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Pesquisa : D08.811.277.040.330.200.100 [Categoria DeCS]
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[PMID]:28674108
[Au] Autor:Schmid SL
[Ad] Endereço:Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX sandra.schmid@utsouthwestern.edu.
[Ti] Título:Reciprocal regulation of signaling and endocytosis: Implications for the evolving cancer cell.
[So] Source:J Cell Biol;216(9):2623-2632, 2017 Sep 04.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cell surface receptor uptake via clathrin-mediated endocytosis (CME) and subsequent intracellular sorting for degradation or recycling regulates the strength and specificity of downstream signaling. Signaling, in turn, modulates early endocytic trafficking. This reciprocal regulation of signaling and endocytosis provides opportunities for the establishment of feedback loops to enhance or suppress surface-derived signals. Recent studies suggest that dynamin-1, a presumed neuron-specific isoform of the large, membrane fission GTPase, can be activated in nonneuronal cells downstream of cancer-relevant signaling pathways and thereby function as a nexus between signaling and early endocytic trafficking. I speculate that sustained up-regulation and/or acute activation of dynamin-1 in cancer cells contributes to a program of "adaptive" CME that alters signaling to enhance cancer cell survival, migration, and proliferation.
[Mh] Termos MeSH primário: Dinamina I/metabolismo
Endocitose
Neoplasias/metabolismo
Receptores de Superfície Celular/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Animais
Movimento Celular
Proliferação Celular
Vesículas Revestidas por Clatrina/metabolismo
Retroalimentação Fisiológica
Seres Humanos
Neoplasias/patologia
Transporte Proteico
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Receptors, Cell Surface); EC 3.5.1.50 (Dynamin I)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170705
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201705017


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[PMID]:28171750
[Au] Autor:Chen PH; Bendris N; Hsiao YJ; Reis CR; Mettlen M; Chen HY; Yu SL; Schmid SL
[Ad] Endereço:Department of Cell Biology, UT Southwestern Medical Center, Dallas, TX 75390, USA. Electronic address: ping-hung.chen@utsouthwestern.edu.
[Ti] Título:Crosstalk between CLCb/Dyn1-Mediated Adaptive Clathrin-Mediated Endocytosis and Epidermal Growth Factor Receptor Signaling Increases Metastasis.
[So] Source:Dev Cell;40(3):278-288.e5, 2017 Feb 06.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Signaling receptors are internalized and regulated by clathrin-mediated endocytosis (CME). Two clathrin light chain isoforms, CLCa and CLCb, are integral components of the endocytic machinery whose differential functions remain unknown. We report that CLCb is specifically upregulated in non-small-cell lung cancer (NSCLC) cells and is associated with poor patient prognosis. Engineered single CLCb-expressing NSCLC cells, as well as "switched" cells that predominantly express CLCb, exhibit increased rates of CME and altered clathrin-coated pit dynamics. This "adaptive CME" resulted from upregulation of dynamin-1 (Dyn1) and its activation through a positive feedback loop involving enhanced epidermal growth factor (EGF)-dependent Akt/GSK3ß phosphorylation. CLCb/Dyn1-dependent adaptive CME selectively altered EGF receptor trafficking, enhanced cell migration in vitro, and increased the metastatic efficiency of NSCLC cells in vivo. We define molecular mechanisms for adaptive CME in cancer cells and a role for the reciprocal crosstalk between signaling and CME in cancer progression.
[Mh] Termos MeSH primário: Carcinoma Pulmonar de Células não Pequenas/patologia
Cadeias Leves de Clatrina/metabolismo
Clatrina/metabolismo
Dinamina I/metabolismo
Endocitose
Neoplasias Pulmonares/patologia
Receptor do Fator de Crescimento Epidérmico/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Animais
Carcinoma Pulmonar de Células não Pequenas/genética
Linhagem Celular Tumoral
Movimento Celular
Invaginações Revestidas da Membrana Celular/metabolismo
Endossomos/metabolismo
Feminino
Regulação Neoplásica da Expressão Gênica
Glicogênio Sintase Quinase 3 beta/metabolismo
Seres Humanos
Neoplasias Pulmonares/genética
Camundongos Nus
Metástase Neoplásica
Fosforilação
Transporte Proteico
Proteínas Proto-Oncogênicas c-akt/metabolismo
Fatores de Risco
Transdução de Sinais
Análise de Sobrevida
Regulação para Cima/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (APPL1 protein, human); 0 (Adaptor Proteins, Signal Transducing); 0 (Clathrin); 0 (Clathrin Light Chains); EC 2.7.10.1 (Receptor, Epidermal Growth Factor); EC 2.7.11.1 (Glycogen Synthase Kinase 3 beta); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 3.5.1.50 (Dynamin I)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170208
[St] Status:MEDLINE


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[PMID]:27997171
[Au] Autor:Odell LR; Abdel-Hamid MK; Hill TA; Chau N; Young KA; Deane FM; Sakoff JA; Andersson S; Daniel JA; Robinson PJ; McCluskey A
[Ad] Endereço:Chemistry, School of Environmental and Life Sciences, The University of Newcastle , Callaghan, New South Wales 2308, Australia.
[Ti] Título:Pyrimidine-Based Inhibitors of Dynamin I GTPase Activity: Competitive Inhibition at the Pleckstrin Homology Domain.
[So] Source:J Med Chem;60(1):349-361, 2017 Jan 12.
[Is] ISSN:1520-4804
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The large GTPase dynamin mediates membrane fission during clathrin-mediated endocytosis (CME). The aminopyrimidine compounds were reported to disrupt dynamin localization to the plasma membrane via the PH domain and implicate this mechanism in the inhibition of CME. We have used a computational approach of binding site identification, docking, and interaction energy calculations to design and synthesize a new library of aminopyrimidine analogues targeting site-2 of the pleckstrin homology (PH) domain. The optimized analogues showed low micromolar inhibition against both dynamin I (IC = 10.6 ± 1.3 to 1.6 ± 0.3 µM) and CME (IC = 65.9 ± 7.7 to 3.7 ± 1.1 mM), which makes this series among the more potent inhibitors of dynamin and CME yet reported. In CME and growth inhibition cell-based assays, the data obtained was consistent with dynamin inhibition. CEREP ExpresS profiling identified off-target effects at the cholecystokinin, dopamine D , histamine H and H , melanocortin, melatonin, muscarinic M and M , neurokinin, opioid KOP and serotonin receptors.
[Mh] Termos MeSH primário: Dinamina I/antagonistas & inibidores
Inibidores Enzimáticos/farmacologia
Domínios de Homologia à Plecstrina/efeitos dos fármacos
Pirimidinas/farmacologia
[Mh] Termos MeSH secundário: Ligação Competitiva
Espectroscopia de Ressonância Magnética Nuclear de Carbono-13
Linhagem Celular Tumoral
Ensaios de Seleção de Medicamentos Antitumorais
Inibidores Enzimáticos/metabolismo
Seres Humanos
Espectrometria de Massas
Espectroscopia de Prótons por Ressonância Magnética
Pirimidinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Pyrimidines); EC 3.5.1.50 (Dynamin I); K8CXK5Q32L (pyrimidine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161221
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jmedchem.6b01422


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[PMID]:27974247
[Au] Autor:Chojnacka K; Bilinska B; Mruk DD
[Ad] Endereço:Center for Biomedical Research, Population Council, 1230 York Avenue, New York, NY, USA.
[Ti] Título:Annexin A2 is critical for blood-testis barrier integrity and spermatid disengagement in the mammalian testis.
[So] Source:Biochim Biophys Acta;1864(3):527-545, 2017 03.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Throughout spermatogenesis, two important processes occur at late stage VIII of the seminiferous epithelial cycle in the rat testis: preleptotene spermatocytes commence entry into the adluminal compartment and step 19 spermatids release from the seminiferous epithelium. Presently, it is not clear how these processes, which involve extensive restructuring of unique Sertoli-Sertoli and Sertoli-germ cell junctions, are mediated. We aimed to determine whether annexin A2 (ANXA2), a Ca -dependent and phospholipid-binding protein, participates in cell junction dynamics. To address this, in vitro and in vivo RNA interference studies were performed on prepubertal Sertoli cells and adult rat testes. The endpoints of Anxa2 knockdown were determined by immunoblotting, morphological analyses, fluorescent immunostaining, and barrier integrity assays. In the testis, ANXA2 localized to the Sertoli cell stalk, with specific staining at the blood-testis barrier and the concave (ventral) surface of elongated spermatids. ANXA2 also bound actin when testis lysates were used for immunoprecipitation. Anxa2 knockdown was found to disrupt the Sertoli cell/blood-testis barrier in vitro and in vivo. The disruption in barrier function was substantiated by changes in the localization of claudin-11, zona occludens-1, N-cadherin, and ß-catenin. Furthermore, Anxa2 knockdown resulted in spermiation defects caused by a dysfunction of tubulobulbar complexes, testis-specific actin-rich ultrastructures that internalize remnant cell junction components prior to spermiation. Additionally, there were changes in the localization of several tubulobulbar complex component proteins, including actin-related protein 3, cortactin, and dynamin I/II. Our results indicate that ANXA2 is critical for the integrity of the blood-testis barrier and the timely release of spermatids.
[Mh] Termos MeSH primário: Anexina A2/genética
Barreira Hematotesticular/metabolismo
Regulação da Expressão Gênica no Desenvolvimento
Células de Sertoli/metabolismo
Espermátides/metabolismo
Espermatogênese/genética
[Mh] Termos MeSH secundário: Proteína 3 Relacionada a Actina/genética
Proteína 3 Relacionada a Actina/metabolismo
Animais
Anexina A2/antagonistas & inibidores
Anexina A2/metabolismo
Barreira Hematotesticular/crescimento & desenvolvimento
Caderinas/genética
Caderinas/metabolismo
Claudinas/genética
Claudinas/metabolismo
Cortactina/genética
Cortactina/metabolismo
Dinamina I/genética
Dinamina I/metabolismo
Dinamina II/genética
Dinamina II/metabolismo
Junções Intercelulares/genética
Masculino
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/metabolismo
RNA Interferente Pequeno/genética
RNA Interferente Pequeno/metabolismo
Ratos
Ratos Sprague-Dawley
Epitélio Seminífero/citologia
Epitélio Seminífero/crescimento & desenvolvimento
Epitélio Seminífero/metabolismo
Células de Sertoli/citologia
Transdução de Sinais
Espermátides/crescimento & desenvolvimento
Espermátides/ultraestrutura
Espermatócitos/crescimento & desenvolvimento
Espermatócitos/metabolismo
Espermatócitos/ultraestrutura
Proteína da Zônula de Oclusão-1/genética
Proteína da Zônula de Oclusão-1/metabolismo
beta Catenina/genética
beta Catenina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actin-Related Protein 3); 0 (Annexin A2); 0 (Cadherins); 0 (Claudins); 0 (Cldn11 protein, rat); 0 (Cortactin); 0 (Ctnnb1 protein, rat); 0 (Cttn protein, rat); 0 (N-cadherin, rat); 0 (Nerve Tissue Proteins); 0 (RNA, Small Interfering); 0 (Tjp1 protein, rat); 0 (Zonula Occludens-1 Protein); 0 (beta Catenin); EC 3.5.1.50 (Dynamin I); EC 3.6.5.5 (Dynamin II)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161216
[St] Status:MEDLINE


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[PMID]:27755386
[Au] Autor:Koh-Tan HH; Dashti M; Wang T; Beattie W; Mcclure J; Young B; Dominiczak AF; McBride MW; Graham D
[Ad] Endereço:aInstitute of Cardiovascular & Medical Sciences, BHF Glasgow Cardiovascular Research Centre, University of Glasgow, Glasgow, UK bDepartment of Anatomical Pathology, Pathology North (Hunter), John Hunter Hospital, New Lambton, New South Wales, Australia.
[Ti] Título:Dissecting the genetic components of a quantitative trait locus for blood pressure and renal pathology on rat chromosome 3.
[So] Source:J Hypertens;35(2):319-329, 2017 Feb.
[Is] ISSN:1473-5598
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: We have previously confirmed the importance of rat chromosome 3 (RNO3) genetic loci on blood pressure elevation, pulse pressure (PP) variability and renal pathology during salt challenge in the stroke-prone spontaneously hypertensive (SHRSP) rat. The aims of this study were to generate a panel of RNO3 congenic sub-strains to genetically dissect the implicated loci and identify positional candidate genes by microarray expression profiling and analysis of next-generation sequencing data. METHOD AND RESULTS: A panel of congenic sub-strains were generated containing Wistar-Kyoto (WKY)-introgressed segments of varying size on the SHRSP genetic background, focused within the first 50 Mbp of RNO3. Haemodynamic profiling during salt challenge demonstrated significantly reduced systolic blood pressure, diastolic blood pressure and PP variability in SP.WKYGla3a, SP.WKYGla3c, SP.WKYGla3d and SP.WKYGla3e sub-strains. Only SBP and DBP were significantly reduced during salt challenge in SP.WKYGla3b and SP.WKYGla3f sub-strains, whereas SP.WKYGla3g rats did not differ in haemodynamic response to SHRSP. Those sub-strains demonstrating significantly reduced PP variability during salt challenge also demonstrated significantly reduced renal pathology and proteinuria. Microarray expression profiling prioritized two candidate genes for blood pressure regulation (Dnm1, Tor1b), localized within the common congenic interval shared by SP.WKYGla3d and SP.WKYGla3f strains, and one candidate gene for salt-induced PP variability and renal pathology (Rabgap1), located within the region unique to the SP.WKYGla3d strain. Comparison of next-generation sequencing data identified variants within additional positional genes that are likely to affect protein function. CONCLUSION: This study has identified distinct intervals on RNO3-containing genes that may be important for blood pressure regulation and renal pathology during salt challenge.
[Mh] Termos MeSH primário: Pressão Sanguínea/genética
Dinamina I/genética
Hipertensão/genética
Chaperonas Moleculares/genética
Locos de Características Quantitativas
[Mh] Termos MeSH secundário: Animais
Animais Congênicos
Mapeamento Cromossômico
Cromossomos de Mamíferos
Perfilação da Expressão Gênica
Sequenciamento de Nucleotídeos em Larga Escala
Hipertensão/patologia
Rim/metabolismo
Masculino
Análise de Sequência com Séries de Oligonucleotídeos
Ratos
Ratos Endogâmicos SHR
Ratos Endogâmicos WKY
Análise de Sequência de DNA
Cloreto de Sódio na Dieta/administração & dosagem
Acidente Vascular Cerebral/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Molecular Chaperones); 0 (Sodium Chloride, Dietary); 0 (Tor1b protein, rat); EC 3.5.1.50 (Dynamin I)
[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:161019
[St] Status:MEDLINE
[do] DOI:10.1097/HJH.0000000000001155


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[PMID]:27229184
[Au] Autor:Mahapatra S; Lou X
[Ad] Endereço:Department of Neuroscience, School of Medicine and Public Health, University of Wisconsin-Madison, Madison, WI, 53706, USA.
[Ti] Título:Dynamin-1 deletion enhances post-tetanic potentiation and quantal size after tetanic stimulation at the calyx of Held.
[So] Source:J Physiol;595(1):193-206, 2017 Jan 01.
[Is] ISSN:1469-7793
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:KEY POINTS: Post-tetanic potentiation (PTP) is attributed mainly to an increase in release probability (P ) and/or readily-releasable pool (RRP) in many synapses, but the role of endocytosis in PTP is unknown. Using the calyx of Held synapse from tissue-specific dynamin-1 knockout (cKO) mice (P16-20), we report that cKO synapses show enhanced PTP compared to control. We found significant increases in both spontaneous excitatory postsynaptic current (spEPSC) amplitude and RRP size (estimated by a train of 30 APs at 100 Hz) in cKO over control during PTP. Actin depolymerization blocks the increase in spEPSC amplitude in both control and cKO, and it abolishes the enhancement of PTP in cKO. PTP is sensitive to the PKC inhibitor GF109203X in both control and cKO. We conclude that an activity-dependent quantal size increase contributes to the enhancement of PTP in cKO over control and an altered endocytosis affects short-term plasticity through quantal size changes. ABSTRACT: High-frequency stimulation leads to post-tetanic potentiation (PTP) at many types of synapses. Previous studies suggest that PTP results primarily from a protein kinase C (PKC)-dependent increase in release probability (P ) and/or readily-releasable pool (RRP) of synaptic vesicles (SVs), but the role of SV endocytosis in PTP is unknown. Using the mature calyx of Held (P16-20), we report that tissue-specific ablation of dynamin-1 (cKO), an endocytic protein crucial for SV regeneration, enhances PTP in cKO over control. To explore the mechanism of this enhancement, we estimated the changes in paired-pulse ratios (PPRs) and RRP size during PTP. RRP was estimated by the back-extrapolation of cumulative EPSC amplitudes during a train of 30 action potentials at 100 Hz (termed RRP ). We found an increase in RRP during PTP in both control and cKO, but no significant changes in the PPR. Moreover, the amplitude and frequency of spontaneous excitatory postsynaptic currents (spEPSCs) increased during PTP in both control and cKO; however, the spEPSC amplitude in cKO during PTP was significantly larger than in control. Actin depolymerization reagent latrunculin-B (Lat-B) abolished the activity-dependent increase in spEPSC amplitude in both control and cKO, but selectively blocked the enhancement of PTP in cKO, without affecting PTP in control. PKC inhibitor GF109203X nearly abolished PTP in both control and cKO. These data suggest that the quantal size increase contributes to the enhancement of PTP in dynamin-1 cKO, and this change depends on strong synaptic activity and actin polymerization.
[Mh] Termos MeSH primário: Tronco Encefálico/fisiologia
Dinamina I/fisiologia
Sinapses/fisiologia
[Mh] Termos MeSH secundário: Animais
Dinamina I/genética
Estimulação Elétrica
Endocitose
Potenciais Pós-Sinápticos Excitadores
Camundongos Knockout
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.5.1.50 (Dynamin I)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160528
[St] Status:MEDLINE
[do] DOI:10.1113/JP271937


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[PMID]:27903237
[Au] Autor:Maekawa T; Sasaoka T; Azuma S; Ichikawa T; Melrose HL; Farrer MJ; Obata F
[Ad] Endereço:Department of Biochemistry, Graduate School of Medical Sciences, Kitasato University, 1-15-1 Kitasato, Minami-ku, Sagamihara, Kanagawa, 252-0373, Japan. maekawa@kitasato-u.ac.jp.
[Ti] Título:Leucine-rich repeat kinase 2 (LRRK2) regulates α-synuclein clearance in microglia.
[So] Source:BMC Neurosci;17(1):77, 2016 Nov 30.
[Is] ISSN:1471-2202
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: α-Synuclein (αSYN) has been genetically implicated in familial and sporadic Parkinson's disease (PD), and is associated with disease susceptibility, progression and pathology. Excess amounts of αSYN are toxic to neurons. In the brain, microglial αSYN clearance is closely related to neuronal survival. Leucine-rich repeat kinase 2 (LRRK2) is the one of the other genes implicated in familial and sporadic PD. While LRRK2 is known to be expressed in microglia, its true function remains to be elucidated. In this study, we investigated αSYN clearance by microglia isolated from LRRK2-knockout (KO) mice. RESULTS: In LRRK2-KO microglia, αSYN was taken up in larger amounts and cleared from the supernatant more effectively than for microglia isolated from wild-type (WT) mice. This higher clearance ability of LRRK2-KO microglia was thought to be due to an increase of Rab5-positive endosomes, but not Rab7- or Rab11-positive endosomes. Increased engagement between Rab5 and dynamin 1 was also observed in LRRK2-KO microglia. CONCLUSION: LRRK2 negatively regulates the clearance of αSYN accompanied by down-regulation of the endocytosis pathway. Our findings reveal a new functional role of LRRK2 in microglia and offer a new insight into the mechanism of PD pathogenesis.
[Mh] Termos MeSH primário: Serina-Treonina Proteína Quinase-2 com Repetições Ricas em Leucina/metabolismo
Microglia/metabolismo
alfa-Sinucleína/metabolismo
[Mh] Termos MeSH secundário: Animais
Western Blotting
Encéfalo/metabolismo
Encéfalo/patologia
Células Cultivadas
Dinamina I/metabolismo
Endocitose/fisiologia
Endossomos/metabolismo
Imunofluorescência
Serina-Treonina Proteína Quinase-2 com Repetições Ricas em Leucina/genética
Camundongos Endogâmicos C57BL
Camundongos Knockout
Microglia/patologia
Proteínas Recombinantes/metabolismo
Proteínas rab5 de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Proteins); 0 (Snca protein, mouse); 0 (alpha-Synuclein); EC 2.7.11.1 (Leucine-Rich Repeat Serine-Threonine Protein Kinase-2); EC 2.7.11.1 (Lrrk2 protein, mouse); EC 3.5.1.50 (Dynamin I); EC 3.6.5.2 (rab5 GTP-Binding Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170821
[Lr] Data última revisão:
170821
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161202
[St] Status:MEDLINE


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[PMID]:27806796
[Au] Autor:Deng XL; Yin F; Zhang CL; Ma YP; He F; Wu LW; Peng J
[Ad] Endereço:Department of Pediatrics, Xiangya Hospital of Central South University, Hunan Intellectual and Developmental Disabilities Research Center, Changsha 410008, China.
[Ti] Título:[Dynamin-1-related infantile spasms: a case report and review of literature].
[So] Source:Zhonghua Er Ke Za Zhi;54(11):856-859, 2016 Nov 02.
[Is] ISSN:0578-1310
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:To analyze the clinical and gene mutation characteristics of dynamin-1 (DNM1)-related infantile spasms. Clinical, laboratory and genetic data of one case of DNM1-related infantile spasms diagnosed by Xiangya Hospital in September 2015 were analyzed.Through taking "Dynamin-1" "DNM1" as key words to search at CNKI, Wanfang, PubMed and OMIM to date (April 2016), the clinical characteristics of 9 reported cases of DNM1-related epileptic encephalopathy in international literature with our case were reviewed. The boy is the second child of healthy and nonconsanguineous parents.At 7 months, he started to have seizures with head dropping, and he was brought for the first time to our hospital at the age of 17 months.The patient presented with severe psychomotor retardation, epilepsy, muscular hypotonia, and electroencephalography showed hypsarhythmia.He received 28 days of adrenocorticotropic hormone (ACTH) therapy.After that, his seizures were improved with valproic acid and levetiracetam, and disappeared between 3 years and 5 months to 5 years and 5 months of age on treatment with valproic acid only.Exome-sequencing study (trios) identified novel heterozygous mutation c. 443A>G (p.Glu148Arg) in DNM1. Up to now, 9 cases of epileptic encephalopathy (infantile spasms or Lennox-Gastaut syndrome) associated with de novo DNM1 gene mutations have been reported. The main clinical features of DNM1 mutations include intractable seizures, intellectual disability, developmental delay, hypotonia, and developmental delay before the onset of seizures.
[Mh] Termos MeSH primário: Dinamina I/genética
Espasmos Infantis/genética
[Mh] Termos MeSH secundário: Criança
Pré-Escolar
Deficiências do Desenvolvimento
Eletroencefalografia
Epilepsia
Feminino
Seres Humanos
Lactente
Síndrome de Lennox Gastaut
Masculino
Mutação
Convulsões
Ácido Valproico
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
614OI1Z5WI (Valproic Acid); EC 3.5.1.50 (Dynamin I)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161104
[St] Status:MEDLINE
[do] DOI:10.3760/cma.j.issn.0578-1310.2016.11.014


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[PMID]:27788222
[Au] Autor:Tham DK; Joshi B; Moukhles H
[Ad] Endereço:Department of Cellular and Physiological Sciences, University of British Columbia, Vancouver, British Columbia, Canada.
[Ti] Título:Aquaporin-4 Cell-Surface Expression and Turnover Are Regulated by Dystroglycan, Dynamin, and the Extracellular Matrix in Astrocytes.
[So] Source:PLoS One;11(10):e0165439, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The water-permeable channel aquaporin-4 (AQP4) is highly expressed in perivascular astrocytes of the mammalian brain and represents the major conduit for water across the blood-brain barrier. Within these cells, AQP4 is found in great quantities at perivascular endfoot sites but is detected in lesser amounts at the membrane domains within the brain parenchyma. We had previously established that this polarization was regulated by the interaction between dystroglycan (DG), an extracellular matrix receptor that is co-expressed with AQP4, and the laminin that is contained within the perivascular basal lamina. In the present study, we have attempted to describe the mechanisms that underlie this regulation, using primary astrocyte cultures. Via biotinylation, we found that the cell-surface expression of AQP4 is DG-dependent and is potentiated by laminin. We also determined that this laminin-dependent increase occurs not through an upregulation of total AQP4 levels, but rather from a redirection of AQP4 from an intracellular, EEA-1-associated pool to the cell surface. We then demonstrated an association between DG and dynamin and showed that dynamin functioned in conjunction with clathrin to regulate surface AQP4 amounts. Furthermore, we observed that DG preferentially binds to the inactive forms of dynamin, suggesting that this interaction was inhibitory for AQP4 endocytosis. Finally, we showed that laminin selectively upregulates the cell-surface expression of the M23 isoform of AQP4. Our data therefore indicate that the dual interation of DG with laminin and dynamin is involved in the regulation of AQP4 internalization, leading to its asymmetric enrichment at perivascular astrocyte endfeet.
[Mh] Termos MeSH primário: Aquaporina 4/metabolismo
Astrócitos/citologia
Dinamina I/metabolismo
Distroglicanas/metabolismo
Matriz Extracelular/metabolismo
Regulação da Expressão Gênica
[Mh] Termos MeSH secundário: Animais
Caveolina 1/metabolismo
Membrana Celular/efeitos dos fármacos
Membrana Celular/metabolismo
Clatrina/metabolismo
Cães
Endocitose/efeitos dos fármacos
Endossomos/efeitos dos fármacos
Endossomos/metabolismo
Matriz Extracelular/efeitos dos fármacos
Regulação da Expressão Gênica/efeitos dos fármacos
Guanosina Trifosfato/metabolismo
Seres Humanos
Laminina/metabolismo
Células Madin Darby de Rim Canino
Isoformas de Proteínas/metabolismo
Transporte Proteico/efeitos dos fármacos
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aquaporin 4); 0 (Caveolin 1); 0 (Clathrin); 0 (Laminin); 0 (Protein Isoforms); 146888-27-9 (Dystroglycans); 86-01-1 (Guanosine Triphosphate); EC 3.5.1.50 (Dynamin I)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170623
[Lr] Data última revisão:
170623
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161028
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0165439


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[PMID]:27748822
[Au] Autor:Yoo DY; Jung HY; Kim JW; Yim HS; Kim DW; Nam H; Suh JG; Choi JH; Won MH; Yoon YS; Hwang IK
[Ad] Endereço:Department of Anatomy and Cell Biology, College of Veterinary Medicine and Research Institute for Veterinary Science, Seoul National University, Seoul 08826, Republic of Korea.
[Ti] Título:Reduction of dynamin 1 in the hippocampus of aged mice is associated with the decline in hippocampal­dependent memory.
[So] Source:Mol Med Rep;14(5):4755-4760, 2016 Nov.
[Is] ISSN:1791-3004
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Dynamin 1 is a known synaptic protein, which has is key in the presynaptic regulation of endocytosis. The present study investigated the association between age and the observed changes in Morris water maze performance, and immunoreactivity and protein levels of dynamin 1 in the mouse hippocampal formation. In addition, the effects of dynasore, an inhibitor of dynamin 1, on the hippocampal dependent memory were determined to elucidate the correlation between dynamin 1 and memory. In the training phase of the Morris water maze task, the mean escape latency of the aged group (24 months old) was significantly longer, compared with that of the adult group (4 months old), although the average swimming speed and the total distance traveled during the probe trial were similar in the two groups. In the aged group, the time spent locating the target platform was significantly longer and the time spent in the correct quadrant was significantly shorter, compared with those in the adult group. In the adult group, a moderate level of dynamin 1 was detected in the hippocampal CA1 and CA3 regions, and in the dentate gyrus. In the aged group, the immunoreactivity of dynamin 1 was almost eliminated in the CA3 region and the dentate gyrus. In addition, the protein levels of dynamin 1 in the brain were significantly lower in the aged group, compared with those in the adult group. The direct infusion of dynasore, significantly reduced the contextual memory, compared with that of animals in the vehicle­treated group. These results suggested that dynamin 1 was susceptible to the aging process, and that a reduction in dynamin 1 may result in hippocampal­dependent memory deficits by disrupting endocytosis and the release of neurotransmitters.
[Mh] Termos MeSH primário: Dinamina I/metabolismo
Hipocampo/metabolismo
Hipocampo/fisiopatologia
Memória
[Mh] Termos MeSH secundário: Envelhecimento
Animais
Modelos Animais de Doenças
Dinamina I/genética
Expressão Gênica
Imuno-Histoquímica
Masculino
Aprendizagem em Labirinto
Transtornos da Memória/genética
Transtornos da Memória/metabolismo
Camundongos
Memória Espacial
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.5.1.50 (Dynamin I)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170406
[Lr] Data última revisão:
170406
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE
[do] DOI:10.3892/mmr.2016.5804



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