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[PMID]:28892514
[Au] Autor:El-Hamoly T; El-Sharawy DM; El Refaye MS; Abd El-Rahman SS
[Ad] Endereço:Drug Radiation Research Department, National Center for Radiation Research and Technology, Atomic Energy Authority, Cairo, Egypt.
[Ti] Título:L-thyroxine modifies nephrotoxicity by regulating the apoptotic pathway: The possible role of CD38/ADP-ribosyl cyclase-mediated calcium mobilization.
[So] Source:PLoS One;12(9):e0184157, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Thyroid hormones are well-established as a key regulator of many cellular metabolic pathways developed in various pathogeneses. Here, we dedicated the current work to investigate the role of thyroid hormone analogue (L-thyroxine, L-TH) in regulating the renal cytotoxicity using in vivo and in vitro models. Swiss mice were exposed to gamma radiation (IRR, 6Gy) or treated with cisplatin (CIS, 15 mg/kg, i.p.) for induction of nephrotoxicity. Remarkably, pretreatment with L-TH (1µg/kg) ameliorated the elevated kidney function biomarkers, oxidative stress and protected the renal tissue from the subsequent cellular damage. Likewise, L-TH inhibited the apoptotic cascade by down-regulating the extreme consumption of the cellular energy (ATP), the expression of caspase-3 and Bax, and the stimulation of cyclic ADP ribose (cADPR)/calcium mobilization. Moreover, incubation with L-TH (120nM/4h) significantly blocked the cytotoxicity of CIS on Vero cells and the depletion of NAD+ content as well as modified the ADP-ribose cyclase (CD38) enzymatic activity. High doses of L-TH (up to30 nM/4h) inversely increased the radiosensitivity of Vero cells towards IRR (up to 6Gy). On the other hand, L-TH did not interfere CIS-induced cytotoxicity of colorectal adenocarcinoma (Caco-2) cell line. In conclusion, pretreatment with L-TH could be a promising protective approach to the renal cellular damage induced during either CIS or IRR therapy by regulating the unbalanced oxidative status, the expression of pro-apoptotic biomarkers via modulation of cADPR mediated-calcium mobilization.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Rim/efeitos dos fármacos
Rim/metabolismo
Substâncias Protetoras/farmacologia
Transdução de Sinais/efeitos dos fármacos
Tiroxina/farmacologia
[Mh] Termos MeSH secundário: ADP-Ribosil Ciclase/metabolismo
ADP-Ribosil Ciclase 1/metabolismo
Animais
Biomarcadores
Cálcio/metabolismo
Sobrevivência Celular/efeitos dos fármacos
Cercopithecus aethiops
Fragmentação do DNA/efeitos dos fármacos
Rim/patologia
Rim/efeitos da radiação
Testes de Função Renal
Masculino
Camundongos
Mitocôndrias/metabolismo
Modelos Animais
Estresse Oxidativo/efeitos dos fármacos
Células Vero
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Protective Agents); EC 3.2.2.5 (ADP-ribosyl Cyclase); EC 3.2.2.6 (ADP-ribosyl Cyclase 1); Q51BO43MG4 (Thyroxine); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170912
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184157


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[PMID]:28340569
[Au] Autor:Higashida H; Liang M; Yoshihara T; Akther S; Fakhrul A; Stanislav C; Nam TS; Kim UH; Kasai S; Nishimura T; Al Mahmuda N; Yokoyama S; Ishihara K; Gerasimenko M; Salmina A; Zhong J; Tsuji T; Tsuji C; Lopatina O
[Ad] Endereço:Research Centre for Child Mental Development, Kanazawa University, Kanazawa, 920-8640, Japan. haruhiro@med.kanazawa-u.ac.jp.
[Ti] Título:An immunohistochemical, enzymatic, and behavioral study of CD157/BST-1 as a neuroregulator.
[So] Source:BMC Neurosci;18(1):35, 2017 Mar 24.
[Is] ISSN:1471-2202
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Recent rodent and human studies provide evidence in support of the fact that CD157, well known as bone marrow stromal cell antigen-1 (BST-1) and a risk factor in Parkinson's disease, also meaningfully acts in the brain as a neuroregulator and affects social behaviors. It has been shown that social behaviors are impaired in CD157 knockout mice without severe motor dysfunction and that CD157/BST1 gene single nucleotide polymorphisms are associated with autism spectrum disorder in humans. However, it is still necessary to determine how this molecule contributes to the brain's physiological and pathophysiological functions. METHODS: To gain fresh insights about the relationship between the presence of CD157 in the brain and its enzymatic activity, and aberrant social behavior, CD157 knockout mice of various ages were tested. RESULTS: CD157 immunoreactivity colocalized with nestin-positive cells and elements in the ventricular zones in E17 embryos. Brain CD157 mRNA levels were high in neonates but low in adults. Weak but distinct immunoreactivity was detected in several areas in the adult brain, including the amygdala. CD157 has little or no base exchange activity, but some ADP-ribosyl cyclase activity, indicating that CD157 formed cyclic ADP-ribose but much less nicotinic acid adenine dinucleotide phosphate, with both mobilizing Ca from intracellular Ca pools. Social avoidance in CD157 knockout mice was rescued by a single intraperitoneal injection of oxytocin. CONCLUSIONS: CD157 may play a role in the embryonic and adult nervous systems. The functional features of CD157 can be explained in part through the production of cyclic ADP-ribose rather than nicotinic acid adenine dinucleotide phosphate. Further experiments are required to elucidate how the embryonic expression of CD157 in neural stem cells contributes to behaviors in adults or to psychiatric symptoms.
[Mh] Termos MeSH primário: ADP-Ribosil Ciclase/metabolismo
Antígenos CD/metabolismo
Encéfalo/enzimologia
Comportamento Social
[Mh] Termos MeSH secundário: ADP-Ribosil Ciclase/genética
ADP-Ribosil Ciclase 1/genética
ADP-Ribosil Ciclase 1/metabolismo
Animais
Animais Recém-Nascidos
Antígenos CD/genética
Aprendizagem da Esquiva/fisiologia
Encéfalo/embriologia
Encéfalo/crescimento & desenvolvimento
ADP-Ribose Cíclica/metabolismo
Proteínas Ligadas por GPI/genética
Proteínas Ligadas por GPI/metabolismo
Células HEK293
Seres Humanos
Imuno-Histoquímica
Masculino
Glicoproteínas de Membrana/genética
Glicoproteínas de Membrana/metabolismo
Camundongos Endogâmicos C57BL
Camundongos Endogâmicos ICR
Camundongos Knockout
Modelos Animais
NADP/análogos & derivados
NADP/metabolismo
Nestina/metabolismo
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD); 0 (GPI-Linked Proteins); 0 (Membrane Glycoproteins); 0 (Nes protein, mouse); 0 (Nestin); 0 (RNA, Messenger); 119340-53-3 (Cyclic ADP-Ribose); 53-59-8 (NADP); 5502-96-5 (NAADP); EC 3.2.2.5 (ADP-ribosyl Cyclase); EC 3.2.2.5 (ADP-ribosyl cyclase 2); EC 3.2.2.5 (Cd38 protein, mouse); EC 3.2.2.6 (ADP-ribosyl Cyclase 1)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170326
[St] Status:MEDLINE
[do] DOI:10.1186/s12868-017-0350-7


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[PMID]:28295574
[Au] Autor:Hattori T; Kaji M; Ishii H; Jureepon R; Takarada-Iemata M; Minh Ta H; Manh Le T; Konno A; Hirai H; Shiraishi Y; Ozaki N; Yamamoto Y; Okamoto H; Yokoyama S; Higashida H; Kitao Y; Hori O
[Ad] Endereço:Department of Neuroanatomy, Graduate School of Medical Sciences, Kanazawa University, Kanazawa, Ishikawa, Japan.
[Ti] Título:CD38 positively regulates postnatal development of astrocytes cell-autonomously and oligodendrocytes non-cell-autonomously.
[So] Source:Glia;65(6):974-989, 2017 Jun.
[Is] ISSN:1098-1136
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Glial development is critical for the function of the central nervous system. CD38 is a multifunctional molecule with ADP-ribosyl cyclase activity. While critical roles of CD38 in the adult brain such as oxytocin release and social behavior have been reported, those in the developing brain remain largely unknown. Here we demonstrate that deletion of Cd38 leads to impaired development of astrocytes and oligodendrocytes in mice. CD38 is highly expressed in the developing brains between postnatal day 14 (P14) and day 28 (P28). In situ hybridization and FACS analysis revealed that CD38 is expressed predominantly in astrocytes in these periods. Analyses of the cortex of Cd38 knockout (Cd38 ) mice revealed delayed development of astrocytes and subsequently delayed differentiation of oligodendrocytes (OLs) at postnatal stages. In vitro experiments using primary OL cultures, mixed glial cultures, and astrocytic conditioned medium showed that astrocytic CD38 regulates the development of astrocytes in a cell-autonomous manner and the differentiation of OLs in a non-cell-autonomous manner. Further experiments revealed that connexin43 (Cx43) in astrocytes plays a promotive role for CD38-mediated OL differentiation. Finally, increased levels of NAD , caused by CD38 deficiency, are likely to be responsible for the suppression of astrocytic Cx43 expression and OL differentiation. Our data indicate that CD38 is a positive regulator of astrocyte and OL development.
[Mh] Termos MeSH primário: ADP-Ribosil Ciclase 1/metabolismo
ADP-Ribosil Ciclase/metabolismo
Astrócitos/metabolismo
Encéfalo/crescimento & desenvolvimento
Encéfalo/metabolismo
Glicoproteínas de Membrana/metabolismo
Oligodendroglia/metabolismo
[Mh] Termos MeSH secundário: ADP-Ribosil Ciclase/genética
ADP-Ribosil Ciclase 1/genética
Animais
Astrócitos/citologia
Encéfalo/citologia
Diferenciação Celular/fisiologia
Células Cultivadas
Técnicas de Cocultura
Conexina 43/metabolismo
Feminino
Masculino
Glicoproteínas de Membrana/genética
Camundongos Endogâmicos ICR
Camundongos Knockout
NAD/metabolismo
Oligodendroglia/citologia
Ratos Wistar
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Connexin 43); 0 (GJA1 protein, mouse); 0 (Membrane Glycoproteins); 0U46U6E8UK (NAD); EC 3.2.2.5 (ADP-ribosyl Cyclase); EC 3.2.2.5 (Cd38 protein, mouse); EC 3.2.2.5 (Cd38 protein, rat); EC 3.2.2.6 (ADP-ribosyl Cyclase 1)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170316
[St] Status:MEDLINE
[do] DOI:10.1002/glia.23139


  4 / 1432 MEDLINE  
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[PMID]:27664703
[Au] Autor:Jiao C; Yang R; Gu Z
[Ad] Endereço:College of Food Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu 210095, People's Republic of China.
[Ti] Título:Cyclic ADP-ribose and IP3 mediate abscisic acid-induced isoflavone accumulation in soybean sprouts.
[So] Source:Biochem Biophys Res Commun;479(3):530-536, 2016 Oct 21.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this study, the roles of ABA-cADPR-Ca and ABA-IP3-Ca signaling pathways in UV-B-induced isoflavone accumulation in soybean sprouts were investigated. Results showed that abscisic acid (ABA) up regulated cyclic ADP-ribose (cADPR) and inositol 1,4,5-trisphosphate (IP3) levels in soybean sprouts under UV-B radiation. Furthermore, cADPR and IP3, as second messengers of UV-B-triggered ABA, induced isoflavone accumulation by up-regulating proteins and genes expression and activity of isoflavone biosynthetic-enzymes (chalcone synthase, CHS; isoflavone synthase, IFS). After Ca was chelated by EGTA, isoflavone content decreased. Overall, ABA-induced cADPR and IP3 up regulated isoflavone accumulation which was mediated by Ca signaling via enhancing the expression of proteins and genes participating in isoflavone biosynthesis in soybean sprouts under UV-B radiation.
[Mh] Termos MeSH primário: Ácido Abscísico/metabolismo
ADP-Ribose Cíclica/metabolismo
Inositol 1,4,5-Trifosfato/metabolismo
Feijão de Soja/metabolismo
[Mh] Termos MeSH secundário: ADP-Ribosil Ciclase/metabolismo
Cálcio/química
Cálcio/metabolismo
Quelantes/química
Perfilação da Expressão Gênica
Isoflavonas/química
Reação em Cadeia da Polimerase em Tempo Real
Sistemas do Segundo Mensageiro
Transdução de Sinais
Raios Ultravioleta
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chelating Agents); 0 (Isoflavones); 119340-53-3 (Cyclic ADP-Ribose); 72S9A8J5GW (Abscisic Acid); 85166-31-0 (Inositol 1,4,5-Trisphosphate); EC 3.2.2.5 (ADP-ribosyl Cyclase); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170827
[Lr] Data última revisão:
170827
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160925
[St] Status:MEDLINE


  5 / 1432 MEDLINE  
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[PMID]:27547294
[Au] Autor:Guan XH; Liu XH; Hong X; Zhao N; Xiao YF; Wang LF; Tang L; Jiang K; Qian YS; Deng KY; Ji G; Fu M; Xin HB
[Ad] Endereço:Institute of Translational Medicine, Nanchang University, Nanchang 330031, China.
[Ti] Título:CD38 Deficiency Protects the Heart from Ischemia/Reperfusion Injury through Activating SIRT1/FOXOs-Mediated Antioxidative Stress Pathway.
[So] Source:Oxid Med Cell Longev;2016:7410257, 2016.
[Is] ISSN:1942-0994
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ischemia/reperfusion (I/R) injury induces irreversible oxidative stress damage to the cardiac muscle. We previously observed that CD38 deficiency remarkably protects mouse embryonic fibroblasts (MEFs) from oxidative stress-induced injury. However, whether CD38 deficiency protects from I/R injury in the heart is not explored. Here, we showed that the hearts of CD38 deficient mice or wild type mice supplied with exogenous NAD were significantly protected from ischemia/reperfusion injury, seen as reduction of the myocardial infarct sizes when the mice were subjected to 30 min ischemia followed by 24 hours of reperfusion. Consistently, the protection of CD38 deficiency on hypoxia/reoxygenation (H/R) injury was confirmed with a CD38 knockdown H9c2 stable cell line. Furthermore, we observed that knockdown of CD38 remarkably inhibited ROS generation and intracellular Ca(2+) overloading induced by H/R in H9c2 cells. The FOXO1 and FOXO3 expressions were significantly elevated by H/R injury in CD38 knockdown cells compared with normal H9c2 cells. The cell immunofluorescence assay showed that FOXO1 nuclear translocation was significantly increased in CD38 knockdown H9c2 cells. In addition, we demonstrated that the increase of FOXO1 nuclear translocation was associated with the increased expressions of antioxidant catalase and SOD2 and the attenuated expression of the ROS generation enzyme NOX4. In conclusion, our results provide new evidence that CD38 deficiency protects the heart from I/R injury through activating SIRT1/FOXOs-mediated antioxidative stress pathway.
[Mh] Termos MeSH primário: ADP-Ribosil Ciclase 1/deficiência
ADP-Ribosil Ciclase/deficiência
Proteína Forkhead Box O3/metabolismo
Glicoproteínas de Membrana/deficiência
Infarto do Miocárdio/prevenção & controle
Traumatismo por Reperfusão Miocárdica/prevenção & controle
Miocárdio/enzimologia
Proteínas do Tecido Nervoso/metabolismo
Estresse Oxidativo
Sirtuína 1/metabolismo
[Mh] Termos MeSH secundário: ADP-Ribosil Ciclase/genética
ADP-Ribosil Ciclase 1/genética
Animais
Apoptose
Cálcio/metabolismo
Linhagem Celular
Modelos Animais de Doenças
Genótipo
Masculino
Glicoproteínas de Membrana/genética
Camundongos Endogâmicos C57BL
Camundongos Knockout
Infarto do Miocárdio/enzimologia
Infarto do Miocárdio/genética
Infarto do Miocárdio/patologia
Traumatismo por Reperfusão Miocárdica/enzimologia
Traumatismo por Reperfusão Miocárdica/genética
Traumatismo por Reperfusão Miocárdica/patologia
Miocárdio/patologia
NADPH Oxidase 4
NADPH Oxidases/metabolismo
Fenótipo
Interferência de RNA
Ratos
Espécies Reativas de Oxigênio/metabolismo
Transdução de Sinais
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Forkhead Box Protein O3); 0 (Foxo3a protein, rat); 0 (Membrane Glycoproteins); 0 (Nerve Tissue Proteins); 0 (Reactive Oxygen Species); 147604-79-3 (Foxo1 protein, rat); EC 1.6.3.- (NADPH Oxidase 4); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.- (Nox4 protein, rat); EC 3.2.2.5 (ADP-ribosyl Cyclase); EC 3.2.2.5 (Cd38 protein, mouse); EC 3.2.2.5 (Cd38 protein, rat); EC 3.2.2.6 (ADP-ribosyl Cyclase 1); EC 3.5.1.- (Sirt1 protein, rat); EC 3.5.1.- (Sirtuin 1); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160823
[St] Status:MEDLINE
[do] DOI:10.1155/2016/7410257


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[PMID]:27064071
[Au] Autor:Haikarainen T; Lehtiö L
[Ad] Endereço:Biocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, FI-90014 Oulu, Finland.
[Ti] Título:Proximal ADP-ribose Hydrolysis in Trypanosomatids is Catalyzed by a Macrodomain.
[So] Source:Sci Rep;6:24213, 2016 Apr 11.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:ADP-ribosylation is a ubiquitous protein modification utilized by both prokaryotes and eukaryotes for several cellular functions, such as DNA repair, proliferation, and cell signaling. Higher eukaryotes, such as humans, utilize various enzymes to reverse the modification and to regulate ADP-ribose dependent signaling. In contrast, some lower eukaryotes, including trypanosomatids, lack many of these enzymes and therefore have a much more simplified ADP-ribose metabolism. Here we identified and characterized ADP-ribose hydrolases from Trypanosoma brucei and Trypanosoma cruzi, which are homologous to human O-acetyl-ADP-ribose deacetylases MacroD1 and MacroD2. The enzymes are capable for hydrolysis of protein linked ADP-ribose and a product of sirtuin-mediated lysine deacetylation, O-acetyl-ADP-ribose. Crystal structures of the trypanosomatid macrodomains revealed a conserved catalytic site with distinct differences to human MacroD1 and MacroD2.
[Mh] Termos MeSH primário: ADP-Ribosil Ciclase/metabolismo
Proteínas de Protozoários/metabolismo
Trypanosoma brucei brucei/enzimologia
Trypanosoma cruzi/enzimologia
[Mh] Termos MeSH secundário: ADP-Ribosil Ciclase/química
ADP-Ribosil Ciclase/genética
Adenosina Difosfato Ribose/metabolismo
Sequência de Aminoácidos
Sítios de Ligação
Biocatálise
Calorimetria
Domínio Catalítico
Cristalografia por Raios X
Seres Humanos
Hidrolases/química
Hidrolases/metabolismo
Hidrólise
Dados de Sequência Molecular
Estrutura Terciária de Proteína
Proteínas de Protozoários/química
Proteínas de Protozoários/genética
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/química
Proteínas Recombinantes/isolamento & purificação
Alinhamento de Sequência
Sirtuínas/metabolismo
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Protozoan Proteins); 0 (Recombinant Proteins); 20762-30-5 (Adenosine Diphosphate Ribose); EC 3.- (Hydrolases); EC 3.2.2.5 (ADP-ribosyl Cyclase); EC 3.5.1.- (Sirtuins)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170302
[Lr] Data última revisão:
170302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160412
[St] Status:MEDLINE
[do] DOI:10.1038/srep24213


  7 / 1432 MEDLINE  
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[PMID]:27020835
[Au] Autor:Peng QY; Ai ML; Zhang LN; Zou Y; Ma XH; Ai YH
[Ad] Endereço:Department of Critical Care Medicine, Xiang-Ya Hospital, Central South University, Changsha, Hunan Province, China.
[Ti] Título:Blocking NAD(+)/CD38/cADPR/Ca(2+) pathway in sepsis prevents organ damage.
[So] Source:J Surg Res;201(2):480-9, 2016 Apr.
[Is] ISSN:1095-8673
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Although the nicotinamide adenine dinucleotide (NAD(+))/CD38/cyclic ADP ribose (cADPR)/Ca(2+) signaling pathway has been shown to regulate intracellular calcium homeostasis and functions in multiple inflammatory processes, its role in sepsis remains unknown. The aim of this study was to determine whether the NAD(+)/CD38/cADPR/Ca(2+) signaling pathway is activated during sepsis and whether an inhibitor of this pathway, 8-Br-cADPR, protects the organs from sepsis-induced damage. MATERIALS AND METHODS: Male Sprague-Dawley rats were subjected to cecal ligation and puncture (CLP) or sham laparotomies. NAD(+), cADPR, CD38, and intracellular Ca(2+) levels were measured in the hearts, livers, and kidneys of septic rats at 0, 6, 12, 24, and 48 h after CLP surgery. Rats were also divided into sham, CLP, and CLP+8-Br-cADPR groups, and the hearts, livers, and kidneys were hematoxylin-eosin-stained and assayed for malondialdehyde and superoxide dismutase activities. RESULTS: NAD(+), cADPR, CD38, and intracellular Ca(2+) levels increased in the hearts, livers, and kidneys of septic rats as early as 6-24 h after CLP surgery. Treatment with 8-Br-cADPR inhibited sepsis-induced intracellular Ca(2+) mobilization, attenuated tissue injury, reduced malondialdehyde levels, and increased superoxide dismutase activity in septic rats. CONCLUSIONS: The NAD(+)/CD38/cADPR/Ca(2+) signaling pathway was activated during sepsis in the CLP rat model. Blocking this pathway with 8-Br-cADPR protected hearts, livers, and kidneys from sepsis-induced damage.
[Mh] Termos MeSH primário: Sinalização do Cálcio/efeitos dos fármacos
ADP-Ribose Cíclica/análogos & derivados
Insuficiência de Múltiplos Órgãos/prevenção & controle
Sepse/complicações
[Mh] Termos MeSH secundário: ADP-Ribosil Ciclase/metabolismo
ADP-Ribosil Ciclase 1/metabolismo
Animais
Cálcio/metabolismo
ADP-Ribose Cíclica/metabolismo
ADP-Ribose Cíclica/farmacologia
ADP-Ribose Cíclica/uso terapêutico
Modelos Animais de Doenças
Avaliação Pré-Clínica de Medicamentos
Masculino
Malondialdeído/metabolismo
Glicoproteínas de Membrana/metabolismo
Insuficiência de Múltiplos Órgãos/etiologia
NAD/metabolismo
Distribuição Aleatória
Ratos Sprague-Dawley
Sepse/metabolismo
Superóxido Dismutase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (8-bromo-cyclic-ADP-ribose); 0 (Membrane Glycoproteins); 0U46U6E8UK (NAD); 119340-53-3 (Cyclic ADP-Ribose); 4Y8F71G49Q (Malondialdehyde); EC 1.15.1.1 (Superoxide Dismutase); EC 3.2.2.5 (ADP-ribosyl Cyclase); EC 3.2.2.5 (Cd38 protein, rat); EC 3.2.2.6 (ADP-ribosyl Cyclase 1); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160330
[St] Status:MEDLINE


  8 / 1432 MEDLINE  
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[PMID]:26947077
[Au] Autor:Sitnik KM; Wendland K; Weishaupt H; Uronen-Hansson H; White AJ; Anderson G; Kotarsky K; Agace WW
[Ad] Endereço:Section for Immunology and Vaccinology, National Veterinary Institute, Technical University of Denmark, Bülowsvej 27, 1870 Frederiksberg C, Denmark. Electronic address: kasit@vet.dtu.dk.
[Ti] Título:Context-Dependent Development of Lymphoid Stroma from Adult CD34(+) Adventitial Progenitors.
[So] Source:Cell Rep;14(10):2375-88, 2016 Mar 15.
[Is] ISSN:2211-1247
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Despite the key role of primary and secondary lymphoid organ stroma in immunity, our understanding of the heterogeneity and ontogeny of these cells remains limited. Here, we identify a functionally distinct subset of BP3(-)PDPN(+)PDGFRß(+)/α(+)CD34(+) stromal adventitial cells in both lymph nodes (LNs) and thymus that is located within the vascular niche surrounding PDPN(-)PDGFRß(+)/α(-)Esam-1(+)ITGA7(+) pericytes. CD34(+) adventitial cells developed in late embryonic thymus and in postnatal LNs and in the thymus originated, along with pericytes, from a common anlage-seeding progenitor population. Using lymphoid organ re-aggregate grafts, we demonstrate that adult CD34(+) adventitial cells are capable of differentiating into multiple lymphoid stroma-like subsets including pericyte-, FRC-, MRC-, and FDC-like cells, the development of which was lymphoid environment-dependent. These findings extend the current understanding of lymphoid mesenchymal cell heterogeneity and highlight a role of the CD34(+) adventitia as a potential ubiquitous source of lymphoid stromal precursors in postnatal tissues.
[Mh] Termos MeSH primário: Antígenos CD34/metabolismo
Células Estromais/metabolismo
[Mh] Termos MeSH secundário: ADP-Ribosil Ciclase/genética
ADP-Ribosil Ciclase/metabolismo
Animais
Antígenos CD/genética
Antígenos CD/metabolismo
Diferenciação Celular
Células Cultivadas
Embrião de Mamíferos/citologia
Embrião de Mamíferos/metabolismo
Citometria de Fluxo
Proteínas Ligadas por GPI/genética
Proteínas Ligadas por GPI/metabolismo
Imuno-Histoquímica
Linfonodos/citologia
Linfonodos/metabolismo
Receptor beta de Linfotoxina/deficiência
Receptor beta de Linfotoxina/genética
Receptor beta de Linfotoxina/metabolismo
Glicoproteínas de Membrana/genética
Glicoproteínas de Membrana/metabolismo
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Pericitos/citologia
Pericitos/metabolismo
Receptor beta de Fator de Crescimento Derivado de Plaquetas/genética
Receptor beta de Fator de Crescimento Derivado de Plaquetas/metabolismo
Transdução de Sinais
Células Estromais/citologia
Timo/citologia
Timo/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antigens, CD); 0 (Antigens, CD34); 0 (GPI-Linked Proteins); 0 (Gp38 protein, mouse); 0 (Ltbr protein, mouse); 0 (Lymphotoxin beta Receptor); 0 (Membrane Glycoproteins); EC 2.7.10.1 (Receptor, Platelet-Derived Growth Factor beta); EC 3.2.2.5 (ADP-ribosyl Cyclase); EC 3.2.2.5 (ADP-ribosyl cyclase 2)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160308
[St] Status:MEDLINE


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[PMID]:26660500
[Au] Autor:Ting KY; Leung CF; Graeff RM; Lee HC; Hao Q; Kotaka M
[Ad] Endereço:School of Life Sciences, the Chinese University of Hong Kong, Hong Kong.
[Ti] Título:Porcine CD38 exhibits prominent secondary NAD(+) cyclase activity.
[So] Source:Protein Sci;25(3):650-61, 2016 Mar.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cyclic ADP-ribose (cADPR) mobilizes intracellular Ca(2+) stores and activates Ca(2+) influx to regulate a wide range of physiological processes. It is one of the products produced from the catalysis of NAD(+) by the multifunctional CD38/ADP-ribosyl cyclase superfamily. After elimination of the nicotinamide ring by the enzyme, the reaction intermediate of NAD(+) can either be hydrolyzed to form linear ADPR or cyclized to form cADPR. We have previously shown that human CD38 exhibits a higher preference towards the hydrolysis of NAD(+) to form linear ADPR while Aplysia ADP-ribosyl cyclase prefers cyclizing NAD(+) to form cADPR. In this study, we characterized the enzymatic properties of porcine CD38 and revealed that it has a prominent secondary NAD(+) cyclase activity producing cADPR. We also determined the X-ray crystallographic structures of porcine CD38 and were able to observe conformational flexibility at the base of the active site of the enzyme which allow the NAD(+) reaction intermediate to adopt conformations resulting in both hydrolysis and cyclization forming linear ADPR and cADPR respectively.
[Mh] Termos MeSH primário: ADP-Ribosil Ciclase 1/metabolismo
NAD/metabolismo
[Mh] Termos MeSH secundário: ADP-Ribosil Ciclase/química
ADP-Ribosil Ciclase/metabolismo
ADP-Ribosil Ciclase 1/química
Sequência de Aminoácidos
Animais
Cristalografia por Raios X
ADP-Ribose Cíclica/metabolismo
Seres Humanos
Modelos Moleculares
Domínios Proteicos
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0U46U6E8UK (NAD); 119340-53-3 (Cyclic ADP-Ribose); EC 3.2.2.5 (ADP-ribosyl Cyclase); EC 3.2.2.6 (ADP-ribosyl Cyclase 1)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151215
[St] Status:MEDLINE
[do] DOI:10.1002/pro.2859


  10 / 1432 MEDLINE  
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[PMID]:26490516
[Au] Autor:Carulli G; Marini A; Sammuri P; Domenichini C; Ottaviano V; Pacini S; Petrini M
[Ad] Endereço:Division of Hematology , Department of Clinical and Experimental Medicine, University of Pisa.
[Ti] Título:Combination of CD157 and FLAER to Detect Peripheral Blood Eosinophils by Multiparameter Flow Cytometry.
[So] Source:J Clin Exp Hematop;55(2):55-60, 2015.
[Is] ISSN:1880-9952
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:The identification of eosinophils by flow cytometry is difficult because most of the surface antigens expressed by eosinophils are shared with neutrophils. Some methods have been proposed, generally based on differential light scatter properties, enhanced autofluorescence, lack of CD16 or selective positivity of CD52. Such methods, however, show several limitations. In the present study we report a novel method based on the analysis of glycosylphosphatidylinositol (GPI)-linked molecules. The combination of CD157 and FLAER was used, since FLAER recognizes all GPI-linked molecules, while CD157 is absent on the membrane of eosinophils and expressed by neutrophils. Peripheral blood samples from normal subjects and patients with variable percentages of eosinophils (n = 31), and without any evidence for circulating immature myeloid cells, were stained with the combination of FLAER-Alexa Fluor and CD157-PE. A FascCanto II cytometer was used. Granulocytes were gated after CD33 staining and eosinophils were identified as CD157(-)/FLAER(+) events. Neutrophils were identified as CD157(+)/FLAER(+) events. The percentages of eosinophils detected by this method showed a very significant correlation both with automated counting and with manual counting (r = 0.981 and 0.989, respectively). Sorting assays were carried out by a S3 Cell Sorter: cytospins obtained from CD157(-)/FLAER(+) events consisted of 100% eosinophils, while samples from CD157(+)/FLAER(+) events were represented only by neutrophils. In conclusion, this method shows high sensitivity and specificity in order to distinguish eosinophils from neutrophils by flow cytometry. However, since CD157 is gradually up-regulated throughout bone marrow myeloid maturation, our method cannot be applied to cases characterized by immature myeloid cells.
[Mh] Termos MeSH primário: ADP-Ribosil Ciclase/química
Antígenos CD/química
Toxinas Bacterianas/química
Eosinófilos/citologia
Citometria de Fluxo/métodos
Proteínas Citotóxicas Formadoras de Poros/química
[Mh] Termos MeSH secundário: Antígenos CD/metabolismo
Antígenos de Neoplasias/metabolismo
Antígeno CD52
Eosinófilos/metabolismo
Feminino
Proteínas Ligadas por GPI/química
Proteínas Ligadas por GPI/metabolismo
Glicoproteínas/metabolismo
Seres Humanos
Masculino
Receptores de IgG/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antigens, CD); 0 (Antigens, Neoplasm); 0 (Bacterial Toxins); 0 (CD52 Antigen); 0 (CD52 protein, human); 0 (FCGR3B protein, human); 0 (GPI-Linked Proteins); 0 (Glycoproteins); 0 (Pore Forming Cytotoxic Proteins); 0 (Receptors, IgG); 53126-24-2 (aerolysin); EC 3.2.2.5 (ADP-ribosyl Cyclase); EC 3.2.2.5 (ADP-ribosyl cyclase 2)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151023
[St] Status:MEDLINE
[do] DOI:10.3960/jslrt.55.55



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