche 454 sequencing was used to obtain over 685,000 reads from cDNA encoding immunoglobulin heavy (IGH) and light (IGK and IGL) genes isolated from immature, naïve, or total splenic B cells in engrafted NOD-scid-IL2Rγ(null) mice, and compared with over 940,000 reads from peripheral B cells of two healthy volunteers. We find that while naïve B-cell repertoires in humanized mice are chiefly indistinguishable from those in human blood B cells, and display highly correlated patterns of immunoglobulin gene segment use, the complementarity-determining region H3 (CDR-H3) repertoires are nevertheless extremely diverse and are specific for each individual. Despite this diversity, preferential D(H)-J(H) pairings repeatedly occur within the CDR-H3 interval that are strikingly similar across all repertoires examined, implying a genetic constraint imposed on repertoire generation. Moreover, CDR-H3 length, charged amino-acid content, and hydropathy are indistinguishable between humans and humanized mice, with no evidence of global autoimmune signatures. Importantly, however, a statistically greater usage of the inherently autoreactive IGHV4-34 and IGKV4-1 genes was observed in the newly formed immature B cells relative to naïve B or total splenic B cells in the humanized mice, a finding consistent with the deletion of autoreactive B cells in humans. Overall, our results provide evidence that key features of the primary repertoire are shaped by genetic factors intrinsic to human B cells and are principally unaltered by differences between mouse and human stromal microenvironments.
[Mh] Termos MeSH primário: Anticorpos Monoclonais Humanizados/genética
Linfócitos B/imunologia
Variação Genética
Hematopoese/imunologia
Camundongos Endogâmicos NOD/imunologia
Camundongos SCID/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Monoclonais Humanizados/imunologia
Sequência de Bases
Biologia Computacional
Primers do DNA/genética
DNA Complementar/genética
Citometria de Fluxo
Corantes Fluorescentes
Transplante de Células-Tronco Hematopoéticas
Seres Humanos
Subunidades de Imunoglobulinas/genética
Subunidade gama Comum de Receptores de Interleucina/genética
Camundongos
Camundongos Endogâmicos NOD/genética
Camundongos SCID/genética
Dados de Sequência Molecular
Análise de Sequência de DNA
Estatísticas não Paramétricas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Antibodies, Monoclonal, Humanized); 0 (DNA Primers); 0 (DNA, Complementary); 0 (Fluorescent Dyes); 0 (Il2rg protein, mouse); 0 (Immunoglobulin Subunits); 0 (Interleukin Receptor Common gamma Subunit)
[Em] Mês de entrada:1209
[Cu] Atualização por classe:150225
[Lr] Data última revisão:
150225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120505
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0035497


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[PMID]:21906471
[Au] Autor:Wang JT; Wang J
[Ad] Endereço:Department of Medical Research, Guangzhou General Hospital of Guangzhou Military Command, Guangzhou 510010, China. wjiangtao80@126.com
[Ti] Título:[Screening of single-chain variable fragment (scFv) to bone sialoprotein].
[So] Source:Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi;27(9):979-81, 2011 Sep.
[Is] ISSN:1007-8738
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:AIM: To select single-chain variable fragment(scFv) antibody specific for bone sialoprotein(BSP) from Human Single Fold scFv Libraries. METHODS: Human Single Fold scFv Libraries were panned against immobilized BSP in a microtiter plate, after three rounds of panning, 96 clones were determined specific to BSP. The specificity of each scFv clone was determined by ELISA. The coding gene for BSP protein scFv has been sequenced. RESULTS: Phage antibody for BSP protein had a specific combination character. There were 368 bp, 527 bp, 935 bp which werer light chain, heavy chain and joint gene fragment with the resuLt of PCR. The DNA sequence data showed that there were 11 differences of the amino acids in the light chain, while there were only 3 differences in the heavy chain of scFv. CONCLUSION: scFv specific to BSP has been identified by means of phage display technology.
[Mh] Termos MeSH primário: Sialoproteína de Ligação à Integrina/imunologia
Anticorpos de Cadeia Única/imunologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Especificidade de Anticorpos/genética
Seres Humanos
Subunidades de Imunoglobulinas/genética
Sialoproteína de Ligação à Integrina/metabolismo
Biblioteca de Peptídeos
Anticorpos de Cadeia Única/metabolismo
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Immunoglobulin Subunits); 0 (Integrin-Binding Sialoprotein); 0 (Peptide Library); 0 (Single-Chain Antibodies)
[Em] Mês de entrada:1201
[Cu] Atualização por classe:110912
[Lr] Data última revisão:
110912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110913
[St] Status:MEDLINE


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[PMID]:21903335
[Au] Autor:Petrusic V; Zivkovic I; Stojanovic M; Stojicevic I; Marinkovic E; Dimitrijevic L
[Ad] Endereço:Institute of Virology, Vaccines and Sera - Torlak, Vojvode Stepe 458, 11221 Belgrade, Serbia. vzpetrusic@gmail.com
[Ti] Título:Hexameric immunoglobulin M in humans: desired or unwanted?
[So] Source:Med Hypotheses;77(6):959-61, 2011 Dec.
[Is] ISSN:1532-2777
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Immunoglobulin M (IgM) is the first antibody produced upon infection, and is often suggested as the first line of defense of human immune system. In addition to being present on the surface of naïve B cells as a monomeric molecule, IgM is always secreted as a polymer. The most abundant IgM polymer in humans is pentamer, composed of five monomeric units, joined together by so-called joining or J chain. On the other hand, it is well known that hexameric IgM can be also found in human sera. Its presence is often related to different dissorders (Waldenström's macroglobulinemia, cold agglutinin, and recurrent urinary bacterial infections), although it is believed that small amounts of hexamer are present in normal human sera as well. Unlike pentamer, IgM hexamer contains six monomeric blocks and completely lacks J chain. Although it has been decades since its discovery, the precise function of IgM hexamer is still unknown. Since it was documented that hexamer is very potent in activating complement, it is suggested that its production in humans must be under strict control, and that it is produced in special conditions, when strong activation of complement is absolutely needed. However, the question is whether hexameric IgM is really a secret weapon or just an undesirable molecule in humans. According to structural and known functional characteristics of both pentamers and hexamers of IgM, it can be concluded that hexamers are, in addition to being maybe too reactive to be around, probably not that efficient in protecting us from bacterial and viral infections.
[Mh] Termos MeSH primário: Ativação do Complemento/imunologia
Imunoglobulina M/química
Imunoglobulina M/imunologia
Subunidades de Imunoglobulinas/imunologia
[Mh] Termos MeSH secundário: Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Immunoglobulin M); 0 (Immunoglobulin Subunits)
[Em] Mês de entrada:1203
[Cu] Atualização por classe:111107
[Lr] Data última revisão:
111107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110910
[St] Status:MEDLINE
[do] DOI:10.1016/j.mehy.2011.08.018


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[PMID]:21842603
[Au] Autor:Kimura Y; Imai H
[Ti] Título:[Secondary membranous nephropathy].
[So] Source:Nihon Jinzo Gakkai Shi;53(5):697-702, 2011.
[Is] ISSN:0385-2385
[Cp] País de publicação:Japan
[La] Idioma:jpn
[Mh] Termos MeSH primário: Glomerulonefrite Membranosa/etiologia
[Mh] Termos MeSH secundário: Aldeído Redutase/imunologia
Antirreumáticos/efeitos adversos
Doenças Autoimunes/complicações
Transporte Biológico
Membrana Basal Glomerular/metabolismo
Glomerulonefrite Membranosa/diagnóstico
Glomerulonefrite Membranosa/imunologia
Glomerulonefrite Membranosa/patologia
Doença Enxerto-Hospedeiro/complicações
Antígenos de Histocompatibilidade Classe I/fisiologia
Seres Humanos
Imunoglobulina G/metabolismo
Subunidades de Imunoglobulinas/metabolismo
Infecção/complicações
Neoplasias/complicações
Neprilisina/imunologia
Fosfopiruvato Hidratase/imunologia
Receptores Fc/fisiologia
Receptores da Fosfolipase A2/imunologia
Superóxido Dismutase/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antirheumatic Agents); 0 (Fc receptor, neonatal); 0 (Histocompatibility Antigens Class I); 0 (Immunoglobulin G); 0 (Immunoglobulin Subunits); 0 (Receptors, Fc); 0 (Receptors, Phospholipase A2); EC 1.1.1.21 (Aldehyde Reductase); EC 1.15.1.1 (Superoxide Dismutase); EC 1.15.1.1 (superoxide dismutase 2); EC 3.4.24.11 (Neprilysin); EC 4.2.1.11 (Phosphopyruvate Hydratase)
[Em] Mês de entrada:1111
[Cu] Atualização por classe:110816
[Lr] Data última revisão:
110816
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110817
[St] Status:MEDLINE



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