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[PMID]:28860329
[Au] Autor:Fledrich R; Mannil M; Leha A; Ehbrecht C; Solari A; Pelayo-Negro AL; Berciano J; Schlotter-Weigel B; Schnizer TJ; Prukop T; Garcia-Angarita N; Czesnik D; Haberlová J; Mazanec R; Paulus W; Beissbarth T; Walter MC; Triaal C; Hogrel JY; Dubourg O; Schenone A; Baets J; De Jonghe P; Shy ME; Horvath R; Pareyson D; Seeman P; Young P; Sereda MW
[Ad] Endereço:Department of Clinical Neurophysiology, University Medical Center Göttingen (UMG), Göttingen, Germany.
[Ti] Título:Biomarkers predict outcome in Charcot-Marie-Tooth disease 1A.
[So] Source:J Neurol Neurosurg Psychiatry;88(11):941-952, 2017 Nov.
[Is] ISSN:1468-330X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Charcot-Marie-Tooth disease type 1A (CMT1A) is the most common inherited neuropathy, a debilitating disease without known cure. Among patients with CMT1A, disease manifestation, progression and severity are strikingly variable, which poses major challenges for the development of new therapies. Hence, there is a strong need for sensitive outcome measures such as disease and progression biomarkers, which would add powerful tools to monitor therapeutic effects in CMT1A. METHODS: We established a pan-European and American consortium comprising nine clinical centres including 311 patients with CMT1A in total. From all patients, the CMT neuropathy score and secondary outcome measures were obtained and a skin biopsy collected. In order to assess and validate disease severity and progression biomarkers, we performed qPCR on a set of 16 animal model-derived potential biomarkers in skin biopsy mRNA extracts. RESULTS: In 266 patients with CMT1A, a cluster of eight cutaneous transcripts differentiates disease severity with a sensitivity and specificity of 90% and 76.1%, respectively. In an additional cohort of 45 patients with CMT1A, from whom a second skin biopsy was taken after 2-3 years, the cutaneous mRNA expression of GSTT2, CTSA, PPARG, CDA, ENPP1 and NRG1-Iis changing over time and correlates with disease progression. CONCLUSIONS: In summary, we provide evidence that cutaneous transcripts in patients with CMT1A serve as disease severity and progression biomarkers and, if implemented into clinical trials, they could markedly accelerate the development of a therapy for CMT1A.
[Mh] Termos MeSH primário: Doença de Charcot-Marie-Tooth/terapia
Progressão da Doença
Marcadores Genéticos/genética
Pele/patologia
Resultado do Tratamento
[Mh] Termos MeSH secundário: Adulto
Idoso
Biópsia
Catepsina A/genética
Doença de Charcot-Marie-Tooth/sangue
Doença de Charcot-Marie-Tooth/genética
Feminino
Glutationa Transferase/genética
Glicoproteínas/genética
Seres Humanos
Masculino
Meia-Idade
Neuregulina-1/genética
PPAR gama/genética
Diester Fosfórico Hidrolases/genética
Prognóstico
Pirofosfatases/genética
RNA Mensageiro/genética
Reação em Cadeia da Polimerase em Tempo Real
Transcrição Genética/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CDAN1 protein, human); 0 (Genetic Markers); 0 (Glycoproteins); 0 (NRG1 protein, human); 0 (Neuregulin-1); 0 (PPAR gamma); 0 (RNA, Messenger); EC 2.5.1.- (GSTT2 protein, human); EC 2.5.1.18 (Glutathione Transferase); EC 3.1.4.- (Phosphoric Diester Hydrolases); EC 3.1.4.1 (ectonucleotide pyrophosphatase phosphodiesterase 1); EC 3.4.16.5 (CTSA protein, human); EC 3.4.16.5 (Cathepsin A); EC 3.6.1.- (Pyrophosphatases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171114
[Lr] Data última revisão:
171114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170902
[St] Status:MEDLINE
[do] DOI:10.1136/jnnp-2017-315721


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[PMID]:28422978
[Au] Autor:Haag C; Pohlmann T; Feldbrügge M
[Ad] Endereço:Heinrich Heine University Düsseldorf, Institute for Microbiology, Cluster of Excellence on Plant Sciences, Düsseldorf, Germany.
[Ti] Título:The ESCRT regulator Did2 maintains the balance between long-distance endosomal transport and endocytic trafficking.
[So] Source:PLoS Genet;13(4):e1006734, 2017 Apr.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In highly polarised cells, like fungal hyphae, early endosomes function in both endocytosis as well as long-distance transport of various cargo including mRNA and protein complexes. However, knowledge on the crosstalk between these seemingly different trafficking processes is scarce. Here, we demonstrate that the ESCRT regulator Did2 coordinates endosomal transport in fungal hyphae of Ustilago maydis. Loss of Did2 results in defective vacuolar targeting, less processive long-distance transport and abnormal shuttling of early endosomes. Importantly, the late endosomal protein Rab7 and vacuolar protease Prc1 exhibit increased shuttling on these aberrant endosomes suggesting defects in endosomal maturation and identity. Consistently, molecular motors fail to attach efficiently explaining the disturbed processive movement. Furthermore, the endosomal mRNP linker protein Upa1 is hardly present on endosomes resulting in defects in long-distance mRNA transport. In conclusion, the ESCRT regulator Did2 coordinates precise maturation of endosomes and thus provides the correct membrane identity for efficient endosomal long-distance transport.
[Mh] Termos MeSH primário: Complexos Endossomais de Distribuição Requeridos para Transporte/genética
Endossomos/genética
Transporte Proteico/genética
Transporte de RNA/genética
Proteínas de Saccharomyces cerevisiae/genética
Ustilago/genética
[Mh] Termos MeSH secundário: Catepsina A/genética
Polaridade Celular/genética
Endocitose/genética
Complexos Endossomais de Distribuição Requeridos para Transporte/metabolismo
Endossomos/metabolismo
Hifas/genética
Hifas/crescimento & desenvolvimento
Hifas/metabolismo
RNA Mensageiro/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/crescimento & desenvolvimento
Proteínas de Saccharomyces cerevisiae/metabolismo
Vesículas Transportadoras/genética
Vesículas Transportadoras/metabolismo
Ustilago/crescimento & desenvolvimento
Proteínas rab de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DID2 protein, S cerevisiae); 0 (Endosomal Sorting Complexes Required for Transport); 0 (RNA, Messenger); 0 (Saccharomyces cerevisiae Proteins); 152989-05-4 (rab7 protein); EC 3.4.16.5 (Cathepsin A); EC 3.4.16.5 (PRC1 protein, S cerevisiae); EC 3.6.5.2 (rab GTP-Binding Proteins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170601
[Lr] Data última revisão:
170601
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170420
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006734


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[PMID]:28234994
[Au] Autor:Pan X; Wang Y; Lübke T; Hinek A; Pshezhetsky AV
[Ad] Endereço:Department of Medical Genetics, CHU Sainte-Justine Research Center, University of Montreal, Montreal, Quebec, Canada.
[Ti] Título:Mice, double deficient in lysosomal serine carboxypeptidases Scpep1 and Cathepsin A develop the hyperproliferative vesicular corneal dystrophy and hypertrophic skin thickenings.
[So] Source:PLoS One;12(2):e0172854, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Vasoactive and mitogenic peptide, endothelin-1 (ET-1) plays an important role in physiology of the ocular tissues by regulating the growth of corneal epithelial cells and maintaining the hemodynamics of intraocular fluids. We have previously established that ET-1 can be degraded in vivo by two lysosomal/secreted serine carboxypeptidases, Cathepsin A (CathA) and Serine Carboxypeptidase 1 (Scpep1) and that gene-targeted CathAS190A /Scpep1-/- mice, deficient in CathA and Scpep1 have a prolonged half-life of circulating ET-1 associated with systemic hypertension. In the current work we report that starting from 6 months of age, ~43% of CathAS190A /Scpep1-/- mice developed corneal clouding that eventually caused vision impairment. Histological evaluation of these mice demonstrated a selective fibrotic thickening and vacuolization of the corneas, resembling human hyperproliferative vesicular corneal stromal dystrophy and coexisting with a peculiar thickening of the skin epidermis. Moreover, we found that cultured corneal epithelial cells, skin fibroblasts and vascular smooth muscle cells derived from CathA/Scpep1-deficient mice, demonstrated a significantly higher proliferative response to treatment with exogenous ET-1, as compared with cells from wild type mice. We also detected increased activation level of ERK1/2 and AKT kinases involved in cell proliferation in the ET-1-treated cultured cells from CathA/Scpep1 deficient mice. Together, results from our experimental model suggest that; in normal tissues the tandem of serine carboxypeptidases, Scpep1 and CathA likely constitutes an important part of the physiological mechanism responsible for the balanced elimination of heightened levels of ET-1 that otherwise would accumulate in tissues and consequently contribute to development of the hyper-proliferative corneal dystrophy and abnormal skin thickening.
[Mh] Termos MeSH primário: Carboxipeptidases/genética
Catepsina A/genética
Distrofias Hereditárias da Córnea/genética
Lisossomos/enzimologia
Pele/patologia
[Mh] Termos MeSH secundário: Animais
Humor Aquoso/metabolismo
Carboxipeptidases/metabolismo
Catepsina A/metabolismo
Proliferação Celular
Distrofias Hereditárias da Córnea/metabolismo
Endotelina-1/farmacologia
Epiderme/patologia
Feminino
Fibroblastos/citologia
Fibrose
Hemodinâmica
Masculino
Camundongos
Camundongos Knockout
Miócitos de Músculo Liso/citologia
Miofibroblastos/citologia
Fosforilação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Endothelin-1); EC 3.4.- (Carboxypeptidases); EC 3.4.16.- (Scpep1 protein, mouse); EC 3.4.16.5 (Cathepsin A)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170225
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0172854


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[PMID]:28189789
[Au] Autor:B S GK; Surolia A
[Ad] Endereço:Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India.
[Ti] Título:N-Glycosylation analysis of yeast Carboxypeptidase Y reveals the ultimate removal of phosphate from glycans at Asn .
[So] Source:Int J Biol Macromol;98:582-585, 2017 May.
[Is] ISSN:1879-0003
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Carboxypeptidase Y from Saccharomyces cerivisiae was characterized for its site specific N-glycosylation through mass spectrometry. The N-glycopeptides were derived using non specific proteases and are analysed directly on liquid chromatography coupled to ion trap mass spectrometer in tandem mode. The evaluation of glycan fragment ions and the Y ions (peptide+HexNAc) revealed the glycan sequence and the corresponding site of attachment. We observed the microheterogeneity in N-glycans such as Man GlcNAc at Asn , Man GlcNAc at Asn , Man GlcNAc at Asn and phosphorylated Man GlcNAc as well as Man GlcNAc at Asn . The presence of N-glycans with Man GlcNAc indicated that in vacuoles the steady release of mannose/phospho mannose residues from glycans occurs initially at Asn or Asn followed by at Asn . However, glycans at Asn which comprises Man residues as reported earlier remain intact suggesting its inaccessibility for a similar processing. This in turn indicates the interaction of the glycan at Asn with the polypeptide chain implicating it in the folding of the protein.
[Mh] Termos MeSH primário: Catepsina A/química
Polissacarídeos/química
Saccharomyces cerevisiae/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos/genética
Asparagina/química
Catepsina A/metabolismo
Glicopeptídeos/química
Glicopeptídeos/genética
Glicosilação
Seres Humanos
Fosfatos/química
Fosforilação
Dobramento de Proteína
Saccharomyces cerevisiae/genética
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycopeptides); 0 (Phosphates); 0 (Polysaccharides); 7006-34-0 (Asparagine); EC 3.4.16.5 (Cathepsin A)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170324
[Lr] Data última revisão:
170324
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170213
[St] Status:MEDLINE


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[PMID]:28133419
[Au] Autor:Calhan OY; Seyrantepe V
[Ad] Endereço:Department of Molecular Biology and Genetics, Izmir Institute of Technology, Gulbahce Mahallesi, Urla, Izmir, Turkey.
[Ti] Título:Mice with Catalytically Inactive Cathepsin A Display Neurobehavioral Alterations.
[So] Source:Behav Neurol;2017:4261873, 2017.
[Is] ISSN:1875-8584
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The lysosomal carboxypeptidase A, Cathepsin A (CathA), is a serine protease with two distinct functions. CathA protects -galactosidase and sialidase Neu1 against proteolytic degradation by forming a multienzyme complex and activates sialidase Neu1. CathA deficiency causes the lysosomal storage disease, galactosialidosis. These patients present with a broad range of clinical phenotypes, including growth retardation, and neurological deterioration along with the accumulation of the vasoactive peptide, endothelin-1, in the brain. Previous in vitro studies have shown that CathA has specific activity against vasoactive peptides and neuropeptides, including endothelin-1 and oxytocin. A mutant mouse with catalytically inactive CathA enzyme ( ) shows increased levels of endothelin-1. In the present study, we elucidated the involvement of CathA in learning and long-term memory in 3-, 6-, and 12-month-old mice. Hippocampal endothelin-1 and oxytocin accumulated in mice, which showed learning impairments as well as long-term and spatial memory deficits compared with wild-type littermates, suggesting that CathA plays a significant role in learning and in memory consolidation through its regulatory role in vasoactive peptide processing.
[Mh] Termos MeSH primário: Comportamento Animal/fisiologia
Catepsina A/fisiologia
Endotelina-1/metabolismo
Hipocampo/metabolismo
Aprendizagem/fisiologia
Transtornos da Memória/metabolismo
Ocitocina/metabolismo
[Mh] Termos MeSH secundário: Animais
Catepsina A/metabolismo
Modelos Animais de Doenças
Hipocampo/enzimologia
Masculino
Consolidação da Memória/fisiologia
Transtornos da Memória/enzimologia
Memória de Longo Prazo/fisiologia
Camundongos
Camundongos Endogâmicos C57BL
Memória Espacial/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Endothelin-1); 50-56-6 (Oxytocin); EC 3.4.16.5 (Cathepsin A)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170224
[Lr] Data última revisão:
170224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170131
[St] Status:MEDLINE
[do] DOI:10.1155/2017/4261873


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[PMID]:27664989
[Au] Autor:Bugiani M; Kevelam SH; Bakels HS; Waisfisz Q; Ceuterick-de Groote C; Niessen HW; Abbink TE; Lesnik Oberstein SA; van der Knaap MS
[Ad] Endereço:From the Departments of Child Neurology (M.B., S.H.K., H.S.B., T.E.M.A., M.S.v.d.K.) and Pathology (M.B., H.W.M.N.), Neuroscience Campus Amsterdam, VU University Medical Center, Amsterdam; Department of Clinical Genetics (Q.W.), VU University Medical Center, Amsterdam, the Netherlands; Laboratory fo
[Ti] Título:Cathepsin A-related arteriopathy with strokes and leukoencephalopathy (CARASAL).
[So] Source:Neurology;87(17):1777-1786, 2016 Oct 25.
[Is] ISSN:1526-632X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To characterize the clinical and MRI features of 2 families with adult-onset dominant leukoencephalopathy and strokes and identify the underlying genetic cause. METHODS: We applied MRI pattern recognition, whole-exome sequencing, and neuropathology. RESULTS: Based on brain imaging, 13 family members of 40 years or older from 2 families were diagnosed with the disease; in 11 family members of the same age, MRI was normal. In the affected family members, MRI showed a leukoencephalopathy that was disproportionately severe compared to the clinical disease. The clinical picture was dominated by ischemic and hemorrhagic strokes, slow and late cognitive deterioration, and therapy-resistant hypertension. With whole-exome sequencing, we identified one variant shared by both families and segregating with the disease: c.973C>T in CTSA. Haplotype analysis revealed a shared 1,145-kb interval encompassing the CTSA variant on chromosome 20q13.12, suggesting a common ancestor. Brain autopsy of 3 patients showed a leukoencephalopathy that was disproportionately extensive compared to the vascular abnormalities. CTSA encodes cathepsin A. Recessive CTSA mutations cause galactosialidosis. One of the numerous cathepsin A functions is to degrade endothelin-1. In the patients, striking endothelin-1 immunoreactivity was found in white matter astrocytes, correlating with increased numbers of premyelinating oligodendrocyte progenitors. This finding supports a role for endothelin-1 in the leukoencephalopathy through inhibition of oligodendrocyte progenitor maturation. CONCLUSIONS: CARASAL (cathepsin A-related arteriopathy with strokes and leukoencephalopathy) is a novel hereditary adult-onset cerebral small vessel disease. It is of interest that, next to the cerebral vascular abnormalities, endothelin-1 may have a role in the pathogenesis of the extensive leukoencephalopathy.
[Mh] Termos MeSH primário: Hemorragia
Leucoencefalopatias
Acidente Vascular Cerebral
Malformações Vasculares
[Mh] Termos MeSH secundário: Adulto
Idoso
Encéfalo/diagnóstico por imagem
Encéfalo/metabolismo
Encéfalo/ultraestrutura
Catepsina A/genética
Endotelinas/metabolismo
Saúde da Família
Feminino
Estudo de Associação Genômica Ampla
Hemorragia/complicações
Hemorragia/diagnóstico por imagem
Hemorragia/genética
Seres Humanos
Leucoencefalopatias/complicações
Leucoencefalopatias/diagnóstico por imagem
Leucoencefalopatias/genética
Imagem por Ressonância Magnética
Masculino
Repetições de Microssatélites
Meia-Idade
Mutação/genética
Exame Neurológico
Acidente Vascular Cerebral/complicações
Acidente Vascular Cerebral/diagnóstico por imagem
Acidente Vascular Cerebral/genética
Malformações Vasculares/complicações
Malformações Vasculares/diagnóstico por imagem
Malformações Vasculares/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Endothelins); EC 3.4.16.5 (CTSA protein, human); EC 3.4.16.5 (Cathepsin A)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170512
[Lr] Data última revisão:
170512
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:160925
[St] Status:MEDLINE


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[PMID]:27524515
[Au] Autor:James AW; Gowsalya R; Nachiappan V
[Ad] Endereço:Biomembrane Lab, Department of Biochemistry, School of Life Sciences, Bharathidasan University, Tiruchirappalli 620 024, Tamilnadu, India.
[Ti] Título:Dolichyl pyrophosphate phosphatase-mediated N-glycosylation defect dysregulates lipid homeostasis in Saccharomyces cerevisiae.
[So] Source:Biochim Biophys Acta;1861(11):1705-1718, 2016 Nov.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The endoplasmic reticulum (ER) has numerous biological functions including protein synthesis, protein folding, and lipid synthesis. The CAX4 gene encodes dolichyl pyrophosphate (Dol-PP) phosphatase, which is involved in protein N-glycosylation. In cax4Δ cells, the N-glycosylation of the vacuolar carboxypeptidase (CPY) was severely affected, and expression of the ER chaperone Kar2p was elevated, which resulted in UPR activation as an adaptive response. The cax4Δ cell growth was reduced, and this could be attributed to the formation of clumped aggregates, high vesiculation of the intracellular membrane, and plasma membrane alterations were depicted using DiOC6 fluorescence. In the cax4 deletion strain, the transcription factors INO2 and INO4 were upregulated, and the negative regulator OPI1 was concomitantly down regulated, which led to the derepression of the phospholipid genes CHO2, OPI3, PSD1, and PSD2 and resulted in increased phospholipid levels. However, the TAG, SE, and LD levels were significantly reduced, and FFA, sterol, and DAG levels were increased. These findings could be attributed to the derepression of the TAG and SE lipases TGL3, TGL4, TGL5, YEH1, and YEH2 and the repression of LRO1, DGA1, ARE1, and ARE2 in cax4Δ cells. Interestingly, the overexpression of SEC59 or CAX4 in cax4Δ cells prevented the ER stress and growth defect, and restored normal level of phospholipids, neutral lipids, and LDs. The current study revealed the disruption of N-glycosylation-induced ER stress, altered lipid homeostasis accounts for pleiotropic phenotype. Thus, CAX4 regulates membrane biogenesis by coordinating lipid homeostasis with protein quality control.
[Mh] Termos MeSH primário: Fosfatos de Dolicol/metabolismo
Homeostase
Metabolismo dos Lipídeos
Pirofosfatases/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/enzimologia
[Mh] Termos MeSH secundário: Western Blotting
Catepsina A/metabolismo
Membrana Celular/metabolismo
Estresse do Retículo Endoplasmático
Fluorescência
Regulação Fúngica da Expressão Gênica
Genes Fúngicos
Teste de Complementação Genética
Glicosilação
Proteínas de Fluorescência Verde/metabolismo
Gotículas Lipídicas/metabolismo
Metabolismo dos Lipídeos/genética
Mutação/genética
Fenótipo
Fosfolipídeos/metabolismo
Fosfotransferases (Aceptor do Grupo Álcool)/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/crescimento & desenvolvimento
Fatores de Tempo
Resposta a Proteínas não Dobradas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CAX4 protein, S cerevisiae); 0 (Dolichol Phosphates); 0 (Phospholipids); 0 (RNA, Messenger); 0 (Saccharomyces cerevisiae Proteins); 147336-22-9 (Green Fluorescent Proteins); 37247-98-6 (dolichol pyrophosphate); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.1.108 (dolichol kinase); EC 3.4.16.5 (Cathepsin A); EC 3.6.1.- (Pyrophosphatases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160816
[St] Status:MEDLINE


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[PMID]:27432266
[Au] Autor:Petrera A; Kern U; Linz D; Gomez-Auli A; Hohl M; Gassenhuber J; Sadowski T; Schilling O
[Ad] Endereço:Institute of Molecular Medicine and Cell Research, University of Freiburg , Stefan Meier Strasse 17, 79104 Freiburg, Germany.
[Ti] Título:Proteomic Profiling of Cardiomyocyte-Specific Cathepsin A Overexpression Links Cathepsin A to the Oxidative Stress Response.
[So] Source:J Proteome Res;15(9):3188-95, 2016 Sep 02.
[Is] ISSN:1535-3907
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cathepsin A (CTSA) is a lysosomal carboxypeptidase present at the cell surface and secreted outside the cell. Additionally, CTSA binds to ß-galactosidase and neuraminidase 1 to protect them from degradation. CTSA has gained attention as a drug target for the treatment of cardiac hypertrophy and heart failure. Here, we investigated the impact of CTSA on the murine cardiac proteome in a mouse model of cardiomyocyte-specific human CTSA overexpression using liquid chromatography-tandem mass spectrometry in conjunction with an isotopic dimethyl labeling strategy. We identified up to 2000 proteins in each of three biological replicates. Statistical analysis by linear models for microarray data (limma) found >300 significantly affected proteins (moderated p-value ≤0.01), thus establishing CTSA as a key modulator of the cardiac proteome. CTSA strongly impaired the balance of the proteolytic system by upregulating several proteases such as cathepsin B, cathepsin D, and cathepsin Z while down-regulating numerous protease inhibitors. Moreover, cardiomyocyte-specific human CTSA overexpression strongly reduced the levels of numerous antioxidative stress proteins, i.e., peroxiredoxins and protein deglycase DJ-1. In vitro, using cultured rat cardiomyocytes, ectopic overexpression of CTSA resulted in accumulation of reactive oxygen species. Collectively, our proteomic and functional data strengthen an association of CTSA with the cellular oxidative stress response.
[Mh] Termos MeSH primário: Catepsina A/farmacologia
Miócitos Cardíacos/metabolismo
Estresse Oxidativo
Proteômica/métodos
[Mh] Termos MeSH secundário: Animais
Catepsina A/metabolismo
Cromatografia Líquida
Seres Humanos
Espectrometria de Massas
Camundongos
Estresse Oxidativo/efeitos dos fármacos
Proteólise
Proteoma/efeitos dos fármacos
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proteome); 0 (Reactive Oxygen Species); EC 3.4.16.5 (Cathepsin A)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160720
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jproteome.6b00413


  9 / 639 MEDLINE  
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[PMID]:27425760
[Au] Autor:Tian M; Zhang N; Liu X; Guo L; Yang L
[Ad] Endereço:Key Laboratory of Nanobiosensing and Nanobioanalysis at Universities of Jilin Province, Department of Chemistry, Northeast Normal University, 5268 Renmin Street, Changchun, Jilin Province 130024, PR China.
[Ti] Título:Sequential on-line C-terminal sequencing of peptides based on carboxypeptidase Y digestion and optically gated capillary electrophoresis with laser-induced fluorescence detection.
[So] Source:J Chromatogr A;1459:152-159, 2016 Aug 12.
[Is] ISSN:1873-3778
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:We report a novel method for sequential on-line C-terminal sequencing of peptides, which combines carboxypeptidase Y (CPY) digestion with on-line derivatization and optically gated capillary electrophoresis with laser-induced fluorescence detection (OGCE-LIF). Various factors that may affect the C-terminal sequencing were investigated and optimized. High repeatability of on-line derivatization and the sequential OGCE-LIF assay of amino acids (AAs) was achieved with relative standard deviation (RSD) (n=20) less than 1.5% and 3.2% for migration time and peak height, respectively. A total of 13 AAs was efficiently separated in the present study, indicating that the method can be used for sequencing of peptides consisting of the 13 AAs studied. Using two synthesized N-terminally blocked peptides as test examples, we show that the present method can on-line monitor the released AAs with a temporal resolution of 50s during the entire CPY digestion process. The rates of AA release as a function of digestion time were easily measured; thus, the AA sequence of the peptide was determined with just one OGCE assay. Our study indicates the present approach is an effective, reliable, and convenient method for rapid analysis of the C-terminal sequence of peptides, with potential application in peptide analysis and proteome research.
[Mh] Termos MeSH primário: Catepsina A/metabolismo
Eletroforese Capilar
Peptídeos/análise
Espectrometria de Fluorescência
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Lasers
Peptídeos/química
Peptídeos/metabolismo
Análise de Sequência de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptides); EC 3.4.16.5 (Cathepsin A)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170806
[Lr] Data última revisão:
170806
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160719
[St] Status:MEDLINE


  10 / 639 MEDLINE  
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[PMID]:27363206
[Au] Autor:Duan W; Zhang Y; Xu G
[Ti] Título:Optimization and application of protein C-terminal labeling by carboxypeptidase Y.
[So] Source:Sheng Wu Gong Cheng Xue Bao;32(1):135-48, 2016 Jan.
[Is] ISSN:1000-3061
[Cp] País de publicação:China
[La] Idioma:eng
[Ab] Resumo:Proteolytic cleavage is one of the post-translational modifications and plays important roles in many biological processes, such as apoptosis and tumor cell metastasis. The identification of the cleavage events can improve our understanding of their biological functions in these processes. Although proteomic approaches using N-terminal labeling have resulted in the discovery of many proteolytic cleavages, this strategy has its own inherent drawbacks. Labeling of protein C-termini is an alternative approach. Here, we optimized the labeling procedure in the profiling protein C-termini by enzymatic labeling (ProC-TEL) and improved the labeling efficiency for the positive isolation of protein C-terminal peptides and mass spectrometric identification. We applied this approach to a complex protein mixture from Escherichia coli and identified many C-terminal peptides and internal cleaved peptides from more than 120 proteins. From the identified cleavages, we found several previously known internal proteolytic cleavage sites and many novel ones which may play roles in regulating normal biological processes. This work provides a potential new way, complementary to the N-terminomics, for the identification of proteolytic cleavages in complex biological systems.
[Mh] Termos MeSH primário: Catepsina A/química
Proteína C/química
Processamento de Proteína Pós-Traducional
Proteômica
[Mh] Termos MeSH secundário: Proteólise
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Protein C); EC 3.4.16.5 (Cathepsin A)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:160701
[Lr] Data última revisão:
160701
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160702
[St] Status:MEDLINE



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