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[PMID]:27697835
[Au] Autor:Napier BA; Brubaker SW; Sweeney TE; Monette P; Rothmeier GH; Gertsvolf NA; Puschnik A; Carette JE; Khatri P; Monack DM
[Ad] Endereço:Department of Microbiology and Immunology, Stanford University, Stanford, CA 94305.
[Ti] Título:Complement pathway amplifies caspase-11-dependent cell death and endotoxin-induced sepsis severity.
[So] Source:J Exp Med;213(11):2365-2382, 2016 Oct 17.
[Is] ISSN:1540-9538
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cell death and release of proinflammatory mediators contribute to mortality during sepsis. Specifically, caspase-11-dependent cell death contributes to pathology and decreases in survival time in sepsis models. Priming of the host cell, through TLR4 and interferon receptors, induces caspase-11 expression, and cytosolic LPS directly stimulates caspase-11 activation, promoting the release of proinflammatory cytokines through pyroptosis and caspase-1 activation. Using a CRISPR-Cas9-mediated genome-wide screen, we identified novel mediators of caspase-11-dependent cell death. We found a complement-related peptidase, carboxypeptidase B1 (Cpb1), to be required for caspase-11 gene expression and subsequent caspase-11-dependent cell death. Cpb1 modifies a cleavage product of C3, which binds to and activates C3aR, and then modulates innate immune signaling. We find the Cpb1-C3-C3aR pathway induces caspase-11 expression through amplification of MAPK activity downstream of TLR4 and Ifnar activation, and mediates severity of LPS-induced sepsis (endotoxemia) and disease outcome in mice. We show C3aR is required for up-regulation of caspase-11 orthologues, caspase-4 and -5, in primary human macrophages during inflammation and that c3aR1 and caspase-5 transcripts are highly expressed in patients with severe sepsis; thus, suggesting that these pathways are important in human sepsis. Our results highlight a novel role for complement and the Cpb1-C3-C3aR pathway in proinflammatory signaling, caspase-11 cell death, and sepsis severity.
[Mh] Termos MeSH primário: Caspases/metabolismo
Proteínas do Sistema Complemento/metabolismo
Sepse/enzimologia
Sepse/patologia
[Mh] Termos MeSH secundário: Animais
Sistemas CRISPR-Cas
Carboxipeptidase B/metabolismo
Morte Celular
Complemento C3/metabolismo
Endotoxemia/sangue
Endotoxemia/patologia
Endotoxinas
Ativação Enzimática
Regulação da Expressão Gênica
Seres Humanos
Inflamação/genética
Inflamação/patologia
Mediadores da Inflamação/metabolismo
Sistema de Sinalização das MAP Quinases
Macrófagos/enzimologia
Macrófagos/metabolismo
Macrófagos/patologia
Camundongos
Modelos Biológicos
Fosforilação
Células RAW 264.7
Receptores de Complemento/metabolismo
Receptores de Interferon/metabolismo
Salmonella/fisiologia
Shigella/fisiologia
Receptor 4 Toll-Like/metabolismo
Proteínas Quinases p38 Ativadas por Mitógeno/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Complement C3); 0 (Endotoxins); 0 (Inflammation Mediators); 0 (Receptors, Complement); 0 (Receptors, Interferon); 0 (Toll-Like Receptor 4); 0 (complement C3a receptor); 9007-36-7 (Complement System Proteins); EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases); EC 3.4.17.2 (Carboxypeptidase B); EC 3.4.22.- (Casp11 protein, mouse); EC 3.4.22.- (Caspases)
[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:161005
[St] Status:MEDLINE


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[PMID]:27522657
[Au] Autor:Kim DG; Kim HJ; Kim HJ
[Ad] Endereço:Graduate School of Pharmaceutical Management, Chung-Ang University, 84 Heukseok-Ro, Dongjak-Gu, Seoul, 06974, South Korea.
[Ti] Título:Effects of carboxypeptidase B treatment and elevated temperature on recombinant monoclonal antibody charge variants in cation-exchange chromatography analysis.
[So] Source:Arch Pharm Res;39(10):1472-1481, 2016 Oct.
[Is] ISSN:0253-6269
[Cp] País de publicação:Korea (South)
[La] Idioma:eng
[Ab] Resumo:Charge variants (acidic and basic) of recombinant monoclonal antibodies (Mabs) have received much attention due to their potential biological effects. C-terminal lysine variants are common in Mabs and their proportion is affected by the manufacturing process. In the present study, changes of trastuzumab charge variants brought about by carboxypeptidase B treatment and subsequent storage at 8 or 37 °C for up to 24 h were monitored by cation-exchange chromatography analysis to investigate the effects of C-terminal lysine cleavage and its subsequent reaction at 8 or 37 °C. C-terminal lysine cleavage at 8 °C reduced the fraction of basic species and had little effect on the fraction of acidic species. Analysis of individual peaks demonstrated that C-terminal lysine cleavage induced both increases and decreases in individual acidic variants, with the result that there was little overall change in the overall proportion of acidic species. It appeared that most of the basic variant Mab molecules but only a fraction of the acidic variant molecules had C-terminal lysines. Increasing the temperature to 37 °C appeared to increase the fraction of acidic species and decrease main species significantly, without a similar change in basic species. These results indicate that length of exposure to elevated temperature is a critical consideration in charge variant analysis.
[Mh] Termos MeSH primário: Anticorpos Monoclonais/análise
Carboxipeptidase B/análise
Resinas de Troca de Cátion/química
Temperatura Alta
Proteínas Recombinantes/análise
[Mh] Termos MeSH secundário: Animais
Células CHO
Cromatografia Líquida de Alta Pressão/métodos
Cricetinae
Cricetulus
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Cation Exchange Resins); 0 (Recombinant Proteins); EC 3.4.17.2 (Carboxypeptidase B)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170127
[Lr] Data última revisão:
170127
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160815
[St] Status:MEDLINE


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[PMID]:27358403
[Au] Autor:Szabó A; Pilsak C; Bence M; Witt H; Sahin-Tóth M
[Ad] Endereço:From the Department of Molecular and Cell Biology and.
[Ti] Título:Complex Formation of Human Proelastases with Procarboxypeptidases A1 and A2.
[So] Source:J Biol Chem;291(34):17706-16, 2016 08 19.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The pancreas secretes digestive proenzymes typically in their monomeric form. A notable exception is the ternary complex formed by proproteinase E, chymotrypsinogen C, and procarboxypeptidase A (proCPA) in cattle and other ruminants. In the human and pig pancreas binary complexes of proCPA with proelastases were found. To characterize complex formation among human pancreatic protease zymogens in a systematic manner, we performed binding experiments using recombinant proelastases CELA2A, CELA3A, and CELA3B; chymotrypsinogens CTRB1, CTRB2, CTRC, and CTRL1; and procarboxypeptidases CPA1, CPA2, and CPB1. We found that proCELA3B bound not only to proCPA1 (KD 43 nm) but even more tightly to proCPA2 (KD 18 nm), whereas proCELA2A bound weakly to proCPA1 only (KD 152 nm). Surprisingly, proCELA3A, which shares 92% identity with proCELA3B, did not form stable complexes due to the evolutionary replacement of Ala(241) with Gly. The polymorphic nature of position 241 in both CELA3A (∼4% Ala(241) alleles) and CELA3B (∼2% Gly(241) alleles) points to individual variations in complex formation. The functional effect of complex formation was delayed procarboxypeptidase activation due to increased affinity of the inhibitory activation peptide, whereas proelastase activation was unchanged. We conclude that complex formation among human pancreatic protease zymogens is limited to a subset of proelastases and procarboxypeptidases. Complex formation stabilizes the inhibitory activation peptide of procarboxypeptidases and thereby increases zymogen stability and controls activation.
[Mh] Termos MeSH primário: Carboxipeptidases A/metabolismo
Precursores Enzimáticos/metabolismo
Elastase Pancreática/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Animais
Carboxipeptidase B/genética
Carboxipeptidase B/metabolismo
Carboxipeptidases A/genética
Bovinos
Linhagem Celular
Ativação Enzimática/fisiologia
Precursores Enzimáticos/genética
Seres Humanos
Mutação de Sentido Incorreto
Elastase Pancreática/genética
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (CPB1 protein, human); 0 (Enzyme Precursors); EC 3.4.17.1 (Carboxypeptidases A); EC 3.4.17.2 (Carboxypeptidase B); EC 3.4.21.36 (Pancreatic Elastase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171120
[Lr] Data última revisão:
171120
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160701
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.743237


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[PMID]:26766000
[Au] Autor:Wijekoon CJ; Ukuwela AA; Wedd AG; Xiao Z
[Ad] Endereço:School of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria 3010, Australia.
[Ti] Título:Evaluation of employing poly-lysine tags versus poly-histidine tags for purification and characterization of recombinant copper-binding proteins.
[So] Source:J Inorg Biochem;162:286-294, 2016 Sep.
[Is] ISSN:1873-3344
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Quantitative characterization of metalloproteins at molecular and atomic levels generally requires tens of milligrams of highly purified samples, a situation frequently challenged by problems in generating unmodified native forms. A variety of affinity tags, such as the popular poly-histidine tag, have been developed to facilitate purification but they generally rely on expensive affinity resins and their presence may interfere with protein characterization. This paper documents that addition of a poly-lysine tag to the C-terminus enables, for the copper-binding proteins examined, ready purification in large scale via cost-effective cation-exchange chromatography. The tag may be removed readily by the enzyme carboxypeptidase B to generate the native protein with no extra residues. However, this cleavage step is normally not necessary since the poly-lysine tag is shown to have no detectable affinity for either Cu(I) or Cu(II) and imposes no interference to the copper binding properties of the target proteins. In contrast, the poly-histidine tag possesses a sub-picomolar affinity for Cu(I) and -nanomolar affinity for Cu(II) and may need to be removed for reliable characterization of the target proteins. These conclusions may be extended to the study of other metallo-proteins and metallo-enzymes.
[Mh] Termos MeSH primário: Proteínas de Transporte/isolamento & purificação
Cobre/química
Histidina/química
Polilisina/química
Proteínas Recombinantes de Fusão/isolamento & purificação
[Mh] Termos MeSH secundário: Carboxipeptidase B/química
Proteínas de Transporte/química
Proteínas de Transporte/genética
Cátions Bivalentes
Cátions Monovalentes
Cromatografia de Afinidade/métodos
Cromatografia por Troca Iônica/métodos
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Pseudomonas fluorescens/química
Pseudomonas fluorescens/metabolismo
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/genética
Coloração e Rotulagem/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Cations, Divalent); 0 (Cations, Monovalent); 0 (Recombinant Fusion Proteins); 0 (copper-binding protein); 25104-18-1 (Polylysine); 26062-48-6 (polyhistidine); 4QD397987E (Histidine); 789U1901C5 (Copper); EC 3.4.17.2 (Carboxypeptidase B)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160115
[St] Status:MEDLINE


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[PMID]:26457527
[Au] Autor:Akparov V; Sokolenko N; Timofeev V; Kuranova I
[Ad] Endereço:Protein Chemistry Department, State Research Institute for Genetics and Selection of Industrial Microorganisms, 1yi Dorozhnyi Proezd 1, 117545 Moscow, Russian Federation.
[Ti] Título:Structure of the complex of carboxypeptidase B and N-sulfamoyl-L-arginine.
[So] Source:Acta Crystallogr F Struct Biol Commun;71(Pt 10):1335-40, 2015 Oct.
[Is] ISSN:2053-230X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Porcine pancreatic carboxypeptidase B (EC 3.4.23.6) was complexed with a stable transition-state analogue, N-sulfamoyl-L-arginine, in which an S atom imitates the sp(3)-hybridized carbon in the scissile-bond surrogate. Crystals were grown in a form belonging to the same space group, P41212, as the uncomplexed enzyme. X-ray data were collected to a resolution of 1.25 Å. The molecule was refined and the positions of non-H atoms of the inhibitor and water molecules were defined using difference Fourier maps. The enzyme-inhibitor complex and 329 water molecules were further refined to a crystallographic R factor of 0.159. The differences in conformation between the complexed and uncomplexed forms of carboxypeptidase B are shown. The inhibitor is bound in a curved conformation in the active-site cleft, and the sulfamide group is bound to the Zn ion in an asymmetric bidentate fashion. The complex is stabilized by hydrogen bonds between the N1/N2 guanidine group of the inhibitor and the Asp255 carboxyl of the enzyme. The side-chain CH2 groups of the inhibitor are in van der Waals contact with Leu203 and Ile247 in the enzyme. This study provides useful clues concerning how the transition state of arginine may bind to carboxypeptidase B and therefore provides an insight into the structural basis of carboxypeptidase B selectivity, which is useful for the rational design of a carboxypeptidase with improved selectivity for industrial recombinant pro-insulin processing.
[Mh] Termos MeSH primário: Arginina/análogos & derivados
Arginina/química
Carboxipeptidase B/química
Sulfonamidas/química
[Mh] Termos MeSH secundário: Animais
Arginina/síntese química
Domínio Catalítico
Cristalização
Cristalografia por Raios X
Ligações de Hidrogênio
Ligantes
Soluções
Eletricidade Estática
Sulfonamidas/síntese química
Sus scrofa
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ligands); 0 (N-sulfamoylarginine); 0 (Solutions); 0 (Sulfonamides); 94ZLA3W45F (Arginine); EC 3.4.17.2 (Carboxypeptidase B)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:171001
[Lr] Data última revisão:
171001
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151013
[St] Status:MEDLINE
[do] DOI:10.1107/S2053230X15016799


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[PMID]:26352934
[Au] Autor:Mongkol W; Arunyawat U; Surat W; Kubera A
[Ad] Endereço:Department of Genetics, Faculty of Science, Kasetsart University, Bangkok, 10900, Thailand.
[Ti] Título:Active Compounds Against Anopheles minimus Carboxypeptidase B for Malaria Transmission-Blocking Strategy.
[So] Source:J Med Entomol;52(6):1322-32, 2015 Nov.
[Is] ISSN:0022-2585
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Malaria transmission-blocking compounds have been studied to block the transmission of malaria parasites, especially the drug-resistant Plasmodium. Carboxypeptidase B (CPB) in the midgut of Anopheline mosquitoes has been demonstrated to be essential for the sexual development of Plasmodium in the mosquito. Thus, the CPB is a potential target for blocking compounds. The aim of this research was to screen compounds from the National Cancer Institute (NCI) diversity dataset and U.S. Food and Drug Administration (FDA)-approved drugs that could reduce the Anopheles CPB activity. The cDNA fragment of cpb gene from An. minimus (cpbAmi) was amplified and sequenced. The three-dimensional structure of CPB was predicted from the deduced amino acid sequence. The virtual screening of the compounds from NCI diversity set IV and FDA-approved drugs was performed against CPBAmi. The inhibition activity against CPBAmi of the top-scoring molecules was characterized in vitro. Three compounds-NSC-1014, NSC-332670, and aminopterin with IC50 at 0.99 mM, 1.55 mM, and 0.062 mM, respectively-were found to significantly reduce the CPBAmi activity.
[Mh] Termos MeSH primário: Anopheles/enzimologia
Carboxipeptidase B/antagonistas & inibidores
Malária/prevenção & controle
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Anopheles/genética
Carboxipeptidase B/genética
Clonagem Molecular
Malária/transmissão
Simulação de Acoplamento Molecular
Dados de Sequência Molecular
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.4.17.2 (Carboxypeptidase B)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:151106
[Lr] Data última revisão:
151106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150910
[St] Status:MEDLINE
[do] DOI:10.1093/jme/tjv133


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[PMID]:26316592
[Au] Autor:Nakano E; Geisz A; Masamune A; Niihori T; Hamada S; Kume K; Kakuta Y; Aoki Y; Matsubara Y; Ebert K; Ludwig M; Braun M; Groneberg DA; Shimosegawa T; Sahin-Tóth M; Witt H
[Ad] Endereço:Division of Gastroenterology, Tohoku University Graduate School of Medicine, Sendai, Japan;
[Ti] Título:Variants in pancreatic carboxypeptidase genes CPA2 and CPB1 are not associated with chronic pancreatitis.
[So] Source:Am J Physiol Gastrointest Liver Physiol;309(8):G688-94, 2015 Oct 15.
[Is] ISSN:1522-1547
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Genetic alterations in the carboxypeptidase A1 gene (CPA1) are associated with early onset chronic pancreatitis (CP). Besides CPA1, there are two other human pancreatic carboxypeptidases (CPA2 and CPB1). Here we examined whether CPA2 and CPB1 alterations are associated with CP in Japan and Germany. All exons and flanking introns of CPA2 and CPB1 were sequenced in 477 Japanese patients with CP (234 alcoholic, 243 nonalcoholic) and in 497 German patients with nonalcoholic CP by targeted next-generation sequencing and/or Sanger sequencing. Secretion and enzymatic activity of CPA2 and CPB1 variants were determined after transfection into HEK 293T cells. We identified six nonsynonymous CPA2 variants (p.V67I, p.G166R, p.D168E, p.D173H, p.R237W, and p.G388S), eight nonsynonymous CPB1 alterations (p.S65G, p.N120S, p.D172E, p.R195H, p.D208N, p.F232L, p.A317V, and p.D364Y), and one splice-site variant (c.687+1G>T) in CPB1. Functional analysis revealed essentially complete loss of function in CPA2 variants p.R237W and p.G388S and CPB1 variants p.R110H and p.D364Y. None of the CPA2 or CPB1 variants, including those resulting in a marked loss of function, were overrepresented in patients with CP. In conclusion, CPA2 and CPB1 variants are not associated with CP.
[Mh] Termos MeSH primário: Carboxipeptidase B/genética
Carboxipeptidases A/genética
Regulação Enzimológica da Expressão Gênica/fisiologia
Variação Genética
Pancreatite Crônica/enzimologia
Pancreatite Crônica/metabolismo
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Idoso de 80 Anos ou mais
Grupo com Ancestrais do Continente Asiático
Carboxipeptidase B/metabolismo
Carboxipeptidases A/metabolismo
Criança
Pré-Escolar
Grupo com Ancestrais do Continente Europeu
Feminino
Alemanha
Seres Humanos
Lactente
Japão
Masculino
Meia-Idade
Pancreatite Crônica/genética
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CPB1 protein, human); EC 3.4.17.1 (Carboxypeptidases A); EC 3.4.17.2 (Carboxypeptidase B)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150829
[St] Status:MEDLINE
[do] DOI:10.1152/ajpgi.00241.2015


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[PMID]:25920892
[Au] Autor:Deng L; Wang L; Yong F; Xiong J; Jin T; De La Iglesia-Garcia D; Bharucha S; Altaf K; Huang W; Xia Q
[Ad] Endereço:Sichuan Provincial Pancreatitis Center, Department of Integrated Traditional and Western Medicine, West China Hospital, Sichuan University, Chengdu 610041, Sichuan Province, China.
[Ti] Título:Prediction of the severity of acute pancreatitis on admission by carboxypeptidase-B activation peptide: A systematic review and meta-analysis.
[So] Source:Clin Biochem;48(10-11):740-6, 2015 Jul.
[Is] ISSN:1873-2933
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVES: The assessment of acute pancreatitis severity on admission currently remains a challenge to clinicians. A single, rapid biochemical marker would be preferable to clinical and radiological scoring systems. The aim of this study was to undertake a meta-analysis on the value of carboxypeptidase-B activation peptide (CAPAP) in predicting severity of acute pancreatitis on admission. METHODS: Major databases and trial registries were searched to identify all relevant studies from January 1998 to March 2015. Pooled sensitivity, specificity and the diagnostic odds ratios (DOR) with 95% confidence interval (CI) were calculated for each study and were compared to other biomarkers, if included, within the same study. Summary receiver-operating curves (ROC) were conducted and the area under the curve (AUC) was evaluated. RESULTS: In total, six studies were included. At the time of admission, the AUC of serum CAPAP for predicting severity of acute pancreatitis was 0.86 with pooled sensitivity, specificity and DOR of 0.90, 0.70 and 19.08, respectively. When serum CAPAP was compared with urinary CAPAP, the AUC, pooled sensitivity, specificity and DOR were 0.69 vs 0.88, 0.90 vs 0.81, 0.68 vs. 0.77 and 17.96 vs. 18.58, respectively. Similarly, the AUC, pooled sensitivity, specificity and DOR of serum CAPAP vs maximal serum C-reactive protein within the first 3 days of admission were found to be 0.97 vs. 0.82, 0.92 vs. 0.88, 0.81 vs 0.68 and 37.90 vs. 18.80, respectively. CONCLUSIONS: Both serum and urinary CAPAP have the potential to act as a stratification marker on admission in predicting severity of acute pancreatitis.
[Mh] Termos MeSH primário: Carboxipeptidase B/sangue
Pancreatite/sangue
Pancreatite/diagnóstico
Admissão do Paciente
Índice de Gravidade de Doença
[Mh] Termos MeSH secundário: Biomarcadores/sangue
Seres Humanos
Admissão do Paciente/tendências
Valor Preditivo dos Testes
[Pt] Tipo de publicação:JOURNAL ARTICLE; META-ANALYSIS; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Biomarkers); EC 3.4.17.2 (Carboxypeptidase B)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:150623
[Lr] Data última revisão:
150623
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150430
[St] Status:MEDLINE


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[PMID]:25903579
[Au] Autor:Bouchal P; Dvoráková M; Roumeliotis T; Bortlícek Z; Ihnatová I; Procházková I; Ho JT; Maryás J; Imrichová H; Budinská E; Vyzula R; Garbis SD; Vojtesek B; Nenutil R
[Ad] Endereço:From the ‡Masaryk Memorial Cancer Institute, Regional Centre for Applied Molecular Oncology, Brno, Czech Republic; §Masaryk University, Faculty of Science, Department of Biochemistry, Brno, Czech Republic;
[Ti] Título:Combined Proteomics and Transcriptomics Identifies Carboxypeptidase B1 and Nuclear Factor κB (NF-κB) Associated Proteins as Putative Biomarkers of Metastasis in Low Grade Breast Cancer.
[So] Source:Mol Cell Proteomics;14(7):1814-30, 2015 Jul.
[Is] ISSN:1535-9484
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Current prognostic factors are insufficient for precise risk-discrimination in breast cancer patients with low grade breast tumors, which, in disagreement with theoretical prognosis, occasionally form early lymph node metastasis. To identify markers for this group of patients, we employed iTRAQ-2DLC-MS/MS proteomics to 24 lymph node positive and 24 lymph node negative grade 1 luminal A primary breast tumors. Another group of 48 high-grade tumors (luminal B, triple negative, Her-2 subtypes) was also analyzed to investigate marker specificity for grade 1 luminal A tumors. From the total of 4405 proteins identified (FDR < 5%), the top 65 differentially expressed together with 30 previously identified and control markers were analyzed also at transcript level. Increased levels of carboxypeptidase B1 (CPB1), PDZ and LIM domain protein 2 (PDLIM2), and ring finger protein 25 (RNF25) were associated specifically with lymph node positive grade 1 tumors, whereas stathmin 1 (STMN1) and thymosin beta 10 (TMSB10) associated with aggressive tumor phenotype also in high grade tumors at both protein and transcript level. For CPB1, these differences were also observed by immunohistochemical analysis on tissue microarrays. Up-regulation of putative biomarkers in lymph node positive (versus negative) luminal A tumors was validated by gene expression analysis of an independent published data set (n = 343) for CPB1 (p = 0.00155), PDLIM2 (p = 0.02027) and RELA (p = 0.00015). Moreover, statistically significant connections with patient survival were identified in another public data set (n = 1678). Our findings indicate unique pro-metastatic mechanisms in grade 1 tumors that can include up-regulation of CPB1, activation of NF-κB pathway and changes in cell survival and cytoskeleton. These putative biomarkers have potential to identify the specific minor subpopulation of breast cancer patients with low grade tumors who are at higher than expected risk of recurrence and who would benefit from more intensive follow-up and may require more personalized therapy.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/metabolismo
Neoplasias da Mama/genética
Neoplasias da Mama/metabolismo
Carboxipeptidase B/metabolismo
Perfilação da Expressão Gênica/métodos
NF-kappa B/metabolismo
Proteômica/métodos
[Mh] Termos MeSH secundário: Biomarcadores Tumorais/genética
Bases de Dados de Proteínas
Feminino
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Imuno-Histoquímica
Marcação por Isótopo
Estimativa de Kaplan-Meier
Gradação de Tumores
Metástase Neoplásica
Reprodutibilidade dos Testes
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (CPB1 protein, human); 0 (NF-kappa B); EC 3.4.17.2 (Carboxypeptidase B)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150424
[St] Status:MEDLINE
[do] DOI:10.1074/mcp.M114.041335


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[PMID]:25521592
[Au] Autor:Tham HW; Balasubramaniam VR; Tejo BA; Ahmad H; Hassan SS
[Ad] Endereço:Virus-Host Interaction Research Group, Infectious Disease Laboratory, Jeffrey Cheah School of Medicine and Health Sciences, Monash University Malaysia, Jalan Lagoon Selatan, Bandar Sunway, 47500 Subang Jaya, Selangor, Malaysia. hwtha1@student.monash.edu.
[Ti] Título:CPB1 of Aedes aegypti interacts with DENV2 E protein and regulates intracellular viral accumulation and release from midgut cells.
[So] Source:Viruses;6(12):5028-46, 2014 Dec 16.
[Is] ISSN:1999-4915
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Aedes aegypti is a principal vector responsible for the transmission of dengue viruses (DENV). To date, vector control remains the key option for dengue disease management. To develop new vector control strategies, a more comprehensive understanding of the biological interactions between DENV and Ae. aegypti is required. In this study, a cDNA library derived from the midgut of female adult Ae. aegypti was used in yeast two-hybrid (Y2H) screenings against DENV2 envelope (E) protein. Among the many interacting proteins identified, carboxypeptidase B1 (CPB1) was selected, and its biological interaction with E protein in Ae. aegypti primary midgut cells was further validated. Our double immunofluorescent assay showed that CPB1-E interaction occurred in the endoplasmic reticulum (ER) of the Ae. aegypti primary midgut cells. Overexpression of CPB1 in mosquito cells resulted in intracellular DENV2 genomic RNA or virus particle accumulation, with a lower amount of virus release. Therefore, we postulated that in Ae. aegypti midgut cells, CPB1 binds to the E protein deposited on the ER intraluminal membranes and inhibits DENV2 RNA encapsulation, thus inhibiting budding from the ER, and may interfere with immature virus transportation to the trans-Golgi network.
[Mh] Termos MeSH primário: Aedes/enzimologia
Carboxipeptidase B/metabolismo
Vírus da Dengue/fisiologia
Proteínas de Insetos/metabolismo
Insetos Vetores/enzimologia
Proteínas do Envelope Viral/metabolismo
Liberação de Vírus
[Mh] Termos MeSH secundário: Aedes/genética
Aedes/virologia
Animais
Carboxipeptidase B/genética
Vírus da Dengue/genética
Feminino
Trato Gastrointestinal/metabolismo
Trato Gastrointestinal/virologia
Proteínas de Insetos/genética
Insetos Vetores/genética
Insetos Vetores/virologia
Ligação Proteica
Proteínas do Envelope Viral/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Insect Proteins); 0 (Viral Envelope Proteins); EC 3.4.17.2 (Carboxypeptidase B)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141219
[St] Status:MEDLINE
[do] DOI:10.3390/v6125028



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