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Pesquisa : D12.776.543.940.200 [Categoria DeCS]
Referências encontradas : 1361 [refinar]
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  1 / 1361 MEDLINE  
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[PMID]:29223398
[Au] Autor:Sun J; Wang X; Shi Y; Li J; Li C; Shi Z; Chen Y; Mao B
[Ad] Endereço:State Key Laboratory of Genetic Resources and Evolution, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, China.
[Ti] Título:EphA7 regulates claudin6 and pronephros development in Xenopus.
[So] Source:Biochem Biophys Res Commun;495(2):1580-1587, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Eph/ephrin molecules are widely expressed during embryonic development, and function in a variety of developmental processes. Here we studied the roles of the Eph receptor EphA7 and its soluble form in Xenopus pronephros development. EphA7 is specifically expressed in pronephric tubules at tadpole stages and knockdown of EphA7 by a translation blocking morpholino led to defects in tubule cell differentiation and morphogenesis. A soluble form of EphA7 (sEphA7) was also identified. Interestingly, the membrane level of claudin6 (CLDN6), a tetraspan transmembrane tight junction protein, was dramatically reduced in the translation blocking morpholino injected embryos, but not when a splicing morpholino was used, which blocks only the full length EphA7. In cultured cells, EphA7 binds and phosphorylates CLDN6, and reduces its distribution at the cell surface. Our work suggests a role of EphA7 in the regulation of cell adhesion during pronephros development, whereas sEphA7 works as an antagonist.
[Mh] Termos MeSH primário: Claudinas/metabolismo
Pronefro/embriologia
Receptor EphA7/metabolismo
Proteínas de Xenopus/metabolismo
Xenopus laevis/embriologia
Xenopus laevis/metabolismo
[Mh] Termos MeSH secundário: Animais
Membrana Celular/metabolismo
Regulação da Expressão Gênica no Desenvolvimento
Técnicas de Silenciamento de Genes
Oligodesoxirribonucleotídeos Antissenso/genética
Pronefro/metabolismo
Receptor EphA7/antagonistas & inibidores
Receptor EphA7/genética
Solubilidade
Proteínas de Xenopus/antagonistas & inibidores
Proteínas de Xenopus/genética
Xenopus laevis/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Claudins); 0 (Oligodeoxyribonucleotides, Antisense); 0 (Xenopus Proteins); 0 (claudin 6); EC 2.7.10.1 (Receptor, EphA7)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171211
[St] Status:MEDLINE


  2 / 1361 MEDLINE  
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[PMID]:27771288
[Au] Autor:Gauberg J; Kolosov D; Kelly SP
[Ad] Endereço:Department of Biology, York University, 4700 Keele St, Toronto, ON M3J 1P3 Canada.
[Ti] Título:Claudin tight junction proteins in rainbow trout (Oncorhynchus mykiss) skin: Spatial response to elevated cortisol levels.
[So] Source:Gen Comp Endocrinol;240:214-226, 2017 01 01.
[Is] ISSN:1095-6840
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:This study examined regional distribution and corticosteroid-induced alterations of claudin (cldn) transcript abundance in teleost fish skin. Regional comparison of mRNA encoding 20 Cldns indicated that 12 exhibit differences in abundance along the dorsoventral axis of skin. However, relative abundance of cldns (i.e. most to least abundant) remained similar in different skin regions. Several cldns appear to be present in the epidermis and dermal vasculature whereas others are present only in the epidermis. Increased circulating cortisol levels significantly altered mRNA abundance of 10 cldns in a region specific manner, as well as corticosteroid receptors and 11ß-hydroxysteroid dehydrogenase (type 2). Epidermis and epidermal mucous cell morphometrics also altered in response to cortisol, exhibiting changes that appear to enhance skin barrier properties. Taken together, data provide a first look at spatial variation in the molecular physiology of the teleost fish integument TJ complex and region-specific sensitivity to an endocrine factor.
[Mh] Termos MeSH primário: Claudinas/metabolismo
Hidrocortisona/farmacologia
Oncorhynchus mykiss/metabolismo
Pele/metabolismo
Junções Íntimas/metabolismo
[Mh] Termos MeSH secundário: 11-beta-Hidroxiesteroide Desidrogenases/metabolismo
Animais
Cloretos/sangue
Claudinas/genética
Dieta
Epiderme/efeitos dos fármacos
Epiderme/metabolismo
Células Epiteliais/efeitos dos fármacos
Células Epiteliais/metabolismo
Proteínas de Peixes/genética
Proteínas de Peixes/metabolismo
Hidrocortisona/administração & dosagem
Músculos/efeitos dos fármacos
Músculos/metabolismo
RNA Mensageiro/metabolismo
Pele/efeitos dos fármacos
Sódio/sangue
Junções Íntimas/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chlorides); 0 (Claudins); 0 (Fish Proteins); 0 (RNA, Messenger); 9NEZ333N27 (Sodium); EC 1.1.1.146 (11-beta-Hydroxysteroid Dehydrogenases); WI4X0X7BPJ (Hydrocortisone)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180124
[Lr] Data última revisão:
180124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


  3 / 1361 MEDLINE  
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[PMID]:28939759
[Au] Autor:Wang Y; Mumm JB; Herbst R; Kolbeck R; Wang Y
[Ad] Endereço:Department of Oncology Research, MedImmune, Gaithersburg, MD 20878; and.
[Ti] Título:IL-22 Increases Permeability of Intestinal Epithelial Tight Junctions by Enhancing Claudin-2 Expression.
[So] Source:J Immunol;199(9):3316-3325, 2017 Nov 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dysfunction of the epithelial barrier is a hallmark of inflammatory intestinal diseases. The intestinal epithelial barrier is maintained by expression of tight junctions that connect adjacent epithelial cells and seal the paracellular space. IL-22 is critical for the maintenance of intestinal barrier function through promoting antipathogen responses and regeneration of epithelial tissues in the gut. However, little is known about the effects of IL-22 on the regulation of tight junctions in the intestinal epithelium. In this study we report that IL-22 signals exclusively through the basolateral side of polarized Caco-2 cell monolayers. IL-22 treatment does not affect the flux of uncharged macromolecules across cell monolayers but significantly reduces transepithelial electrical resistance (TEER), indicating an increase of paracellular permeability for ions. IL-22 treatment on Caco-2 monolayers and on primary human intestinal epithelium markedly induces the expression of Claudin-2, a cation-channel-forming tight junction protein. Furthermore, treatment of IL-22 in mice upregulates Claudin-2 protein in colonic epithelial cells. Knocking down Claudin-2 expression with small interfering RNA reverses the reduction of TEER in IL-22-treated cells. Moreover, IL-22-mediated upregulation of Claudin-2 and loss of TEER can be suppressed with the treatment of JAK inhibitors. In summary, our results reveal that IL-22 increases intestinal epithelial permeability by upregulating Claudin-2 expression through the JAK/STAT pathway. These results provide novel mechanistic insights into the role of IL-22 in the regulation and maintenance of the intestinal epithelial barrier.
[Mh] Termos MeSH primário: Claudinas/imunologia
Interleucinas/imunologia
Mucosa Intestinal/imunologia
Transdução de Sinais/imunologia
Junções Íntimas/imunologia
Regulação para Cima/imunologia
[Mh] Termos MeSH secundário: Animais
Células CACO-2
Seres Humanos
Masculino
Camundongos
Camundongos Endogâmicos BALB C
Permeabilidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CLDN2 protein, human); 0 (Claudins); 0 (Cldn2 protein, mouse); 0 (Interleukins); 0 (interleukin-22)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170924
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1700152


  4 / 1361 MEDLINE  
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[PMID]:28878076
[Au] Autor:Siemann DN; Strange DP; Maharaj PN; Shi PY; Verma S
[Ad] Endereço:Department of Tropical Medicine, Medical Microbiology and Pharmacology, John A. Burns School of Medicine, University of Hawaii at Manoa, Honolulu, Hawaii, USA.
[Ti] Título:Zika Virus Infects Human Sertoli Cells and Modulates the Integrity of the Blood-Testis Barrier Model.
[So] Source:J Virol;91(22), 2017 Nov 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Confirmed reports of Zika virus (ZIKV) in human seminal fluid for months after the clearance of viremia suggest the ability of ZIKV to establish persistent infection in the seminiferous tubules, an immune-privileged site in the testis protected by the blood-testis barrier, also called the Sertoli cell (SC) barrier (SCB). However, cellular targets of ZIKV in human testis and mechanisms by which the virus enters seminiferous tubules remain unclear. We demonstrate that primary human SCs were highly susceptible to ZIKV compared to the closely related dengue virus and induced the expression of alpha interferon (IFN-α), key cytokines, and cell adhesion molecules (vascular cell adhesion molecule 1 [VCAM-1] and intracellular adhesion molecule 1 [ICAM-1]). Furthermore, using an SCB model, we show that ZIKV was released on the adluminal side of the SCB model with a higher efficiency than in the blood-brain barrier model. ZIKV-infected SCs exhibited enhanced adhesion of leukocytes that correlated with decreases in SCB integrity. ZIKV infection did not affect the expression of tight and adherens junction proteins such as ZO-1, claudin, and JAM-A; however, exposure of SCs to inflammatory mediators derived from ZIKV-infected macrophages led to the degradation of the ZO-1 protein, which correlated with increased SCB permeability. Taken together, our data suggest that infection of SCs may be one of the crucial steps by which ZIKV gains access to the site of spermatozoon development and identify SCs as a therapeutic target to clear testicular infections. The SCB model opens up opportunities to assess interactions of SCs with other testicular cells and to test the ability of anti-ZIKV drugs to cross the barrier. Recent outbreaks of ZIKV, a neglected mosquito-borne flavivirus, have identified sexual transmission as a new route of disease spread, which has not been reported for other flaviviruses. To be able to sexually transmit for months after the clearance of viremia, ZIKV must establish infection in the seminiferous tubules, the site of spermatozoon development. However, little is known about the cell types that support ZIKV infection in the human testis. Currently, there are no models to study mechanisms of virus persistence in the seminiferous tubules. We provide evidence that ZIKV infection of human Sertoli cells, which are an important component of the seminiferous tubules, is robust and induces a strong antiviral response. The use of an Sertoli cell barrier to describe how ZIKV or inflammatory mediators derived from ZIKV-infected macrophages compromise barrier integrity will enable studies to explore the interactions of other testicular cells with Sertoli cells and to test novel antivirals for clearing testicular ZIKV infection.
[Mh] Termos MeSH primário: Barreira Hematotesticular/imunologia
Células de Sertoli/imunologia
Infecção pelo Zika virus/imunologia
Zika virus/imunologia
[Mh] Termos MeSH secundário: Barreira Hematotesticular/patologia
Barreira Hematotesticular/virologia
Moléculas de Adesão Celular/imunologia
Células Cultivadas
Claudinas/imunologia
Dengue/imunologia
Dengue/patologia
Vírus da Dengue/imunologia
Seres Humanos
Interferon-alfa/imunologia
Macrófagos/imunologia
Macrófagos/patologia
Masculino
Receptores de Superfície Celular/imunologia
Células de Sertoli/patologia
Células de Sertoli/virologia
Molécula 1 de Adesão de Célula Vascular/imunologia
Infecção pelo Zika virus/patologia
Proteína da Zônula de Oclusão-1/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Adhesion Molecules); 0 (Claudins); 0 (F11R protein, human); 0 (Interferon-alpha); 0 (Receptors, Cell Surface); 0 (TJP1 protein, human); 0 (Vascular Cell Adhesion Molecule-1); 0 (Zonula Occludens-1 Protein)
[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:170908
[St] Status:MEDLINE


  5 / 1361 MEDLINE  
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[PMID]:28869648
[Au] Autor:Tanaka H; Tamura A; Suzuki K; Tsukita S
[Ad] Endereço:Laboratory of Biological Science, Graduate School of Frontier Biosciences and Graduate School of Medicine, Osaka University, Osaka, Japan.
[Ti] Título:Site-specific distribution of claudin-based paracellular channels with roles in biological fluid flow and metabolism.
[So] Source:Ann N Y Acad Sci;1405(1):44-52, 2017 Oct.
[Is] ISSN:1749-6632
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The claudins are a family of membrane proteins with at least 27 members in humans and mice. The extracellular regions of claudin proteins play essential roles in cell-cell adhesion and the paracellular barrier functions of tight junctions (TJs) in epithelial cell sheets. Furthermore, the extracellular regions of some claudins function as paracellular channels in the paracellular barrier that allow the selective passage of water, ions, and/or small organic solutes across the TJ in the extracellular space. Structural analyses have revealed a common framework of transmembrane, cytoplasmic, and extracellular regions among the claudin-based paracellular barriers and paracellular channels; however, differences in the claudins' extracellular regions, such as their charges and conformations, determine their properties. Among the biological systems that involve fluid flow and metabolism, it is noted that hepatic bile flow, renal Na reabsorption, and intestinal nutrient absorption are dynamically regulated via site-specific distributions of paracellular channel-forming claudins in tissue. Here, we focus on how site-specific distributions of claudin-2- and claudin-15-based paracellular channels drive their organ-specific functions in the liver, kidney, and intestine.
[Mh] Termos MeSH primário: Claudinas/metabolismo
Células Epiteliais/metabolismo
Proteínas de Membrana/metabolismo
Junções Íntimas/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Absorção Intestinal/fisiologia
Transporte de Íons/fisiologia
Camundongos
Camundongos Knockout
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Claudins); 0 (Membrane Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170905
[St] Status:MEDLINE
[do] DOI:10.1111/nyas.13438


  6 / 1361 MEDLINE  
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[PMID]:28863193
[Au] Autor:Alberini G; Benfenati F; Maragliano L
[Ad] Endereço:Center for Synaptic Neuroscience & Technology (NSYN@UniGe), Istituto Italiano di Tecnologia, Largo Rosanna Benzi, 10, 16132, Genova, Italy.
[Ti] Título:A refined model of claudin-15 tight junction paracellular architecture by molecular dynamics simulations.
[So] Source:PLoS One;12(9):e0184190, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tight-junctions between epithelial cells of biological barriers are specialized molecular structures that regulate the flux of solutes across the barrier, parallel to cell walls. The tight-junction backbone is made of strands of transmembrane proteins from the claudin family, but the molecular mechanism of its function is still not completely understood. Recently, the crystal structure of a mammalian claudin-15 was reported, displaying for the first time the detailed features of transmembrane and extracellular domains. Successively, a structural model of claudin-15-based paracellular channels has been proposed, suggesting a putative assembly that illustrates how claudins associate in the same cell (via cis interactions) and across adjacent cells (via trans interactions). Although very promising, the model offers only a static conformation, with residues missing in the most important extracellular regions and potential steric clashes. Here we present detailed atomic models of paracellular single and double pore architectures, obtained from the putative assembly and refined via structural modeling and all-atom molecular dynamics simulations in double membrane bilayer and water environment. Our results show an overall stable configuration of the complex with a fluctuating pore size. Extracellular residue loops in trans interaction are able to form stable contacts and regulate the size of the pore, which displays a stationary radius of 2.5-3.0 Å at the narrowest region. The side-by-side interactions of the cis configuration are preserved via stable hydrogen bonds, already predicted by cysteine crosslinking experiments. Overall, this work introduces an improved version of the claudin-15-based paracellular channel model that strengthens its validity and that can be used in further computational studies to understand the structural features of tight-junctions regulation.
[Mh] Termos MeSH primário: Claudinas/química
Simulação de Dinâmica Molecular
Junções Íntimas/química
[Mh] Termos MeSH secundário: Simulação por Computador
Cristalografia por Raios X
Seres Humanos
Ligações de Hidrogênio
Estrutura Molecular
Conformação Proteica
Domínios Proteicos
Multimerização Proteica
Software
Solventes/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Claudins); 0 (Solvents); 0 (claudin 15)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170902
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184190


  7 / 1361 MEDLINE  
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[PMID]:28825599
[Au] Autor:Taylor NA; Vick SC; Iglesia MD; Brickey WJ; Midkiff BR; McKinnon KP; Reisdorf S; Anders CK; Carey LA; Parker JS; Perou CM; Vincent BG; Serody JS
[Ad] Endereço:Lineberger Comprehensive Cancer Center.
[Ti] Título:Treg depletion potentiates checkpoint inhibition in claudin-low breast cancer.
[So] Source:J Clin Invest;127(9):3472-3483, 2017 Sep 01.
[Is] ISSN:1558-8238
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Claudin-low breast cancer is an aggressive subtype that confers poor prognosis and is found largely within the clinical triple-negative group of breast cancer patients. Here, we have shown that intrinsic and immune cell gene signatures distinguish the claudin-low subtype clinically as well as in mouse models of other breast cancer subtypes. Despite adaptive immune cell infiltration in claudin-low tumors, treatment with immune checkpoint inhibitory antibodies against cytotoxic T lymphocyte-associated protein 4 (CTLA-4) and programmed death receptor 1 (PD-1) were ineffective in controlling tumor growth. CD4+FoxP3+ Tregs represented a large proportion of the tumor-infiltrating lymphocytes (TILs) in claudin-low tumors, and Tregs isolated from tumor-bearing mice were able to suppress effector T cell responses. Tregs in the tumor microenvironment highly expressed PD-1 and were recruited partly through tumor generation of the chemokine CXCL12. Antitumor efficacy required stringent Treg depletion combined with checkpoint inhibition; delays in tumor growth were not observed using therapies that modestly diminished the number of Tregs in the tumor microenvironment. This study provides evidence that the recruitment of Tregs to the tumor microenvironment inhibits an effective antitumor immune response and highlights early Treg recruitment as a possible mechanism for the lack of response to immune checkpoint blockade antibodies in specific subtypes of cancer that are heavily infiltrated with adaptive immune cells.
[Mh] Termos MeSH primário: Pontos de Checagem do Ciclo Celular
Claudinas/metabolismo
Linfócitos do Interstício Tumoral/imunologia
Linfócitos T Reguladores/imunologia
Neoplasias de Mama Triplo Negativas/tratamento farmacológico
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/farmacologia
Biomarcadores Tumorais/metabolismo
Linfócitos T CD4-Positivos/imunologia
Antígeno CTLA-4/metabolismo
Quimiocina CXCL12/metabolismo
Análise por Conglomerados
Modelos Animais de Doenças
Feminino
Perfilação da Expressão Gênica
Seres Humanos
Linfócitos do Interstício Tumoral/citologia
Neoplasias Mamárias Animais/tratamento farmacológico
Neoplasias Mamárias Animais/imunologia
Camundongos
Camundongos Endogâmicos BALB C
Camundongos Endogâmicos C57BL
Análise de Sequência com Séries de Oligonucleotídeos
Receptor de Morte Celular Programada 1/metabolismo
Neoplasias de Mama Triplo Negativas/imunologia
Microambiente Tumoral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Biomarkers, Tumor); 0 (CTLA-4 Antigen); 0 (CTLA4 protein, human); 0 (CXCL12 protein, human); 0 (Chemokine CXCL12); 0 (Claudins); 0 (PDCD1 protein, human); 0 (Programmed Cell Death 1 Receptor)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170822
[St] Status:MEDLINE


  8 / 1361 MEDLINE  
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[PMID]:28813441
[Au] Autor:Gehne N; Lamik A; Lehmann M; Haseloff RF; Andjelkovic AV; Blasig IE
[Ad] Endereço:Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany.
[Ti] Título:Cross-over endocytosis of claudins is mediated by interactions via their extracellular loops.
[So] Source:PLoS One;12(8):e0182106, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Claudins (Cldns) are transmembrane tight junction (TJ) proteins that paracellularly seal endo- and epithelial barriers by their interactions within the TJs. However, the mechanisms allowing TJ remodeling while maintaining barrier integrity are largely unknown. Cldns and occludin are heterophilically and homophilically cross-over endocytosed into neighboring cells in large, double membrane vesicles. Super-resolution microscopy confirmed the presence of Cldns in these vesicles and revealed a distinct separation of Cldns derived from opposing cells within cross-over endocytosed vesicles. Colocalization of cross-over endocytosed Cldn with the autophagosome markers as well as inhibition of autophagosome biogenesis verified involvement of the autophagosomal pathway. Accordingly, cross-over endocytosed Cldns underwent lysosomal degradation as indicated by lysosome markers. Cross-over endocytosis of Cldn5 depended on clathrin and caveolin pathways but not on dynamin. Cross-over endocytosis also depended on Cldn-Cldn-interactions. Amino acid substitutions in the second extracellular loop of Cldn5 (F147A, Q156E) caused impaired cis- and trans-interaction, as well as diminished cross-over endocytosis. Moreover, F147A exhibited an increased mobility in the membrane, while Q156E was not as mobile but enhanced the paracellular permeability. In conclusion, the endocytosis of TJ proteins depends on their ability to interact strongly with each other in cis and trans, and the mobility of Cldns in the membrane is not necessarily an indicator of barrier permeability. TJ-remodeling via cross-over endocytosis represents a general mechanism for the degradation of transmembrane proteins in cell-cell contacts and directly links junctional membrane turnover to autophagy.
[Mh] Termos MeSH primário: Clatrina/metabolismo
Claudinas/metabolismo
Endocitose/fisiologia
[Mh] Termos MeSH secundário: Animais
Caveolina 1/metabolismo
Linhagem Celular
Clorpromazina/farmacologia
Claudina-3/metabolismo
Claudinas/química
Claudinas/genética
Cães
Endocitose/efeitos dos fármacos
Endocitose/genética
Filipina/farmacologia
Seres Humanos
Imuno-Histoquímica
Camundongos
Ocludina/metabolismo
Ligação Proteica/genética
Ligação Proteica/fisiologia
Transdução de Sinais/efeitos dos fármacos
Junções Íntimas/efeitos dos fármacos
Junções Íntimas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caveolin 1); 0 (Clathrin); 0 (Claudin-3); 0 (Claudins); 0 (Occludin); 87Z59R7D14 (Filipin); U42B7VYA4P (Chlorpromazine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170817
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182106


  9 / 1361 MEDLINE  
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[PMID]:28737760
[Au] Autor:Twomey EC; Yelshanskaya MV; Grassucci RA; Frank J; Sobolevsky AI
[Ad] Endereço:Department of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, New York, New York 10032, USA.
[Ti] Título:Channel opening and gating mechanism in AMPA-subtype glutamate receptors.
[So] Source:Nature;549(7670):60-65, 2017 09 07.
[Is] ISSN:1476-4687
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid)-subtype ionotropic glutamate receptors mediate fast excitatory neurotransmission throughout the central nervous system. Gated by the neurotransmitter glutamate, AMPA receptors are critical for synaptic strength, and dysregulation of AMPA receptor-mediated signalling is linked to numerous neurological diseases. Here we use cryo-electron microscopy to solve the structures of AMPA receptor-auxiliary subunit complexes in the apo, antagonist- and agonist-bound states and determine the iris-like mechanism of ion channel opening. The ion channel selectivity filter is formed by the extended portions of the re-entrant M2 loops, while the helical portions of M2 contribute to extensive hydrophobic interfaces between AMPA receptor subunits in the ion channel. We show how the permeation pathway changes upon channel opening and identify conformational changes throughout the entire AMPA receptor that accompany activation and desensitization. Our findings provide a framework for understanding gating across the family of ionotropic glutamate receptors and the role of AMPA receptors in excitatory neurotransmission.
[Mh] Termos MeSH primário: Microscopia Crioeletrônica
Ativação do Canal Iônico
Receptores de AMPA/química
Receptores de AMPA/ultraestrutura
[Mh] Termos MeSH secundário: Animais
Canais de Cálcio/metabolismo
Claudinas/metabolismo
Células HEK293
Seres Humanos
Interações Hidrofóbicas e Hidrofílicas
Camundongos
Modelos Moleculares
Conformação Proteica
Subunidades Proteicas/agonistas
Subunidades Proteicas/antagonistas & inibidores
Subunidades Proteicas/química
Subunidades Proteicas/metabolismo
Ratos
Receptores de AMPA/agonistas
Receptores de AMPA/antagonistas & inibidores
Transmissão Sináptica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Calcium Channels); 0 (Claudins); 0 (GSG1L protein, mouse); 0 (Protein Subunits); 0 (Receptors, AMPA); 0 (glutamate receptor ionotropic, AMPA 2)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170725
[St] Status:MEDLINE
[do] DOI:10.1038/nature23479


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[PMID]:28695768
[Au] Autor:Bojrab D; Zhang B; Jiang H; Zhang L; Cohen DS; Luo X; Hu Z
[Ad] Endereço:1 Department of Otolaryngology-Head and Neck Surgery, Wayne State University, Detroit, Michigan, USA.
[Ti] Título:Expression of Oligodendrocyte Marker during Peripheral-Central Transitional Zone Formation of the Postnatal Mouse Cochlear Nerve.
[So] Source:Otolaryngol Head Neck Surg;157(3):488-492, 2017 Sep.
[Is] ISSN:1097-6817
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Objective To better understand oligodendrocyte protein expression along the mouse cochlear nerve in postnatal mice. Study Design In vivo murine study. Setting Research laboratory. Subjects and Methods Swiss Webster mice used at multiple postnatal days (0, 1, 3, 5, 7, 8, 10, 14, 30, and 60). There were 5 replicates at each postnatal day. Cryosection was done to produce sections that included the cochlear nucleus, cochlear nerve, and cochlea in a single sample. Differential interference contrast (DIC) microscopy and immunofluorescence with antibodies specific to the oligodendrocyte protein Olig2 were used to study the cochlear nerve of Swiss Webster mice at postnatal days. Results The myelination of central nervous system projections initiates in close proximity to the peripheral nervous system-central nervous system transitional zone (PCTZ), and oligodendrocytes in neonatal mice are seen with immunohistochemistry peripheral to the DIC-PCTZ interface. Conclusions As the PCTZ migrates from the brain to the cochlea, oligodendrocytes are a part of peripheral extension of central nervous system tissue along the cochlear nerve. Expression of oligodendrocyte marker Oligo2 was observed peripherally to the formation of PCTZ, as determined by DIC microscopy.
[Mh] Termos MeSH primário: Claudinas/biossíntese
Nervo Coclear/crescimento & desenvolvimento
Oligodendroglia/metabolismo
[Mh] Termos MeSH secundário: Animais
Animais Recém-Nascidos
Biomarcadores/análise
Claudinas/análise
Camundongos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Claudins); 0 (Cldn11 protein, mouse)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170712
[St] Status:MEDLINE
[do] DOI:10.1177/0194599817718806



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