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[PMID]:28444927
[Au] Autor:Iwamoto S; Kasahara Y; Yoshimura Y; Seko A; Takeda Y; Ito Y; Totani K; Matsuo I
[Ad] Endereço:Graduate School of Science and Technology, Gunma University, 1-5-1, Tenjin-cho, Kiryu, Gunma, 376-8515, Japan.
[Ti] Título:Endo-α-Mannosidase-Catalyzed Transglycosylation.
[So] Source:Chembiochem;18(14):1376-1378, 2017 Jul 18.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:In order for facilitating the synthesis of oligosaccharides, transglycosylation reactions mediated by glycoside hydrolases have been studied in various contexts. In this study, we examined the transglycosylating activity of a Golgi endo-α-mannosidase. We prepared various glycosyl donors and acceptors, and recombinant human Golgi endo-α-mannosidase and its various mutants were expressed. The enzyme was able to mediate transglycosylation from α-glycosyl-fluorides. Systematic screening of various point mutants revealed that the E407D mutant had excellent transglycosylation activity and extremely low hydrolytic activity. Substrate specificity analysis revealed that minimum motif required for glycosyl acceptor is Manα1- 2Man. The synthetic utility of the enzyme was demonstrated by generation of a high-mannose-type undecasaccharide (Glc Man GlcNAc ).
[Mh] Termos MeSH primário: Biocatálise
Oligossacarídeos/metabolismo
alfa-Manosidase/metabolismo
[Mh] Termos MeSH secundário: Glicosilação
Seres Humanos
Conformação Molecular
Oligossacarídeos/química
Especificidade por Substrato
alfa-Manosidase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Oligosaccharides); EC 3.2.1.24 (alpha-Mannosidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170427
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700111


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[PMID]:28284660
[Au] Autor:Jiao J; Wang S; Zhang R; Ma Z; Du G; Chen X; Tao D; Zhao J
[Ad] Endereço:Yingkou Institute of Technology, 115014, China; College of Animal Science, Tarim University, Alar, Xinjiang, 843300, China.
[Ti] Título:iTRAQ-based quantitative proteomics discovering potential serum biomarkers in locoweed poisoned rabbits.
[So] Source:Chem Biol Interact;268:111-118, 2017 Apr 25.
[Is] ISSN:1872-7786
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Locoism threatens the sustainable development of animal husbandry in areas around the world with intensified desertification, especially in the western United States, western China, Canada, and Mexico, among other countries. This study was conducted to discover potential serum biomarkers in locoweed-poisoned rabbits and lay a foundation for early diagnosis of locoism. We performed iTRAQ labeling coupled with two-dimensional liquid chromatography-tandem mass spectrometry (2D LC-MS/MS), comparing locoweed-poisoned rabbits and healthy controls. A total of 78 differentially-expressed proteins (fold change > 1.5 or < 0.67) were identified in the locoweed-poisoned rabbits compared to healthy controls. We found that 57.70% of differentially-expressed proteins were functionally related, and through bioinformatics analysis, we were able to construct a network mainly in complement and coagulation cascades. Significant differences in thrombospondin 4 (THBS4), kininogen 1 (KNG1), hemoglobin (HBB), and complement factor I (CFI) between locoweed poisoned animals and controls were found (P < 0.05) and validated by western blotting. These results suggested that locoweed could damage neurocytes, lower immunity, and form thrombi in rabbits. Our study proposes potential biomarkers for locoism diagnosis and also provides a new experimental basis to understand the pathogenesis of locoism.
[Mh] Termos MeSH primário: Proteínas Sanguíneas/análise
Oxytropis/envenenamento
Proteoma/análise
[Mh] Termos MeSH secundário: Animais
Biomarcadores/sangue
Feminino
Masculino
Proteômica
Coelhos
Swainsonina/farmacologia
alfa-Manosidase/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Blood Proteins); 0 (Proteome); EC 3.2.1.24 (alpha-Mannosidase); RSY4RK37KQ (Swainsonine)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170425
[Lr] Data última revisão:
170425
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170313
[St] Status:MEDLINE


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[PMID]:28245430
[Au] Autor:Chen ZH; Yu YP; Tao J; Liu S; Tseng G; Nalesnik M; Hamilton R; Bhargava R; Nelson JB; Pennathur A; Monga SP; Luketich JD; Michalopoulos GK; Luo JH
[Ad] Endereço:Department of Pathology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania.
[Ti] Título:MAN2A1-FER Fusion Gene Is Expressed by Human Liver and Other Tumor Types and Has Oncogenic Activity in Mice.
[So] Source:Gastroenterology;153(4):1120-1132.e15, 2017 Oct.
[Is] ISSN:1528-0012
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND & AIMS: Human tumors and liver cancer cell lines express the product of a fusion between the first 13 exons in the mannosidase α class 2A member 1 gene (MAN2A1) and the last 6 exons in the FER tyrosine kinase gene (FER), called MAN2A1-FER. We investigated whether MAN2A1-FER is expressed by human liver tumors and its role in liver carcinogenesis. METHODS: We performed reverse transcription polymerase chain reaction analyses of 102 non-small cell lung tumors, 61 ovarian tumors, 70 liver tumors, 156 glioblastoma multiform samples, 27 esophageal adenocarcinomas, and 269 prostate cancer samples, as well as 10 nontumor liver tissues and 20 nontumor prostate tissues, collected at the University of Pittsburgh. We also measured expression by 15 human cancer cell lines. We expressed a tagged form of MAN2A1-FER in NIH3T3 and HEP3B (liver cancer) cells; Golgi were isolated for analysis. MAN2A1-FER was also overexpressed in PC3 or DU145 (prostate cancer), NIH3T3 (fibroblast), H23 (lung cancer), and A-172 (glioblastoma multiforme) cell lines and knocked out in HUH7 (liver cancer) cells. Cells were analyzed for proliferation and in invasion assays, and/or injected into flanks of severe combined immunodeficient mice; xenograft tumor growth and metastasis were assessed. Mice with hepatic deletion of PTEN were given tail-vein injections of MAN2A1-FER. RESULTS: We detected MAN2A1-FER messenger RNA and fusion protein (114 kD) in the hepatocellular carcinoma cell line HUH7, as well as in liver tumors, esophageal adenocarcinoma, glioblastoma multiforme, prostate tumors, non-small cell lung tumors, and ovarian tumors, but not nontumor prostate or liver tissues. MAN2A1-FER protein retained the signal peptide for Golgi localization from MAN2A1 and translocated from the cytoplasm to Golgi in cancer cell lines. MAN2A1-FER had tyrosine kinase activity almost 4-fold higher than that of wild-type FER, and phosphorylated the epidermal growth factor receptor at tyrosine 88 in its N-terminus. Expression of MAN2A1-FER in 4 cell lines led to epidermal growth factor receptor activation of BRAF, MEK, and AKT; HUH7 cells with MAN2A1-FER knockout had significant decreases in phosphorylation of these proteins. Cell lines that expressed MAN2A1-FER had increased proliferation, colony formation, and invasiveness and formed larger (>2-fold) xenograft tumors in mice, with more metastases, than cells not expressing the fusion protein. HUH7 cells with MAN2A1-FER knockout formed smaller xenograft tumors, with fewer metastases, than control HUH7 cells. HUH7, A-172, and PC3 cells that expressed MAN2A1-FER were about 2-fold more sensitive to the FER kinase inhibitor crizotinib and the epidermal growth factor receptor kinase inhibitor canertinib; these drugs slowed growth of xenograft tumors from MAN2A1-FER cells and prevented their metastasis in mice. Hydrodynamic tail-vein injection of MAN2A1-FER resulted in rapid development of liver cancer in mice with hepatic disruption of Pten. CONCLUSIONS: Many human tumor types and cancer cell lines express the MAN2A1-FER fusion, which increases proliferation and invasiveness of cancer cell lines and has liver oncogenic activity in mice.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Transformação Celular Neoplásica/genética
Fusão Gênica
Neoplasias Hepáticas/genética
Proteínas de Fusão Oncogênicas/genética
Oncogenes
Proteínas Tirosina Quinases/genética
alfa-Manosidase/genética
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Movimento Celular
Proliferação Celular
Transformação Celular Neoplásica/metabolismo
Transformação Celular Neoplásica/patologia
Relação Dose-Resposta a Droga
Ativação Enzimática
Regulação Enzimológica da Expressão Gênica
Regulação Neoplásica da Expressão Gênica
Complexo de Golgi/enzimologia
Seres Humanos
Neoplasias Hepáticas/tratamento farmacológico
Neoplasias Hepáticas/enzimologia
Neoplasias Hepáticas/patologia
Camundongos
Camundongos Knockout
Camundongos SCID
Morfolinas/farmacologia
Células NIH 3T3
Invasividade Neoplásica
Transplante de Neoplasias
Proteínas de Fusão Oncogênicas/antagonistas & inibidores
Proteínas de Fusão Oncogênicas/metabolismo
PTEN Fosfo-Hidrolase/deficiência
PTEN Fosfo-Hidrolase/genética
Fosforilação
Inibidores de Proteínas Quinases/farmacologia
Proteínas Tirosina Quinases/antagonistas & inibidores
Proteínas Tirosina Quinases/metabolismo
Pirazóis/farmacologia
Piridinas/farmacologia
Interferência de RNA
Receptor do Fator de Crescimento Epidérmico/genética
Receptor do Fator de Crescimento Epidérmico/metabolismo
Fatores de Tempo
Transfecção
Carga Tumoral
alfa-Manosidase/antagonistas & inibidores
alfa-Manosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (MAN2A1-FER fusion protein, human); 0 (Morpholines); 0 (Oncogene Proteins, Fusion); 0 (Protein Kinase Inhibitors); 0 (Pyrazoles); 0 (Pyridines); 53AH36668S (crizotinib); C78W1K5ASF (Canertinib); EC 2.7.10.1 (EGFR protein, human); EC 2.7.10.1 (Protein-Tyrosine Kinases); EC 2.7.10.1 (Receptor, Epidermal Growth Factor); EC 3.1.3.67 (PTEN Phosphohydrolase); EC 3.1.3.67 (Pten protein, mouse); EC 3.2.1.24 (alpha-Mannosidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170301
[St] Status:MEDLINE


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[PMID]:27693560
[Au] Autor:Fernández-Delgado M; Cortez J; Sulbarán G; Matos C; Incani RN; Ballén DE; Cesari IM
[Ad] Endereço:Centro de Microbiología y Biología Celular, Instituto Venezolano de Investigaciones Científicas (IVIC), Caracas, Venezuela.
[Ti] Título:Differential distribution and biochemical characteristics of hydrolases among developmental stages of Schistosoma mansoni may offer new anti-parasite targets.
[So] Source:Parasitol Int;66(1):816-820, 2017 Feb.
[Is] ISSN:1873-0329
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Schistosoma mansoni enzymes play important roles in host-parasite interactions and are potential targets for immunological and/or pharmacological attack. The aim of this study was to comparatively assess the presence of hydrolytic activities (phosphatases, glycosidases, aminopeptidases) in soluble (SF) and membrane (MF) fractions from different S. mansoni developmental stages (schistosomula 0 and 3h, juveniles, and adult worms of 28 and 45days-old, respectively), by using simple enzyme-substrate microassays. Our results show and confirm the prominent presence of alkaline phosphatase (AlP) activity in the MF of all the above parasite stages, highlighting also the relevant presence of MF-associated α-mannosidase (α-MAN) activity in juveniles. A soluble AlP activity, together with ß-N-D-acetylglucosaminidase (ß-NAG), and α-MAN activities, was detected in SF of schistosomulum 0h. Soluble ß-NAG, α-MAN, acid phosphatase (AcP), leucin (LAP) and alanine (AAP) aminopeptidase activities were also seen in the SF of the other different developmental stages. This work shows different soluble and membrane-associated hydrolytic capacities in each S. mansoni developmental stage from schistosomula to adults that might be exploitable as potential new targets for immune and/or chemoprophylactic strategies.
[Mh] Termos MeSH primário: Fosfatase Alcalina/metabolismo
Glicosídeo Hidrolases/metabolismo
Proteínas de Helminto/metabolismo
Schistosoma mansoni/enzimologia
Schistosoma mansoni/crescimento & desenvolvimento
alfa-Manosidase/isolamento & purificação
alfa-Manosidase/metabolismo
[Mh] Termos MeSH secundário: Fosfatase Alcalina/imunologia
Fosfatase Alcalina/isolamento & purificação
Aminopeptidases/química
Aminopeptidases/imunologia
Aminopeptidases/isolamento & purificação
Animais
Membrana Celular/química
Membrana Celular/enzimologia
Glicosídeo Hidrolases/imunologia
Glicosídeo Hidrolases/isolamento & purificação
Proteínas de Helminto/imunologia
Estágios do Ciclo de Vida
Schistosoma mansoni/imunologia
Esquistossomose mansoni/terapia
alfa-Manosidase/imunologia
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Helminth Proteins); EC 3.1.3.1 (Alkaline Phosphatase); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.24 (alpha-Mannosidase); EC 3.4.11.- (Aminopeptidases)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170417
[Lr] Data última revisão:
170417
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161107
[St] Status:MEDLINE


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[PMID]:27490136
[Au] Autor:Lazar C; Uta M; Petrescu SM; Branza-Nichita N
[Ad] Endereço:Department of Viral Glycoproteins, Institute of Biochemistry of the Romanian Academy, Bucharest, Romania.
[Ti] Título:Novel function of the endoplasmic reticulum degradation-enhancing α-mannosidase-like proteins in the human hepatitis B virus life cycle, mediated by the middle envelope protein.
[So] Source:Cell Microbiol;19(2), 2017 Feb.
[Is] ISSN:1462-5822
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cells replicating the human hepatitis B virus (HBV) express high levels of degradation-enhancing α-mannosidase-like proteins (EDEMs), a family of proteins involved in the endoplasmic reticulum associated degradation, one of the pathways activated during the unfolded protein response. Owing to their α-1,2 mannosidase activity, the EDEM1-3 proteins are able to process the N-linked glycans of misfolded or incompletely folded proteins, providing the recognition signal for their subsequent degradation. The HBV small (S), medium (M), and large (L) surface proteins bear an N-linked glycosylation site in the common S domain that is partially occupied in all proteins. The M protein contains an additional site in its preS2 domain, which is always functional. Here, we report that these oligosaccharides are processed by EDEMs, more efficiently by EDEM3, which induces degradation of L and S proteins, accompanied by a reduction of subviral particles production. In striking contrast, M not only is spared from degradation but its trafficking is also accelerated leading to an improved secretion. This unusual behavior of the M protein requires strictly the mannose trimming of the preS2 N-linked glycan. Furthermore, we show that HBV secretion is significantly inhibited under strong endoplasmic reticulum stress conditions when M expression is prevented by mutagenesis of the viral genome. These observations unfold unique properties of the M protein in the HBV life cycle during unfolded protein response and point to alternative mechanisms employed by EDEMs to alleviate this stress in case of necessity by promoting glycoprotein trafficking rather than degradation.
[Mh] Termos MeSH primário: Retículo Endoplasmático/metabolismo
Vírus da Hepatite B/fisiologia
Interações Hospedeiro-Patógeno
Proteínas do Envelope Viral/metabolismo
alfa-Manosidase/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular
Estresse do Retículo Endoplasmático
Seres Humanos
Processamento de Proteína Pós-Traducional
Transporte Proteico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Viral Envelope Proteins); 0 (middle envelope protein, Hepatitis B virus); EC 3.2.1.24 (alpha-Mannosidase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160805
[St] Status:MEDLINE
[do] DOI:10.1111/cmi.12653


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[PMID]:27920474
[Au] Autor:Hu S; Jiang LB; Zou XJ; Yi W; Tian DY
[Ad] Endereço:Song Hu, Li-Bin Jiang, Xiao-Jing Zou, Wei Yi, De-Ying Tian, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, Hubei Province, China.
[Ti] Título:Hepatitis B virus upregulates host expression of α-1,2-mannosidases the PPARα pathway.
[So] Source:World J Gastroenterol;22(43):9534-9543, 2016 Nov 21.
[Is] ISSN:2219-2840
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:AIM: To assess the effects of hepatitis B virus (HBV) on the expression of host α-1,2-mannosidases and determine the underlying mechanisms. METHODS: We measured the expression levels of MAN1A1, MAN1A2, MAN1B1, and MAN1C1 in cell lines HepG2.2.15, HepN10, HepAD38 and HepG2 by Western blot. Viral antigens (HBsAg and HBeAg) in the culture medium were measured using the chemiluminescence method. HBV DNA quantification assays were performed using a commercial real-time PCR kit. Protein levels of human liver tissue α-1,2-mannosidases were also evaluated by Western blot. Plasmids containing seven individual viral genes of HBV (PTT22-HBx, PTT22-HBs, PTT22-preS2, PTT22-preS1, PTT22-HBc, PTT22-HBe, and PTT22-HBp) or control plasmids (PTT22-vector) were transfected into HepG2 cells. MK886 (PPARα) and GW9662 (PPARγ) inhibitors were used to explore the effects of HBV on α-1,2-mannosidase expression after the PPARα and PPARγ pathways were blocked. RESULTS: We showed that the expression of α-1,2-mannosidases was higher in stably transfected HBV cells than in controls. The expression levels of α-1,2-mannosidase were higher in AD38 cells than those in ND10 cells, which were in turn greater than those in G2.2.15 cells, and positively correlated with the expression of HBsAg in all the cell lines. Levels of α-1,2-mannosidase in non-tumorous liver tissues of HBV-related HCC patients were also higher than in the tissues from non-HBV-related HCC patients. Moreover, transfecting HepG2 cells with a component of the HBV viral envelope also increased the expression of α-1,2-mannosidases. However, this envelope protein component could not induce MAN1C1 expression in the presence of a PPARα inhibitor, MK886. We also found that MK886 did not affect the expression of MAN1C1 in AD38 cells without tetracycline in the culture medium. This phenomenon was not observed in the case of GW9662. CONCLUSION: Our results indicate that HBV increases the expression of α-mannosidases both and activation of the PPARα pathway by its envelope protein.
[Mh] Termos MeSH primário: Vírus da Hepatite B/metabolismo
Hepatite B/enzimologia
Hepatócitos/enzimologia
Hepatócitos/virologia
Fígado/enzimologia
Fígado/virologia
PPAR alfa/metabolismo
alfa-Manosidase/metabolismo
[Mh] Termos MeSH secundário: Células Hep G2
Hepatite B/genética
Hepatite B/virologia
Antígenos de Superfície da Hepatite B/genética
Antígenos de Superfície da Hepatite B/metabolismo
Antígenos E da Hepatite B/genética
Antígenos E da Hepatite B/metabolismo
Vírus da Hepatite B/genética
Hepatócitos/efeitos dos fármacos
Interações Hospedeiro-Patógeno
Seres Humanos
Indóis/farmacologia
Fígado/efeitos dos fármacos
PPAR alfa/antagonistas & inibidores
Transfecção
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hepatitis B Surface Antigens); 0 (Hepatitis B e Antigens); 0 (Indoles); 0 (PPAR alpha); 080626SQ8C (MK-886); EC 3.2.1.24 (alpha-Mannosidase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170503
[Lr] Data última revisão:
170503
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161207
[St] Status:MEDLINE


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[PMID]:27736961
[Au] Autor:Banar M; Emaneini M; Satarzadeh M; Abdellahi N; Beigverdi R; Leeuwen WB; Jabalameli F
[Ad] Endereço:Department of Microbiology, School of Medicine, Tehran University of Medical Sciences, Tehran, Iran.
[Ti] Título:Evaluation of Mannosidase and Trypsin Enzymes Effects on Biofilm Production of Pseudomonas aeruginosa Isolated from Burn Wound Infections.
[So] Source:PLoS One;11(10):e0164622, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Biofilm is an important virulence factor in Pseudomonas aeruginosa and has a substantial role in antibiotic resistance and chronic burn wound infections. New therapeutic agents against P. aeruginosa, degrading biofilms in burn wounds and improving the efficacy of current antimicrobial agents, are required. In this study, the effects of α-mannosidase, ß-mannosidase and trypsin enzymes on the degradation of P. aeruginosa biofilms and on the reduction of ceftazidime minimum biofilm eliminating concentrations (MBEC) were evaluated. All tested enzymes, destroyed the biofilms and reduced the ceftazidime MBECs. However, only trypsin had no cytotoxic effect on A-431 human epidermoid carcinoma cell lines. In conclusion, since trypsin had better features than mannosidase enzymes, it can be a promising agent in combatting P. aeruginosa burn wound infections.
[Mh] Termos MeSH primário: Queimaduras/complicações
Manosidases/farmacologia
Infecções por Pseudomonas/microbiologia
Pseudomonas aeruginosa/efeitos dos fármacos
Tripsina/farmacologia
Infecção dos Ferimentos/microbiologia
[Mh] Termos MeSH secundário: Biofilmes/efeitos dos fármacos
Ceftazidima/farmacologia
Linhagem Celular
Seres Humanos
Manosidases/efeitos adversos
Testes de Sensibilidade Microbiana
Infecções por Pseudomonas/tratamento farmacológico
Pseudomonas aeruginosa/isolamento & purificação
Tripsina/uso terapêutico
Infecção dos Ferimentos/tratamento farmacológico
alfa-Manosidase/efeitos adversos
alfa-Manosidase/farmacologia
beta-Manosidase/efeitos adversos
beta-Manosidase/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9M416Z9QNR (Ceftazidime); EC 3.2.1.- (Mannosidases); EC 3.2.1.24 (alpha-Mannosidase); EC 3.2.1.25 (beta-Mannosidase); EC 3.4.21.4 (Trypsin)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170522
[Lr] Data última revisão:
170522
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161014
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0164622


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[PMID]:27623439
[Au] Autor:Dedola S; Izumi M; Makimura Y; Seko A; Kanamori A; Takeda Y; Ito Y; Kajihara Y
[Ad] Endereço:Japan Science and Technology Agency (JST), ERATO, Ito Glycotrilogy Project, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan.
[Ti] Título:Direct assay for endo-α-mannosidase substrate preference on correctly folded and misfolded model glycoproteins.
[So] Source:Carbohydr Res;434:94-98, 2016 Nov 03.
[Is] ISSN:1873-426X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:We previously reported a unique assay system for UDP-glucose glycoprotein glucosyltransferase (UGGT) toward glycoprotein folding intermediates during the folding process. The assay involved the in vitro folding of both high-mannose type oligosaccharyl crambin, which yielded only the correctly folded glycoprotein form (M9-glycosyl-native-crambin), and its mutant, which yielded misfolded glycoproteins (M9-glycosyl-misfolded-crambin), in the presence of UGGT. The process successfully yielded both mono-glucosylated M9-glycosyl-native-crambin (G1M9-glycosyl-native-crambin) and M9-glycosyl-misfolded-crambin (G1M9-glycosyl-misfolded-crambin). Here, we report the use of our in vitro folding system to evaluate the substrate preference of Golgi endo-α-mannosidase against G1M9-native and -misfolded glycoprotein forms. In our assay Golgi endo-α-mannosidase removed Glc-α-1-3-Man unit from G1M9-native and -misfolded-crambins clearly proving that Golgi endo-α-mannosidase does not have specific preference for correctly folded or misfolded protein structure.
[Mh] Termos MeSH primário: Glicoproteínas/química
Mutação
alfa-Manosidase/metabolismo
[Mh] Termos MeSH secundário: Glicoproteínas/genética
Estrutura Molecular
Proteínas de Plantas/química
Dobramento de Proteína
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycoproteins); 0 (Plant Proteins); 78783-34-3 (crambin protein, Crambe abyssinica); EC 3.2.1.24 (alpha-Mannosidase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170227
[Lr] Data última revisão:
170227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160914
[St] Status:MEDLINE


  9 / 952 MEDLINE  
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[PMID]:27606974
[Au] Autor:Wu C; Han T; Lu H; Zhao B
[Ad] Endereço:College of Animal Veterinary Medicine, Northwest A & F University, Yangling 712100, Shaanxi, People's Republic of China. Electronic address: wucen95888@163.com.
[Ti] Título:The toxicology mechanism of endophytic fungus and swainsonine in locoweed.
[So] Source:Environ Toxicol Pharmacol;47:38-46, 2016 Oct.
[Is] ISSN:1872-7077
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Locoweed is a perennial herbaceous plant included in Astragalus spp. and Oxytropis spp. that contains the toxic indolizidine alkaloid swainsonine. The livestock that consume locoweed can suffer from a type of toxicity called locoism. There are aliphaticnitro compounds, selenium, selenium compounds, and alkaloids in locoweed. The toxic component in locoweed has been identified as swainsonine, an indolizidine alkaloid. Swainsonine inhibits lysosomal a-mannosidase and mannosidase II, resulting in altered oligosaccharide degradation and incomplete glycoprotein processing. Corresponding studies on endophytic fungi producing swainsonine have been isolated from a variety of locoweed, and these endophytic fungi and locoweed have a close relationship. Endophytic fungi can promote the growth of locoweed and increase swainsonine production. As a result, livestock that consume locoweed exhibit several symptoms, including dispirited behavior, staggering gait, chromatopsia, trembling, ataxia, and cellular vacuolar degeneration of most tissues by pathological observation. Locoism results in significant annual economic losses. Therefore, in this paper, we review the current research on locoweed, including that on locoweed species distribution in China, endophyte fungus in locoweed, the toxicology mechanism of locoweed, and the swainsonine effect on reproduction.
[Mh] Termos MeSH primário: Ascomicetos/metabolismo
Astrágalo (Planta)/microbiologia
Oxytropis/microbiologia
Swainsonina/toxicidade
[Mh] Termos MeSH secundário: Animais
Ascomicetos/fisiologia
Astrágalo (Planta)/metabolismo
China
Endófitos/metabolismo
Manosidases/antagonistas & inibidores
Oxytropis/metabolismo
Plantas Daninhas/microbiologia
Swainsonina/metabolismo
Swainsonina/farmacocinética
Simbiose
alfa-Manosidase/classificação
alfa-Manosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
EC 3.2.1.- (Mannosidases); EC 3.2.1.114 (mannosyl-oligosaccharide 1,3 - 1,6-alpha-mannosidase); EC 3.2.1.24 (alpha-Mannosidase); RSY4RK37KQ (Swainsonine)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170213
[Lr] Data última revisão:
170213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160909
[St] Status:MEDLINE


  10 / 952 MEDLINE  
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[PMID]:27189235
[Au] Autor:Aleksanyan H; Liang J; Metzenberg S; Oppenheimer SB
[Ad] Endereço:Department of Biology and Center for Cancer and Developmental Biology,California State University,Northridge,California 91330-8303,USA.
[Ti] Título:Terminal alpha-d-mannosides are critical during sea urchin gastrulation.
[So] Source:Zygote;24(5):775-82, 2016 Oct.
[Is] ISSN:1469-8730
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The sea urchin embryo is a United States National Institutes of Health (NIH) designated model system to study mechanisms that may be involved in human health and disease. In order to examine the importance of high-mannose glycans and polysaccharides in gastrulation, Lytechinus pictus embryos were incubated with Jack bean α-mannosidase (EC 3.2.1.24), an enzyme that cleaves terminal mannose residues that have α1-2-, α1-3-, or α1-6-glycosidic linkages. The enzyme treatment caused a variety of morphological deformations in living embryos, even with α-mannosidase activities as low as 0.06 U/ml. Additionally, formaldehyde-fixed, 48-hour-old L. pictus embryos were microdissected and it was demonstrated that the adhesion of the tip of the archenteron to the roof of the blastocoel in vitro is abrogated by treatment with α-mannosidase. These results suggest that terminal mannose residues are involved in the adhesion between the archenteron and blastocoel roof, perhaps through a lectin-like activity that is not sensitive to fixation.
[Mh] Termos MeSH primário: Gastrulação/fisiologia
Manosídeos/química
Manosídeos/metabolismo
Ouriços-do-Mar/embriologia
[Mh] Termos MeSH secundário: Animais
Embrião não Mamífero/metabolismo
Gástrula/crescimento & desenvolvimento
Gástrula/metabolismo
Ouriços-do-Mar/metabolismo
alfa-Manosidase/química
alfa-Manosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mannosides); EC 3.2.1.24 (alpha-Mannosidase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170609
[Lr] Data última revisão:
170609
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160519
[St] Status:MEDLINE
[do] DOI:10.1017/S0967199416000113



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