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[PMID]:29281629
[Au] Autor:Ojeda Naharros I; Gesemann M; Mateos JM; Barmettler G; Forbes A; Ziegler U; Neuhauss SCF; Bachmann-Gagescu R
[Ad] Endereço:Institute of Molecular Life Sciences, University of Zurich, Zurich, Switzerland.
[Ti] Título:Loss-of-function of the ciliopathy protein Cc2d2a disorganizes the vesicle fusion machinery at the periciliary membrane and indirectly affects Rab8-trafficking in zebrafish photoreceptors.
[So] Source:PLoS Genet;13(12):e1007150, 2017 12.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ciliopathies are human disorders caused by dysfunction of primary cilia, ubiquitous organelles involved in transduction of environmental signals such as light sensation in photoreceptors. Concentration of signal detection proteins such as opsins in the ciliary membrane is achieved by RabGTPase-regulated polarized vesicle trafficking and by a selective barrier at the ciliary base, the transition zone (TZ). Dysfunction of the TZ protein CC2D2A causes Joubert/Meckel syndromes in humans and loss of ciliary protein localization in animal models, including opsins in retinal photoreceptors. The link between the TZ and upstream vesicle trafficking has been little explored to date. Moreover, the role of the small GTPase Rab8 in opsin-carrier vesicle (OCV) trafficking has been recently questioned in a mouse model. Using correlative light and electron microscopy and live imaging in zebrafish photoreceptors, we provide the first live characterization of Rab8-mediated trafficking in photoreceptors in vivo. Our results support a possibly redundant role for both Rab8a/b paralogs in OCV trafficking, based on co-localization of Rab8 and opsins in vesicular structures, and joint movement of Rab8-tagged particles with opsin. We further investigate the role of the TZ protein Cc2d2a in Rab8-mediated trafficking using cc2d2a zebrafish mutants and identify a requirement for Cc2d2a in the latest step of OCV trafficking, namely vesicle fusion. Progressive accumulation of opsin-containing vesicles in the apical portion of photoreceptors lacking Cc2d2a is caused by disorganization of the vesicle fusion machinery at the periciliary membrane with mislocalization and loss of the t-SNAREs SNAP25 and Syntaxin3 and of the exocyst component Exoc4. We further observe secondary defects on upstream Rab8-trafficking with cytoplasmic accumulation of Rab8. Taken together, our results support participation of Rab8 in OCV trafficking and identify a novel role for the TZ protein Cc2d2a in fusion of incoming ciliary-directed vesicles, through organization of the vesicle fusion machinery at the periciliary membrane.
[Mh] Termos MeSH primário: Proteínas de Transporte Vesicular/genética
Proteínas de Transporte Vesicular/metabolismo
Proteínas de Peixe-Zebra/genética
Proteínas de Peixe-Zebra/metabolismo
Proteínas rab de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Transporte Biológico
Movimento Celular
Cílios/genética
Cílios/metabolismo
Seres Humanos
Membranas/metabolismo
Opsinas/genética
Opsinas/metabolismo
Células Fotorreceptoras de Vertebrados/metabolismo
Transporte Proteico
Peixe-Zebra
Proteínas rab de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CC2D2A protein, zebrafish); 0 (Opsins); 0 (Vesicular Transport Proteins); 0 (Zebrafish Proteins); EC 3.6.1.- (Rab8a protein, zebrafish); EC 3.6.1.-. (RAB8A protein, human); EC 3.6.5.2 (rab GTP-Binding Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171228
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007150


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[PMID]:29233870
[Au] Autor:Zachari M; Ganley IG
[Ad] Endereço:MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, U.K.
[Ti] Título:The mammalian ULK1 complex and autophagy initiation.
[So] Source:Essays Biochem;61(6):585-596, 2017 12 12.
[Is] ISSN:1744-1358
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Autophagy is a vital lysosomal degradation pathway that serves as a quality control mechanism. It rids the cell of damaged, toxic or excess cellular components, which if left to persist could be detrimental to the cell. It also serves as a recycling pathway to maintain protein synthesis under starvation conditions. A key initial event in autophagy is formation of the autophagosome, a unique double-membrane organelle that engulfs the cytosolic cargo destined for degradation. This step is mediated by the serine/threonine protein kinase ULK1 (unc-51-like kinase 1), which functions in a complex with at least three protein partners: FIP200 (focal adhesion kinase family interacting protein of 200 kDa), ATG (autophagy-related protein) 13 (ATG13), and ATG101. In this artcile, we focus on the regulation of the ULK1 complex during autophagy initiation. The complex pattern of upstream pathways that converge on ULK1 suggests that this complex acts as a node, converting multiple signals into autophagosome formation. Here, we review our current understanding of this regulation and in turn discuss what happens downstream, once the ULK1 complex becomes activated.
[Mh] Termos MeSH primário: Proteína Homóloga à Proteína-1 Relacionada à Autofagia/metabolismo
Proteínas Relacionadas à Autofagia/metabolismo
Autofagia/fisiologia
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/genética
Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Animais
Autofagia/genética
Proteína Homóloga à Proteína-1 Relacionada à Autofagia/genética
Proteínas Relacionadas à Autofagia/genética
Seres Humanos
Proteínas Tirosina Quinases/genética
Proteínas Tirosina Quinases/metabolismo
Proteínas de Transporte Vesicular/genética
Proteínas de Transporte Vesicular/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Autophagy-Related Proteins); 0 (Vesicular Transport Proteins); EC 2.7.10.1 (Protein-Tyrosine Kinases); EC 2.7.11.1 (Autophagy-Related Protein-1 Homolog)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE
[do] DOI:10.1042/EBC20170021


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[PMID]:29300766
[Au] Autor:Wu Y; Guo XP; Kanemoto S; Maeoka Y; Saito A; Asada R; Matsuhisa K; Ohtake Y; Imaizumi K; Kaneko M
[Ad] Endereço:Department of Biochemistry, Institute of Biomedical and Health Sciences, Hiroshima University, Hiroshima, Japan.
[Ti] Título:Sec16A, a key protein in COPII vesicle formation, regulates the stability and localization of the novel ubiquitin ligase RNF183.
[So] Source:PLoS One;13(1):e0190407, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We identified 37 ubiquitin ligases containing RING-finger and transmembrane domains. Of these, we found that RNF183 is abundantly expressed in the kidney. RNF183 predominantly localizes to the endoplasmic reticulum (ER), Golgi, and lysosome. We identified Sec16A, which is involved in coat protein complex II vesicle formation, as an RNF183-interacting protein. RNF183 colocalized with Sec16A and interacted through the central conserved domain (CCD) of Sec16A. Although Sec16A is not a substrate for RNF183, RNF183 was more rapidly degraded by the ER-associated degradation (ERAD) in the absence of Sec16A. Sec16A also stabilized the interacting ubiquitin ligase RNF152, which localizes to the lysosome and has structural similarity with RNF183. These results suggest that Sec16A appears to regulate the protein stability and localization of lysosomal ubiquitin ligases.
[Mh] Termos MeSH primário: Vesículas Revestidas pelo Complexo de Proteína do Envoltório/metabolismo
Ubiquitina-Proteína Ligases/metabolismo
Proteínas de Transporte Vesicular/fisiologia
[Mh] Termos MeSH secundário: Retículo Endoplasmático/metabolismo
Complexo de Golgi/metabolismo
Seres Humanos
Lisossomos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (SEC16A protein, human); 0 (Vesicular Transport Proteins); EC 2.3.2.27 (RNF183 protein, human); EC 2.3.2.27 (Ubiquitin-Protein Ligases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180105
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190407


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[PMID]:28454729
[Au] Autor:Sato E; Zhang LJ; Dorschner RA; Adase CA; Choudhury BP; Gallo RL
[Ad] Endereço:Department of Dermatology, University of California-San Diego, La Jolla, California, USA.
[Ti] Título:Activation of Parathyroid Hormone 2 Receptor Induces Decorin Expression and Promotes Wound Repair.
[So] Source:J Invest Dermatol;137(8):1774-1783, 2017 Aug.
[Is] ISSN:1523-1747
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this study, we report that TIP39, a parathyroid hormone ligand family member that was recently identified to be expressed in the skin, can induce decorin expression and enhance wound repair. Topical treatment of mice with TIP39 accelerated wound repair, whereas TIP39-deficient mice had delayed repair that was associated with formation of abnormal collagen bundles. To study the potential mechanism responsible for the action of TIP39 in the dermis, fibroblasts were cultured in three-dimensional collagen gels, a process that results in enhanced decorin expression unless activated to differentiate to adipocytes, whereupon these cells reduce expression of several proteoglycans, including decorin. Small interfering RNA-mediated silencing of parathyroid hormone 2 receptor (PTH2R), the receptor for TIP39, suppressed the expression of extracellular matrix-related genes, including decorin, collagens, fibronectin, and matrix metalloproteases. Skin wounds in TIP39 mice had decreased decorin expression, and addition of TIP39 to cultured fibroblasts induced decorin and increased phosphorylation and nuclear translocation of CREB. Fibroblasts differentiated to adipocytes and treated with TIP39 also showed increased decorin and production of chondroitin sulfate. Furthermore, the skin of PTH2R mice showed abnormal extracellular matrix structure, decreased decorin expression, and skin hardness. Thus, the TIP39-PTH2R system appears to be a previously unrecognized mechanism for regulation of extracellular matrix formation and wound repair.
[Mh] Termos MeSH primário: Decorina/genética
Regulação da Expressão Gênica
Proteínas Nucleares/farmacologia
RNA/genética
Receptor Tipo 2 de Hormônio Paratireóideo/genética
Proteínas de Transporte Vesicular/farmacologia
Cicatrização/fisiologia
Ferimentos e Lesões/genética
[Mh] Termos MeSH secundário: Animais
Diferenciação Celular
Células Cultivadas
Decorina/biossíntese
Modelos Animais de Doenças
Feminino
Immunoblotting
Camundongos
Camundongos Endogâmicos C57BL
Reação em Cadeia da Polimerase em Tempo Real
Receptor Tipo 2 de Hormônio Paratireóideo/biossíntese
Transdução de Sinais
Pele/lesões
Pele/metabolismo
Pele/patologia
Cicatrização/efeitos dos fármacos
Ferimentos e Lesões/metabolismo
Ferimentos e Lesões/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Decorin); 0 (Nuclear Proteins); 0 (Receptor, Parathyroid Hormone, Type 2); 0 (Tfip11 protein, mouse); 0 (Vesicular Transport Proteins); 63231-63-0 (RNA)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE


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[PMID]:29326040
[Au] Autor:Noh MR; Jang HS; Song DK; Lee SR; Lipschutz JH; Park KM; Kim JI
[Ad] Endereço:Department of Anatomy and BK21 Plus, Kyungpook National University School of Medicine, Daegu, Republic of Korea.
[Ti] Título:Downregulation of exocyst Sec10 accelerates kidney tubule cell recovery through enhanced cell migration.
[So] Source:Biochem Biophys Res Commun;496(2):309-315, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Migration of surviving kidney tubule cells after sub-lethal injury, for example ischemia/reperfusion (I/R), plays a critical role in recovery. Exocytosis is known to be involved in cell migration, and a key component in exocytosis is the highly-conserved eight-protein exocyst complex. We investigated the expression of a central exocyst complex member, Sec10, in kidneys following I/R injury, as well as the role of Sec10 in wound healing following scratch injury of cultured Madin-Darby canine kidney (MDCK) cells. Sec10 overexpression and knockdown (KD) in MDCK cells were used to investigate the speed of wound healing and the mechanisms underlying recovery. In mice, Sec10 decreased after I/R injury, and increased during the recovery period. In cell culture, Sec10 OE inhibited ruffle formation and wound healing, while Sec10 KD accelerated it. Sec10 OE cells had higher amounts of diacylglycerol kinase (DGK) gamma at the leading edge than did control cells. A DGK inhibitor reversed the inhibition of wound healing and ruffle formation in Sec10 OE cells. Conclusively, downregulation of Sec10 following I/R injury appears to accelerate recovery of kidney tubule cells through activated ruffle formation and enhanced cell migration.
[Mh] Termos MeSH primário: Diacilglicerol Quinase/antagonistas & inibidores
Túbulos Renais/metabolismo
Traumatismo por Reperfusão/prevenção & controle
Proteínas de Transporte Vesicular/genética
[Mh] Termos MeSH secundário: Animais
Bioensaio
Linhagem Celular
Movimento Celular/efeitos dos fármacos
Diacilglicerol Quinase/genética
Diacilglicerol Quinase/metabolismo
Cães
Inibidores Enzimáticos/farmacologia
Exocitose
Regulação da Expressão Gênica
Túbulos Renais/patologia
Células Madin Darby de Rim Canino
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Piperidinas/farmacologia
Quinazolinonas/farmacologia
RNA Interferente Pequeno/genética
RNA Interferente Pequeno/metabolismo
Traumatismo por Reperfusão/genética
Traumatismo por Reperfusão/metabolismo
Traumatismo por Reperfusão/patologia
Proteínas de Transporte Vesicular/agonistas
Proteínas de Transporte Vesicular/antagonistas & inibidores
Proteínas de Transporte Vesicular/metabolismo
Cicatrização/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (EXOC5 protein, mouse); 0 (Enzyme Inhibitors); 0 (Piperidines); 0 (Quinazolinones); 0 (RNA, Small Interfering); 0 (Vesicular Transport Proteins); 120166-69-0 (R 59949); EC 2.7.1.107 (Diacylglycerol Kinase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180113
[St] Status:MEDLINE


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[PMID]:29277369
[Au] Autor:Reddy SS; Shruthi K; Prabhakar YK; Sailaja G; Reddy GB
[Ad] Endereço:Biochemistry Division, National Institute of Nutrition, Hyderabad, India.
[Ti] Título:Implication of altered ubiquitin-proteasome system and ER stress in the muscle atrophy of diabetic rats.
[So] Source:Arch Biochem Biophys;639:16-25, 2018 02 01.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Skeletal muscle is adversely affected in type-1 diabetes, and excessively stimulated ubiquitin-proteasome system (UPS) was found to be a leading cause of muscle wasting or atrophy. The role of endoplasmic reticulum (ER) stress in muscle atrophy of type-1 diabetes is not known. Hence, we investigated the role of UPS and ER stress in the muscle atrophy of chronic diabetes rat model. METHODS: Diabetes was induced with streptozotocin (STZ) in male Sprague-Dawley rats and were sacrificed 2- and 4-months thereafter to collect gastrocnemius muscle. In another experiment, 2-months post-STZ-injection diabetic rats were treated with MG132, a proteasome inhibitor, for the next 2-months and gastrocnemius muscle was collected. RESULTS: The muscle fiber cross-sectional area was diminished in diabetic rats. The expression of UPS components: E1, MURF1, TRIM72, UCHL1, UCHL5, ubiquitinated proteins, and proteasome activity were elevated in the diabetic rats indicating activated UPS. Altered expression of ER-associated degradation (ERAD) components and increased ER stress markers were detected in 4-months diabetic rats. Proteasome inhibition by MG132 alleviated alterations in the UPS and ER stress in diabetic rat muscle. CONCLUSION: Increased UPS activity and ER stress were implicated in the muscle atrophy of diabetic rats and proteasome inhibition exhibited beneficiary outcome.
[Mh] Termos MeSH primário: Diabetes Mellitus Experimental/metabolismo
Estresse do Retículo Endoplasmático
Músculo Esquelético/metabolismo
Atrofia Muscular/metabolismo
Complexo de Endopeptidases do Proteassoma/metabolismo
Ubiquitina/metabolismo
[Mh] Termos MeSH secundário: Animais
Diabetes Mellitus Experimental/tratamento farmacológico
Diabetes Mellitus Experimental/patologia
Leupeptinas/farmacologia
Masculino
Proteínas Musculares/metabolismo
Músculo Esquelético/patologia
Atrofia Muscular/induzido quimicamente
Atrofia Muscular/tratamento farmacológico
Atrofia Muscular/patologia
Inibidores de Proteassoma/farmacologia
Ratos
Ratos Sprague-Dawley
Proteínas com Motivo Tripartido/metabolismo
Ubiquitina Tiolesterase/metabolismo
Ubiquitina-Proteína Ligases/metabolismo
Proteínas Ubiquitinadas/metabolismo
Proteínas de Transporte Vesicular/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Leupeptins); 0 (MG53 protein, rat); 0 (Muscle Proteins); 0 (Proteasome Inhibitors); 0 (Tripartite Motif Proteins); 0 (Ubiquitin); 0 (Ubiquitinated Proteins); 0 (Vesicular Transport Proteins); EC 2.3.2.27 (Trim63 protein, rat); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 3.4.19.12 (UCHL1 protein, rat); EC 3.4.19.12 (Ubiquitin Thiolesterase); EC 3.4.25.1 (Proteasome Endopeptidase Complex); RF1P63GW3K (benzyloxycarbonylleucyl-leucyl-leucine aldehyde)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171227
[St] Status:MEDLINE


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[PMID]:25815565
[Au] Autor:Saligan LN; Lukkahatai N; Holder G; Walitt B; Machado-Vieira R
[Ad] Endereço:a National Institute of Nursing Research, National Institutes of Health , Bethesda , MD , USA.
[Ti] Título:Lower brain-derived neurotrophic factor levels associated with worsening fatigue in prostate cancer patients during repeated stress from radiation therapy.
[So] Source:World J Biol Psychiatry;17(8):608-614, 2016 12.
[Is] ISSN:1814-1412
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVES: Fatigue during cancer treatment is associated with depression. Neurotrophic factors play a major role in depression and stress and might provide insight into mechanisms of fatigue. This study investigated the association between plasma concentrations of three neurotrophic factors (BDNF, brain-derived neurotrophic factor; GDNF, glial-derived neurotrophic factor; and SNAPIN, soluble N-ethylmaleimide sensitive fusion attachment receptor-associated protein) and initial fatigue intensification during external beam radiation therapy (EBRT) in euthymic non-metastatic prostate cancer men. METHODS: Fatigue, as measured by the 13-item Functional Assessment of Cancer Therapy-Fatigue (FACT-F), and plasma neurotrophic factors were collected at baseline (prior to EBRT) and mid-EBRT. Subjects were categorized into fatigue and no fatigue groups using a > 3-point change in FACT-F scores between the two time points. Multiple linear regressions analysed the associations between fatigue and neurotrophic factors. RESULTS: FACT-F scores of 47 subjects decreased from baseline (43.95 ± 1.3) to mid-EBRT (38.36 ± 1.5, P < 0.001), indicating worsening fatigue. SNAPIN levels were associated with fatigue scores (r = 0.43, P = 0.005) at baseline. A significant decrease of BDNF concentration (P = 0.008) was found in fatigued subjects during EBRT (n = 39). CONCLUSIONS: Baseline SNAPIN and decreasing BDNF levels may influence worsening fatigue during EBRT. Further investigations are warranted to confirm their role in the pathophysiology and therapeutics of fatigue.
[Mh] Termos MeSH primário: Fator Neurotrófico Derivado do Encéfalo/sangue
Fadiga/etiologia
Neoplasias da Próstata/sangue
Neoplasias da Próstata/radioterapia
Radioterapia/efeitos adversos
[Mh] Termos MeSH secundário: Idoso
Idoso de 80 Anos ou mais
Depressão/etiologia
Fator Neurotrófico Derivado de Linhagem de Célula Glial/sangue
Seres Humanos
Modelos Lineares
Masculino
Meia-Idade
Índice de Gravidade de Doença
Estados Unidos
Proteínas de Transporte Vesicular/sangue
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., INTRAMURAL
[Nm] Nome de substância:
0 (Brain-Derived Neurotrophic Factor); 0 (GDNF protein, human); 0 (Glial Cell Line-Derived Neurotrophic Factor); 0 (SNAPIN protein, human); 0 (Vesicular Transport Proteins); 0 (brain-derived neurotrophic factor, human)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180123
[Lr] Data última revisão:
180123
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150328
[St] Status:MEDLINE


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[PMID]:29227074
[Au] Autor:Minchenko OH; Tsymbal DO; Minchenko DO; Riabovol OO; Ratushna OO; Karbovskyi LL
[Ti] Título:Hypoxic regulation of the expression of cell proliferation related genes in U87 glioma cells upon inhibition of ire1 signaling enzyme
[So] Source:Ukr Biochem J;88(1):11-21, 2016 Ja-Feb.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:We have studied the effect of inhibition of IRE1 (inositol requiring enzyme 1), which is a central mediator of endoplasmic reticulum stress and a controller of cell proliferation and tumor growth, on hypoxic regulation of the expression of different proliferation related genes in U87 glioma cells. It was shown that hypoxia leads to up-regulation of the expression of IL13RA2, CD24, ING1, ING2, ENDOG, and POLG genes and to down-regulation ­ of KRT18, TRAPPC3, TSFM, and MTIF2 genes at the mRNA level in control glioma cells. Changes for ING1 and CD24 genes were more significant. At the same time, inhibition of IRE1 modifies the effect of hypoxia on the expression of all studied genes. In particular, it increases sensitivity to hypoxia of the expression of IL13RA2, TRAPPC3, ENDOG, and PLOG genes and suppresses the effect of hypoxia on the expression of ING1 gene. Additionally, it eliminates hypoxic regulation of KRT18, CD24, ING2, TSFM, and MTIF2 genes expressions and introduces sensitivity to hypoxia of the expression of BET1 gene in glioma cells. The present study demonstrates that hypoxia, which often contributes to tumor growth, affects the expression of almost all studied genes. Additionally, inhibition of IRE1 can both enhance and suppress the hypoxic regulation of these gene expressions in a gene specific manner and thus possibly contributes to slower glioma growth, but several aspects of this regulation must be further clarified.
[Mh] Termos MeSH primário: Estresse do Retículo Endoplasmático/genética
Endorribonucleases/genética
Regulação Neoplásica da Expressão Gênica
Neuroglia/metabolismo
Proteínas Serina-Treonina Quinases/genética
RNA Mensageiro/genética
Transdução de Sinais/genética
[Mh] Termos MeSH secundário: Antígeno CD24/genética
Antígeno CD24/metabolismo
Hipóxia Celular
Linhagem Celular Tumoral
Proliferação Celular
DNA Polimerase gama/genética
DNA Polimerase gama/metabolismo
Endodesoxirribonucleases/genética
Endodesoxirribonucleases/metabolismo
Endorribonucleases/antagonistas & inibidores
Endorribonucleases/metabolismo
Fatores de Iniciação em Eucariotos/genética
Fatores de Iniciação em Eucariotos/metabolismo
Proteínas de Homeodomínio/genética
Proteínas de Homeodomínio/metabolismo
Seres Humanos
Proteína 1 Inibidora do Crescimento/genética
Proteína 1 Inibidora do Crescimento/metabolismo
Subunidade alfa2 de Receptor de Interleucina-13/genética
Subunidade alfa2 de Receptor de Interleucina-13/metabolismo
Queratina-18/genética
Queratina-18/metabolismo
Proteínas Mitocondriais/genética
Proteínas Mitocondriais/metabolismo
Neuroglia/patologia
Fatores de Alongamento de Peptídeos/genética
Fatores de Alongamento de Peptídeos/metabolismo
Proteínas Serina-Treonina Quinases/antagonistas & inibidores
Proteínas Serina-Treonina Quinases/metabolismo
Proteínas Qc-SNARE/genética
Proteínas Qc-SNARE/metabolismo
RNA Mensageiro/metabolismo
Receptores Citoplasmáticos e Nucleares/genética
Receptores Citoplasmáticos e Nucleares/metabolismo
Proteínas Supressoras de Tumor/genética
Proteínas Supressoras de Tumor/metabolismo
Proteínas de Transporte Vesicular/genética
Proteínas de Transporte Vesicular/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BET1L protein, human); 0 (CD24 Antigen); 0 (Eukaryotic Initiation Factors); 0 (Homeodomain Proteins); 0 (ING1 protein, human); 0 (ING2 protein, human); 0 (Inhibitor of Growth Protein 1); 0 (Interleukin-13 Receptor alpha2 Subunit); 0 (KRT18 protein, human); 0 (Keratin-18); 0 (MTIF2 protein, human); 0 (Mitochondrial Proteins); 0 (Peptide Elongation Factors); 0 (Qc-SNARE Proteins); 0 (RNA, Messenger); 0 (Receptors, Cytoplasmic and Nuclear); 0 (TRAPPC3 protein, human); 0 (TSFM protein, human); 0 (Tumor Suppressor Proteins); 0 (Vesicular Transport Proteins); EC 2.7.11.1 (ERN1 protein, human); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.7.7 (DNA Polymerase gamma); EC 2.7.7.7 (POLG protein, human); EC 3.1.- (Endodeoxyribonucleases); EC 3.1.- (Endoribonucleases); EC 3.1.21.- (endonuclease G)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171212
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.01.011


  9 / 7079 MEDLINE  
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[PMID]:29195077
[Au] Autor:Langridge PD; Struhl G
[Ad] Endereço:Department of Genetics and Development, Columbia University, New York, NY, USA; Mortimer B. Zuckerman Mind Brain Behavior Institute, New York, NY, USA. Electronic address: pl2266@columbia.edu.
[Ti] Título:Epsin-Dependent Ligand Endocytosis Activates Notch by Force.
[So] Source:Cell;171(6):1383-1396.e12, 2017 Nov 30.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:DSL ligands activate Notch by inducing proteolytic cleavage of the receptor ectodomain, an event that requires ligand to be endocytosed in signal-sending cells by the adaptor protein Epsin. Two classes of explanation for this unusual requirement are (1) recycling models, in which the ligand must be endocytosed to be modified or repositioned before it binds Notch and (2) pulling models, in which the ligand must be endocytosed after it binds Notch to exert force that exposes an otherwise buried site for cleavage. We demonstrate in vivo that ligands that cannot enter the Epsin pathway nevertheless bind Notch but fail to activate the receptor because they cannot exert sufficient force. This argues against recycling models and in favor of pulling models. Our results also suggest that once ligand binds receptor, activation depends on a competition between Epsin-mediated ligand endocytosis, which induces cleavage, and transendocytosis of the ligand by the receptor, which aborts the incipient signal.
[Mh] Termos MeSH primário: Proteínas de Drosophila/metabolismo
Drosophila/citologia
Drosophila/metabolismo
Endocitose
Transdução de Sinais
Proteínas de Transporte Vesicular/metabolismo
Asas de Animais/metabolismo
[Mh] Termos MeSH secundário: Animais
Drosophila/crescimento & desenvolvimento
Discos Imaginais/metabolismo
Ligantes
Receptores Notch/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (Ligands); 0 (Lqf protein, Drosophila); 0 (Receptors, Notch); 0 (Vesicular Transport Proteins)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171222
[Lr] Data última revisão:
171222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171202
[St] Status:MEDLINE


  10 / 7079 MEDLINE  
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[PMID]:29031773
[Au] Autor:Wang Y; Ru Y; Liu G; Dong S; Li Y; Zhu X; Zhang F; Chang YZ; Nie G
[Ad] Endereço:Laboratory of Molecular Iron Metabolism, College of Life Science, Hebei Normal University, Shijiazhuang 050024, Hebei Province, China; CAS Key Laboratory for Biomedical Effects of Nanomaterials and Nanosafety, CAS Center for Excellence in Nanoscience, National Center for Nanoscience and Technology,
[Ti] Título:Identification of CDAN1, C15ORF41 and SEC23B mutations in Chinese patients affected by congenital dyserythropoietic anemia.
[So] Source:Gene;640:73-78, 2018 Jan 15.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Congenital dyserythropoietic anaemias (CDAs) are a group of rare haematological disorders characterized by ineffective erythropoiesis and dyserythropoiesis and reduced numbers of red cells, often with an abnormal morphology. Pathogenic defects in CDAN1, C15ORF41, SEC23B, KIF23, KLF1 and GATA1 genes have been identified in CDAs patients. In this study, we described 13 unrelated Chinese CDAs patients and identified 21 mutations, including 5 novel mutations in CDAN1 gene, and 5 novel mutations in SEC23B gene. Additionally, we predicted the molecular consequence of these missense mutations with Polymorphism Phenotyping v2 (Polyphen), Sorting Intolerant From Tolerant (SIFT), MutPred (http://mutpred1.mutdb.org/) and Protein Variation Effect Analyzer (Provean, http://provean.jcvi.org/seq_submit.php) and analyzed the conservation of the mutated amino acid among proteins from several mammalian species.
[Mh] Termos MeSH primário: Anemia Diseritropoética Congênita/diagnóstico
Grupo com Ancestrais do Continente Asiático/genética
Proteínas de Ciclo Celular/genética
Glicoproteínas/genética
Mutação
Proteínas de Transporte Vesicular/genética
[Mh] Termos MeSH secundário: Adolescente
Adulto
Anemia Diseritropoética Congênita/genética
Estudos de Casos e Controles
Criança
Pré-Escolar
Feminino
Seres Humanos
Lactente
Recém-Nascido
Masculino
Meia-Idade
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CDAN1 protein, human); 0 (Cell Cycle Proteins); 0 (Glycoproteins); 0 (SEC23B protein, human); 0 (Vesicular Transport Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171017
[St] Status:MEDLINE



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