Base de dados : MEDLINE
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[PMID]:25447654
[Au] Autor:Harada T; Ishimatsu Y; Nakashima S; Miura S; Tomonaga M; Kakugawa T; Hara S; Sakamoto N; Yoshii C; Mukae H; Kawabata Y; Kohno S
[Ad] Endereço:The Second Department of Internal Medicine, Nagasaki University School of Medicine, Japan.
[Ti] Título:An autopsy case of Hermansky-Pudlak syndrome: a case report and review of the literature on treatment.
[So] Source:Intern Med;53(23):2705-9, 2014.
[Is] ISSN:1349-7235
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Hermansky-Pudlak syndrome (HPS) is a rare genetic disorder, the most common complication of which influencing the prognosis is pulmonary fibrosis. In the present report, we describe an autopsy case of a Japanese woman with HPS. The patient was diagnosed at 50 years of age based on the presence of oculocutaneous albinism, hemorrhagic diathesis, ceroid-lipofuscin accumulation and pulmonary fibrosis. Although systemic steroids, immunosuppressants and pirfenidone were administered for pulmonary involvement, she died from respiratory failure two years later. Obtaining an early diagnosis and taking into consideration the need for lung transplantation is necessary in order to improve the prognosis of HPS. We herein report this very rare Japanese case of HPS with a review of the treatment approaches for HPS complicated with pulmonary fibrosis.
[Mh] Termos MeSH primário: Síndrome de Hermanski-Pudlak/complicações
Síndrome de Hermanski-Pudlak/diagnóstico
Fibrose Pulmonar/complicações
Fibrose Pulmonar/diagnóstico
Insuficiência Respiratória/etiologia
[Mh] Termos MeSH secundário: Corticosteroides/administração & dosagem
Autopsia
Ceroide/metabolismo
Quimioterapia Combinada
Evolução Fatal
Feminino
Transtornos Hemorrágicos/complicações
Transtornos Hemorrágicos/diagnóstico
Síndrome de Hermanski-Pudlak/patologia
Seres Humanos
Imunossupressores/administração & dosagem
Lipofuscina/metabolismo
Transplante de Pulmão
Meia-Idade
Fibrose Pulmonar/tratamento farmacológico
Fibrose Pulmonar/etiologia
Fibrose Pulmonar/patologia
Piridonas/administração & dosagem
Insuficiência Respiratória/patologia
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Adrenal Cortex Hormones); 0 (Ceroid); 0 (Immunosuppressive Agents); 0 (Lipofuscin); 0 (Pyridones); D7NLD2JX7U (pirfenidone)
[Em] Mês de entrada:1505
[Cu] Atualização por classe:141202
[Lr] Data última revisão:
141202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141203
[St] Status:MEDLINE


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[PMID]:24736558
[Au] Autor:Burkovetskaya M; Karpuk N; Xiong J; Bosch M; Boska MD; Takeuchi H; Suzumura A; Kielian T
[Ad] Endereço:Departments of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, Nebraska, United States of America.
[Ti] Título:Evidence for aberrant astrocyte hemichannel activity in Juvenile Neuronal Ceroid Lipofuscinosis (JNCL).
[So] Source:PLoS One;9(4):e95023, 2014.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Juvenile Neuronal Ceroid Lipofuscinosis (JNCL) is a lysosomal storage disease caused by an autosomal recessive mutation in CLN3 that leads to vision loss, progressive cognitive and motor decline, and premature death. Morphological evidence of astrocyte activation occurs early in the disease process and coincides with regions where neuronal loss eventually ensues. However, the consequences of CLN3 mutation on astrocyte function remain relatively ill-defined. Astrocytes play a critical role in CNS homeostasis, in part, by their ability to regulate the extracellular milieu via the formation of extensive syncytial networks coupled by gap junction (GJ) channels. In contrast, unopposed hemichannels (HCs) have been implicated in CNS pathology by allowing the non-discriminant passage of molecules between the intracellular and extracellular milieus. Here we examined acute brain slices from CLN3 mutant mice (CLN3Δex7/8) to determine whether CLN3 loss alters the balance of GJ and HC activity. CLN3Δex7/8 mice displayed transient increases in astrocyte HC opening at postnatal day 30 in numerous brain regions, compared to wild type (WT) animals; however, HC activity steadily decreased at postnatal days 60 and 90 in CLN3Δex7/8 astrocytes to reach levels lower than WT cells. This suggested a progressive decline in astrocyte function, which was supported by significant reductions in glutamine synthetase, GLAST, and connexin expression in CLN3Δex7/8 mice compared to WT animals. Based on the early increase in astrocyte HC activity, CLN3Δex7/8 mice were treated with the novel carbenoxolone derivative INI-0602 to inhibit HCs. Administration of INI-0602 for a one month period significantly reduced lysosomal ceroid inclusions in the brains of CLN3Δex7/8 mice compared to WT animals, which coincided with significant increases in astrocyte GJ communication and normalization of astrocyte resting membrane potential to WT levels. Collectively, these findings suggest that alterations in astrocyte communication may impact the progression of JNCL and could offer a potential therapeutic target.
[Mh] Termos MeSH primário: Astrócitos/metabolismo
Proteínas de Membrana Transportadoras/metabolismo
Lipofuscinoses Ceroides Neuronais/metabolismo
[Mh] Termos MeSH secundário: Animais
Astrócitos/efeitos dos fármacos
Biomarcadores
Encéfalo/metabolismo
Ceroide/metabolismo
Conexinas/genética
Conexinas/metabolismo
Feminino
Junções Comunicantes/metabolismo
Ácido Glutâmico/metabolismo
Homeostase
Lisossomos/metabolismo
Masculino
Glicoproteínas de Membrana/deficiência
Glicoproteínas de Membrana/genética
Camundongos
Camundongos Knockout
Chaperonas Moleculares/genética
Mutação
Lipofuscinoses Ceroides Neuronais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biomarkers); 0 (CLN3 protein, mouse); 0 (Ceroid); 0 (Connexins); 0 (Membrane Glycoproteins); 0 (Membrane Transport Proteins); 0 (Molecular Chaperones); 3KX376GY7L (Glutamic Acid)
[Em] Mês de entrada:1501
[Cu] Atualização por classe:170510
[Lr] Data última revisão:
170510
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140417
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0095023


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[PMID]:24284295
[Au] Autor:Ozyilmaz E; Gunasti S; Kuyuku Y; Polat S; Gumurdulu D; Kuleci S; Hanta I; Kocabas A
[Ad] Endereço:Cukurova University Faculty of Medicine Department of Pulmonary Disease Balcali. ezgiozyilmaz@hotmail.com.
[Ti] Título:Hermansky Pudlak Syndrome and Pulmonary Alveolar Proteinosis at the same patient: first case report in the world literature.
[So] Source:Sarcoidosis Vasc Diffuse Lung Dis;30(3):217-20, 2013 Nov 25.
[Is] ISSN:1124-0490
[Cp] País de publicação:Italy
[La] Idioma:eng
[Ab] Resumo:Hermansky-Pudlak Syndrome (HPS) is a rare autosomal recessive disorder presenting with oculocutaneous albinism, bleeding diathesis and lysosomal accumulation of ceroid lipofuscin which leads to interstitial fibrosis in lung. Pulmonary fibrosis which is usually associated with HPS-1 and HPS-4 subtypes usually manifests in the third/fourth decades of life representing with giant lamellar bodies of alveolar type-II-cells and their apparent degeneration causes restrictive lung disease. Pulmonary manifestation of this syndrome may lead to premature death. Pulmonary Alveolar Proteinosis(PAP) is another rare disease characterized by alveolar deposition of surfactant phospholipids and proteins secondary to defective clearance by alveolar macrophages. PAP may occur as autoimmune diseases and/or secondary to toxic inhalation, systemic infections or hematological disorders. None of the cases were reported secondary to HPS according to the best our knowledge. As well, pulmonary involvement of HPS was never reported as PAP. We report the first case of PAP in a patient with HPS.
[Mh] Termos MeSH primário: Síndrome de Hermanski-Pudlak
Proteinose Alveolar Pulmonar
[Mh] Termos MeSH secundário: Ceroide
Seres Humanos
Pulmão/metabolismo
Fibrose Pulmonar
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ceroid)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:161021
[Lr] Data última revisão:
161021
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131129
[St] Status:MEDLINE


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[PMID]:23249249
[Au] Autor:Van Beersel G; Tihon E; Demine S; Hamer I; Jadot M; Arnould T
[Ad] Endereço:*Laboratory of Biochemistry and Cellular Biology (URBC), NAmur Research Institute for LIfe Sciences (NARILIS), University of Namur (FUNDP), rue de Bruxelles, 61, 5000 Namur, Belgium.
[Ti] Título:Different molecular mechanisms involved in spontaneous and oxidative stress-induced mitochondrial fragmentation in tripeptidyl peptidase-1 (TPP-1)-deficient fibroblasts.
[So] Source:Biosci Rep;33(2):e00023, 2013 Feb 07.
[Is] ISSN:1573-4935
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:NCLs (neuronal ceroid lipofuscinoses) form a group of eight inherited autosomal recessive diseases characterized by the intralysosomal accumulation of autofluorescent pigments, called ceroids. Recent data suggest that the pathogenesis of NCL is associated with the appearance of fragmented mitochondria with altered functions. However, even if an impairement in the autophagic pathway has often been evoked, the molecular mechanisms leading to mitochondrial fragmentation in response to a lysosomal dysfunction are still poorly understood. In this study, we show that fibroblasts that are deficient for the TPP-1 (tripeptidyl peptidase-1), a lysosomal hydrolase encoded by the gene mutated in the LINCL (late infantile NCL, CLN2 form) also exhibit a fragmented mitochondrial network. This morphological alteration is accompanied by an increase in the expression of the protein BNIP3 (Bcl2/adenovirus E1B 19 kDa interacting protein 3) as well as a decrease in the abundance of mitofusins 1 and 2, two proteins involved in mitochondrial fusion. Using RNAi (RNA interference) and quantitative analysis of the mitochondrial morphology, we show that the inhibition of BNIP3 expression does not result in an increase in the reticulation of the mitochondrial population in LINCL cells. However, this protein seems to play a key role in cell response to mitochondrial oxidative stress as it sensitizes mitochondria to antimycin A-induced fragmentation. To our knowledge, our results bring the first evidence of a mechanism that links TPP-1 deficiency and oxidative stress-induced changes in mitochondrial morphology.
[Mh] Termos MeSH primário: Aminopeptidases/genética
Dipeptidil Peptidases e Tripeptidil Peptidases/genética
Mitocôndrias/metabolismo
Lipofuscinoses Ceroides Neuronais/metabolismo
Estresse Oxidativo/genética
Serina Proteases/genética
[Mh] Termos MeSH secundário: Aminopeptidases/deficiência
Autofagia/genética
Células Cultivadas
Ceroide/metabolismo
Dipeptidil Peptidases e Tripeptidil Peptidases/deficiência
Fibroblastos/metabolismo
Fibroblastos/patologia
Seres Humanos
Lisossomos/metabolismo
Lisossomos/patologia
Mitocôndrias/efeitos dos fármacos
Mitocôndrias/patologia
Lipofuscinoses Ceroides Neuronais/patologia
Serina Proteases/deficiência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ceroid); EC 3.4.- (Serine Proteases); EC 3.4.11.- (Aminopeptidases); EC 3.4.14.- (Dipeptidyl-Peptidases and Tripeptidyl-Peptidases); EC 3.4.14.9 (tripeptidyl-peptidase 1)
[Em] Mês de entrada:1409
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121220
[St] Status:MEDLINE


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[PMID]:22847174
[Au] Autor:Ohtaki H; Ohara K; Song D; Miyamoto K; Tsumuraya T; Yofu S; Dohi K; Tanabe S; Sasaki S; Uchida S; Matsunaga M; Shioda S
[Ad] Endereço:Department of Anatomy, Showa University School of Medicine, Tokyo, Japan.
[Ti] Título:Accumulation of autofluorescent storage material in brain is accelerated by ischemia in chloride channel 3 gene-deficient mice.
[So] Source:J Neurosci Res;90(11):2163-72, 2012 Nov.
[Is] ISSN:1097-4547
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Autofluorescent storage material (ASM) is an aging pigment that accumulates during the normal course of senescence. Although the role of ASM has yet to be fully elucidated, ASM has been implicated in age-related neurodegeneration. In this study, we determined the level of ASM in chloride channel 3 (ClC-3) gene-deficient (KO) mice both in response to aging and following mild global ischemia. To understand the mechanism of action of the ASM, mice subjected to ischemia were treated with the cyclooxygenase (COX) inhibitor indomethacin or with the noncompetitive glutamate receptor antagonist MK-801. ClC-3 KO mice displayed age-related neurodegeneration of the neocortex as well as the hippocampus. The cortical layers in particular granular layers became thinner with aging. ASM accumulated in the brains of ClC-3 KO mice was increased seven- to 50-fold over that observed in the corresponding regions of their wild-type littermates. Young wild-type mice survived longer than age-matched ClC-3 KO mice after permanent global ischemia. However, in the case of older animals, the survival curves were similar. The ASM also increased four- to fivefold 10 days after mild global ischemia, an effect that was suppressed by treatment with indomethacin and MK-801. These results suggest that temporary ischemia might trigger a process similar to aging in the brain, mimicking the effect of age-related neurodegenerative diseases.
[Mh] Termos MeSH primário: Envelhecimento/genética
Isquemia Encefálica/genética
Encéfalo/patologia
Ceroide/análise
Canais de Cloreto/deficiência
Lipofuscina/análise
[Mh] Termos MeSH secundário: Envelhecimento/metabolismo
Envelhecimento/patologia
Animais
Encéfalo/metabolismo
Isquemia Encefálica/metabolismo
Isquemia Encefálica/patologia
Canais de Cloreto/biossíntese
Canais de Cloreto/genética
Imuno-Histoquímica
Camundongos
Camundongos Endogâmicos ICR
Camundongos Knockout
Degeneração Neural/genética
Degeneração Neural/metabolismo
Degeneração Neural/patologia
Imagem Óptica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ceroid); 0 (Chloride Channels); 0 (ClC-3 channel); 0 (Lipofuscin)
[Em] Mês de entrada:1304
[Cu] Atualização por classe:120911
[Lr] Data última revisão:
120911
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120801
[St] Status:MEDLINE
[do] DOI:10.1002/jnr.23110


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[PMID]:22108647
[Au] Autor:Asano Y
[Ad] Endereço:Department of Neuroanatomy, Cell Biology and Histology, Hirosaki University Graduate School of Medicine, Hirosaki, Japan. asanoy@cc.hirosaki-u.ac.jp
[Ti] Título:Age-related accumulation of non-heme ferric and ferrous iron in mouse ovarian stroma visualized by sensitive non-heme iron histochemistry.
[So] Source:J Histochem Cytochem;60(3):229-42, 2012 Mar.
[Is] ISSN:1551-5044
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sensitive non-heme iron histochemistry--namely, the perfusion-Perls method and perfusion-Turnbull method--was applied to study the distribution and age-related accumulation of non-heme ferric iron and ferrous iron in mouse ovary. Light and electron microscopic studies revealed that non-heme ferric iron is distributed predominantly in stromal tissue, especially in macrophages. By contrast, the distribution of non-heme ferrous iron was restricted to a few ovoid macrophages. Aged ovaries exhibited remarkable non-heme iron accumulation in all stromal cells. In particular, non-heme ferrous iron level was increased in stromal tissue, suggestive of increased levels of redox-active iron, which can promote oxidative stress. Moreover, intense localization of both non-heme ferric and ferrous iron was observed in aggregated large stromal cells that were then characterized as ceroid-laden enlarged macrophages with frothy cytoplasm. Intraperitoneal iron overload in adult mice resulted in non-heme iron deposition in the entire stroma and generation of enlarged macrophages, suggesting that excessive iron accumulation induced macrophage morphological changes. The data indicated that non-heme iron accumulation in ovarian stromal tissue may be related to aging of the ovary due to increasing oxidative stress.
[Mh] Termos MeSH primário: Envelhecimento/metabolismo
Compostos Férricos/análise
Compostos Ferrosos/análise
Sobrecarga de Ferro/metabolismo
Macrófagos/metabolismo
Ovário/metabolismo
Estresse Oxidativo
[Mh] Termos MeSH secundário: Envelhecimento/patologia
Animais
Ceroide/biossíntese
Feminino
Compostos Férricos/metabolismo
Compostos Ferrosos/metabolismo
Seres Humanos
Sobrecarga de Ferro/induzido quimicamente
Sobrecarga de Ferro/patologia
Complexo Ferro-Dextran
Macrófagos/patologia
Camundongos
Camundongos Endogâmicos C57BL
Microscopia Eletrônica
Ovário/efeitos dos fármacos
Ovário/patologia
Oxirredução
Estresse Oxidativo/efeitos dos fármacos
Perfusão
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ceroid); 0 (Ferric Compounds); 0 (Ferrous Compounds); 9004-66-4 (Iron-Dextran Complex)
[Em] Mês de entrada:1204
[Cu] Atualização por classe:150129
[Lr] Data última revisão:
150129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:111124
[St] Status:MEDLINE
[do] DOI:10.1369/0022155411431734


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[PMID]:21804079
[Au] Autor:Tohma H; Hepworth AR; Shavlakadze T; Grounds MD; Arthur PG
[Ad] Endereço:School of Biomedical, Biomolecular & Chemical Science, The University of Western Australia, Crawley, Western Australia.
[Ti] Título:Quantification of ceroid and lipofuscin in skeletal muscle.
[So] Source:J Histochem Cytochem;59(8):769-79, 2011 Aug.
[Is] ISSN:1551-5044
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ceroid and lipofuscin are autofluorescent granules thought to be generated as a consequence of chronic oxidative stress. Because ceroid and lipofuscin are persistent in tissue, their measurement can provide a lifetime history of exposure to chronic oxidative stress. Although ceroid and lipofuscin can be measured by quantification of autofluorescent granules, current methods rely on subjective assessment. Furthermore, there has not been any evaluation of variables affecting quantitative measurements. The article describes a simple statistical approach that can be readily applied to quantitate ceroid and lipofuscin. Furthermore, it is shown that several factors, including magnification tissue thickness and tissue level, can affect precision and sensitivity. After optimizing for these factors, the authors show that ceroid and lipofuscin can be measured reproducibly in the skeletal muscle of dystrophic mice (ceroid) and aged mice (lipofuscin).
[Mh] Termos MeSH primário: Ceroide/análise
Lipofuscina/análise
Músculo Quadríceps/química
[Mh] Termos MeSH secundário: Envelhecimento/metabolismo
Animais
Interpretação Estatística de Dados
Feminino
Fluorescência
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Endogâmicos mdx
Distrofia Muscular de Duchenne/metabolismo
Distrofia Muscular de Duchenne/patologia
Músculo Quadríceps/patologia
Sensibilidade e Especificidade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ceroid); 0 (Lipofuscin)
[Em] Mês de entrada:1109
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110802
[St] Status:MEDLINE
[do] DOI:10.1369/0022155411412185


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[PMID]:21280898
[Au] Autor:Haka AS; Kramer JR; Dasari RR; Fitzmaurice M
[Ad] Endereço:Massachusetts Institute of Technology, G. R. Harrison Spectroscopy Laboratory, Cambridge, Massachusetts 02139, USA. abh2005@med.cornell.edu
[Ti] Título:Mechanism of ceroid formation in atherosclerotic plaque: in situ studies using a combination of Raman and fluorescence spectroscopy.
[So] Source:J Biomed Opt;16(1):011011, 2011 Jan-Feb.
[Is] ISSN:1560-2281
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Accumulation of the lipid-protein complex ceroid is a characteristic of atherosclerotic plaque. The mechanism of ceroid formation has been extensively studied, because the complex is postulated to contribute to plaque irreversibility. Despite intensive research, ceroid deposits are defined through their fluorescence and histochemical staining properties, while their composition remains unknown. Using Raman and fluorescence spectral microscopy, we examine the composition of ceroid in situ in aorta and coronary artery plaque. The synergy of these two types of spectroscopy allows for identification of ceroid via its fluorescence signature and elucidation of its chemical composition through the acquisition of a Raman spectrum. In accordance with in vitro predictions, low density lipoprotein (LDL) appears within the deposits primarily in its peroxidized form. The main forms of modified LDL detected in both coronary artery and aortic plaques are peroxidation products from the Fenton reaction and myeloperoxidase-hypochlorite pathway. These two peroxidation products occur in similar concentrations within the deposits and represent ∼40 and 30% of the total LDL (native and peroxidized) in the aorta and coronary artery deposits, respectively. To our knowledge, this study is the first to successfully employ Raman spectroscopy to unravel a metabolic pathway involved in disease pathogenesis: the formation of ceroid in atherosclerotic plaque.
[Mh] Termos MeSH primário: Biomarcadores/análise
Ceroide/análise
Placa Aterosclerótica/química
Placa Aterosclerótica/diagnóstico
Espectrometria de Fluorescência/instrumentação
Análise Espectral Raman/instrumentação
[Mh] Termos MeSH secundário: Desenho de Equipamento
Análise de Falha de Equipamento
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biomarkers); 0 (Ceroid)
[Em] Mês de entrada:1105
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110202
[St] Status:MEDLINE
[do] DOI:10.1117/1.3524304


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[PMID]:21210766
[Au] Autor:Dunlop RA; Brunk UT; Rodgers KJ
[Ad] Endereço:Cell Biology Group, Heart Research Institute, 7 Eliza Street, Newtown, NSW 2042, Australia. dunlopr@hri.org.au
[Ti] Título:Proteins containing oxidized amino acids induce apoptosis in human monocytes.
[So] Source:Biochem J;435(1):207-16, 2011 Apr 01.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cellular deposits of oxidized and aggregated proteins are hallmarks of a variety of age-related disorders, but whether such proteins contribute to pathology is not well understood. We previously reported that oxidized proteins form lipofuscin/ceroid-like bodies with a lysosomal-type distribution and up-regulate the transcription and translation of proteolytic lysosomal enzymes in cultured J774 mouse macrophages. Given the recently identified role of lysosomes in the induction of apoptosis, we have extended our studies to explore a role for oxidized proteins in apoptosis. Oxidized proteins were biosynthetically generated in situ by substituting oxidized analogues for parent amino acids. Apoptosis was measured with Annexin-V/PI (propidium iodide), TUNEL (terminal deoxynucleotidyltransferase-mediated dUTP nick-end labelling), MMP (mitochondrial membrane permeabilization), caspase activation and cytochrome c release, and related to lysosomal membrane permeabilization. Synthesized proteins containing the tyrosine oxidation product L-DOPA (L-3,4-dihydroxyphenylalanine) were more potent inducers of apoptosis than proteins containing the phenylalanine oxidation product o-tyrosine. Apoptosis was dependent upon incorporation of oxidized residues, as indicated by complete abrogation in cultures incubated with the non-incorporation control D-DOPA (D-3,4-dihydroxyphenylalanine) or when incorporation was competed out by parent amino acids. The findings of the present study suggest that certain oxidized proteins could play an active role in the progression of age-related disorders by contributing to LMP (lysosomal membrane permeabilization)-initiated apoptosis and may have important implications for the long-term use of L-DOPA as a therapeutic agent in Parkinson's disease.
[Mh] Termos MeSH primário: Apoptose
Levodopa/efeitos adversos
Levodopa/metabolismo
Monócitos/metabolismo
Biossíntese de Proteínas
Tirosina/efeitos adversos
Tirosina/metabolismo
[Mh] Termos MeSH secundário: Envelhecimento
Anexina A5/metabolismo
Caspase 3/metabolismo
Linhagem Celular
Ceroide/efeitos adversos
Fragmentação do DNA
Ativação Enzimática
Seres Humanos
Membranas Intracelulares
Lipofuscina/efeitos adversos
Lisossomos
Potencial da Membrana Mitocondrial
Membranas Mitocondriais
Oxirredução
Permeabilidade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Annexin A5); 0 (Ceroid); 0 (Lipofuscin); 42HK56048U (Tyrosine); 46627O600J (Levodopa); 709-16-0 (2-tyrosine); EC 3.4.22.- (CASP3 protein, human); EC 3.4.22.- (Caspase 3)
[Em] Mês de entrada:1105
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110108
[St] Status:MEDLINE
[do] DOI:10.1042/BJ20100682


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[PMID]:20489146
[Au] Autor:Shevtsova Z; Garrido M; Weishaupt J; Saftig P; Bähr M; Lühder F; Kügler S
[Ad] Endereço:Department of Neurology, University Medicine Göttingen, Waldweg 33, 37073 Göttingen, Germany.
[Ti] Título:CNS-expressed cathepsin D prevents lymphopenia in a murine model of congenital neuronal ceroid lipofuscinosis.
[So] Source:Am J Pathol;177(1):271-9, 2010 Jul.
[Is] ISSN:1525-2191
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Deficiency in Cathepsin D (CtsD), the major cellular lysosomal aspartic proteinase, causes the congenital form of neuronal ceroid lipofuscinoses (NCLs). CtsD-deficient mice show severe visceral lesions like lymphopenia in addition to their central nervous system (CNS) phenotype of ceroid accumulation, microglia activation, and seizures. Here we demonstrate that re-expression of CtsD within the CNS but not re-expression of CtsD in visceral organs prevented both central and visceral pathologies of CtsD(-/-) mice. Our results suggest that CtsD was substantially secreted from CNS neurons and drained from CNS to periphery via lymphatic routes. Through this drainage, CNS-expressed CtsD acts as an important modulator of immune system maintenance and peripheral tissue homeostasis. These effects depended on enzymatic activity and not on proposed functions of CtsD as an extracellular ligand. Our results furthermore demonstrate that the prominent accumulation of ceroid/lipofuscin and activation of microglia in brains of CtsD(-/-) are not lethal factors but can be tolerated by the rodent CNS.
[Mh] Termos MeSH primário: Catepsina D/metabolismo
Sistema Nervoso Central/metabolismo
Modelos Animais de Doenças
Linfopenia/metabolismo
Lipofuscinoses Ceroides Neuronais/metabolismo
[Mh] Termos MeSH secundário: Animais
Catepsina D/genética
Sistema Nervoso Central/patologia
Ceroide/metabolismo
Dependovirus/genética
Dependovirus/metabolismo
Vetores Genéticos
Seres Humanos
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Microglia/metabolismo
Lipofuscinoses Ceroides Neuronais/patologia
Neurônios/metabolismo
Taxa de Sobrevida
Timo/citologia
Distribuição Tecidual
Vísceras/metabolismo
Vísceras/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ceroid); EC 3.4.23.5 (Cathepsin D)
[Em] Mês de entrada:1012
[Cu] Atualização por classe:141203
[Lr] Data última revisão:
141203
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:100522
[St] Status:MEDLINE
[do] DOI:10.2353/ajpath.2010.091267



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