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Pesquisa : D08.811.277.656.350.100.755 [Categoria DeCS]
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[PMID]:26078706
[Au] Autor:Perez I; Blanco L; Sanz B; Errarte P; Ariz U; Beitia M; Fernández A; Loizate A; Candenas ML; Pinto FM; Gil J; López JI; Larrinaga G
[Ad] Endereço:1. Department of Nursing I, School of Nursing, University of the Basque Country (UPV/EHU), Leioa, Bizkaia, Spain ; 2. Department of Physiology, Faculty of Medicine and Dentistry, University of the Basque Country (UPV/EHU), Leioa, Bizkaia, Spain ; 6. BioCruces Health Research Institute, Barakaldo, Bi
[Ti] Título:Altered Activity and Expression of Cytosolic Peptidases in Colorectal Cancer.
[So] Source:Int J Med Sci;12(6):458-67, 2015.
[Is] ISSN:1449-1907
[Cp] País de publicação:Australia
[La] Idioma:eng
[Ab] Resumo:BACKGROUND AND OBJECTIVE: The role of peptidases in carcinogenic processes and their potential usefulness as tumor markers in colorectal cancer (CRC) have been classically attributed to cell-surface enzymes. The objective of the present study was to analyze the activity and mRNA expression of three cytosolic peptidases in the CRC and to correlate the obtained results with classic histopathological parameters for tumor prognosis and survival. METHODS: The activity and mRNA levels of puromycin-sensitive aminopeptidase (PSA), aminopeptidase B (APB) and pyroglutamyl-peptidase I (PGI) were measured by fluorimetric and quantitative RT-PCR methods in colorectal mucosa and tumor tissues and plasma samples from CRC patients (n=81). RESULTS: 1) PSA and APB activity was higher in adenomas and carcinomas than in the uninvolved mucosa. 2) mRNA levels of PSA and PGI was lower in tumors. 3) PGI activity in CRC tissue correlated negatively with histological grade, tumor size and 5-year overall survival of CRC patients. 4) Higher plasmatic APB activity was independently associated with better 5-year overall survival. CONCLUSIONS: Data suggest that cytosolic peptidases may be involved in colorectal carcinogenesis and point to the determination of this enzymes as a valuable method in the determination of CRC prognosis.
[Mh] Termos MeSH primário: Aminopeptidases/biossíntese
Neoplasias Colorretais/genética
Piroglutamil-Peptidase I/biossíntese
[Mh] Termos MeSH secundário: Idoso
Aminopeptidases/genética
Neoplasias Colorretais/enzimologia
Neoplasias Colorretais/patologia
Citosol/enzimologia
Intervalo Livre de Doença
Feminino
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Estimativa de Kaplan-Meier
Masculino
Meia-Idade
Prognóstico
Piroglutamil-Peptidase I/genética
RNA Mensageiro/biossíntese
RNA Mensageiro/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Messenger); EC 3.4.11.- (Aminopeptidases); EC 3.4.11.14 (enkephalin degrading enzyme); EC 3.4.11.6 (aminopeptidase B); EC 3.4.19.3 (Pyroglutamyl-Peptidase I)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150617
[St] Status:MEDLINE
[do] DOI:10.7150/ijms.11808


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[PMID]:25687677
[Au] Autor:Megias MJ; Alba-Araguez F; Luna JD; Vives F; Ramirez-Sanchez M
[Ti] Título:Serum pyroglutamyl aminopeptidase activity: a promising novel biomarker candidate for liver cirrhosis.
[So] Source:Endocr Regul;49(1):20-4, 2015 Jan.
[Is] ISSN:1210-0668
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: As a reflect of tissue damage, serum aminopeptidases have been proposed as biomarkers of various diseases. In order to search new serologic markers for liver cirrhosis we conducted a preliminary study in which we analyzed a broad range of aminopeptidase activities in serum of controls and patients diagnosed with pancreatitis, hepatitis, and liver cirrhosis without distinction among the etiological type or the degree of severity of each condition. METHODS: Alanyl-, arginyl-, glutamyl-, cystinyl- pyroglutamyl-, and aspartyl-aminopeptidase activities were analyzed fluorometrically, using aminoacyl-ß-naphthylamides as substrates. In addition, various parameters, such as alanine transaminase, aspartate transaminase, alkaline phosphatase, total bilirubin, direct bilirubin, and gamma glutamyl transpeptidase were assayed as routine laboratory test for liver function. RESULTS: Compared with control group, alanyl- and arginyl-aminopeptidase activities increased nonspecifically in pancreatitis, hepatitis and liver cirrhosis, glutamyl- and cystinyl-aminopeptidases did not differ between groups and pyroglutamyl-aminopeptidase demonstrated that while pancreatitis and hepatitis did not differ between them and with controls, this activity decreased selectively in liver cirrhosis compared with all the rest of groups (p<0.001 vs. control and p<0.01 vs. pancreatitis and hepatitis). Aspartyl-aminopeptidase also decreased significantly (p<0.05) in liver cirrhosis compared with controls. Routine parameters for liver function test increased, as expected, in the three pathologies analyzed. CONCLUSIONS: Despite the heterogeneous composition of the three patient groups, the specific reduction of the levels of pyroglutamyl-aminopeptidase activity in serum of liver cirrhosis patients might be considered as a potential candidate to be included in a combination of markers for the diagnosis of this disease.
[Mh] Termos MeSH primário: Biomarcadores/sangue
Cirrose Hepática/sangue
Cirrose Hepática/diagnóstico
Piroglutamil-Peptidase I/sangue
[Mh] Termos MeSH secundário: Adulto
Idoso
Idoso de 80 Anos ou mais
Estudos de Casos e Controles
Diagnóstico Diferencial
Feminino
Hepatite/sangue
Seres Humanos
Masculino
Meia-Idade
Pancreatite/sangue
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); EC 3.4.19.3 (Pyroglutamyl-Peptidase I)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150218
[St] Status:MEDLINE


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[PMID]:24379520
[Au] Autor:Larrinaga G; Blanco L; Errarte P; Beitia M; Sanz B; Perez I; Irazusta A; Sánchez CE; Santaolalla F; Andrés L; López JI
[Ad] Endereço:Department of Nursing I, University School of Nursing, University of the Basque Country, P.O. Box 699, 48080 Bilbao, Bizkaia, Spain ; Department of Physiology, Faculty of Medicine and Dentistry, University of the Basque Country, Bilbao, Spain ; BioCruces Research Institute, Spain.
[Ti] Título:Altered peptidase activities in thyroid neoplasia and hyperplasia.
[So] Source:Dis Markers;35(6):825-32, 2013.
[Is] ISSN:1875-8630
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Papillary thyroid carcinoma (PTC), follicular thyroid adenoma (FTA), and thyroid nodular hyperplasia (TNH) are the most frequent diseases of the thyroid gland. Previous studies described the involvement of dipeptidyl-peptidase IV (DPPIV/CD26) in the development of thyroid neoplasia and proposed it as an additional tool in the diagnosis/prognosis of these diseases. However, very little is known about the involvement of other peptidases in neoplastic and hyperplastic processes of this gland. METHODS: The catalytic activity of 10 peptidases in a series of 30 PTC, 10 FTA, and 14 TNH was measured fluorimetrically in tumour and nontumour adjacent tissues. RESULTS: The activity of DPPIV/CD26 was markedly higher in PTC than in FTA, TNH, and nontumour tissues. Aspartyl aminopeptidase (AspAP), alanyl aminopeptidase (AlaAP), prolyl endopeptidase, pyroglutamyl peptidase I, and aminopeptidase B activities were significantly increased in thyroid neoplasms when compared to nontumour tissues. AspAP and AlaAP activities were also significantly higher in PTC than in FTA and TNH. CONCLUSIONS: These data suggest the involvement of DPPIV/CD26 and some cytosolic peptidases in the neoplastic development of PTC and FTA. Further studies will help to define the possible clinical usefulness of AlaAP and AspAP in the diagnosis/prognosis of thyroid neoplasms.
[Mh] Termos MeSH primário: Adenocarcinoma Folicular/enzimologia
Carcinoma Papilar/enzimologia
Dipeptidil Peptidase 4/metabolismo
Glândula Tireoide/enzimologia
Neoplasias da Glândula Tireoide/enzimologia
[Mh] Termos MeSH secundário: Adulto
Antígenos CD13/metabolismo
Feminino
Glutamil Aminopeptidase/metabolismo
Seres Humanos
Hiperplasia/enzimologia
Masculino
Meia-Idade
Piroglutamil-Peptidase I/metabolismo
Serina Endopeptidases/metabolismo
Glândula Tireoide/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.4.11.2 (CD13 Antigens); EC 3.4.11.7 (Glutamyl Aminopeptidase); EC 3.4.14.5 (DPP4 protein, human); EC 3.4.14.5 (Dipeptidyl Peptidase 4); EC 3.4.19.3 (Pyroglutamyl-Peptidase I); EC 3.4.21.- (Serine Endopeptidases); EC 3.4.21.26 (prolyl oligopeptidase)
[Em] Mês de entrada:1407
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140101
[St] Status:MEDLINE
[do] DOI:10.1155/2013/970736


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[PMID]:22799522
[Au] Autor:Mizuguchi M; Takeuchi M; Ohki S; Nabeshima Y; Kouno T; Aizawa T; Demura M; Kawano K; Yutani K
[Ad] Endereço:Faculty of Pharmaceutical Sciences, University of Toyama, 2630, Sugitani, Toyama 930-0194, Japan. mineyuki@pha.u-toyama.ac.jp
[Ti] Título:Structural characterization of a trapped folding intermediate of pyrrolidone carboxyl peptidase from a hyperthermophile.
[So] Source:Biochemistry;51(31):6089-96, 2012 Aug 07.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The refolding of cysteine-free pyrrolidone carboxyl peptidase (PCP-0SH) from a hyperthermophile is unusually slow. PCP-0SH is trapped in the denatured (D1) state at 4 °C and pH 2.3, which is different from the highly denatured state in the presence of concentrated denaturant. In order to elucidate the mechanism of the unusually slow folding, we investigated the structure of the D1 state using NMR techniques with amino acid selectively labeled PCP-0SH. The HSQC spectrum of the D1 state showed that most of the resonances arising from the 114-208 residues are broadened, indicating that conformations of the 114-208 residues are in intermediate exchange on the microsecond to millisecond time scale. Paramagnetic relaxation enhancement data indicated the lack of long-range interactions between the 1-113 and the 114-208 segments in the D1 state. Furthermore, proline scanning mutagenesis showed that the 114-208 segment in the D1 state forms a loosely packed hydrophobic core composed of α4- and α6-helices. From these findings, we conclude that the 114-208 segment of PCP-0SH folds into a stable compact structure with non-native helix-helix association in the D1 state. Therefore, in the folding process from the D1 state to the native state, the α4- and α6-helices become separated and the central ß-sheet is folded between these helices. That is, the non-native interaction between the α4- and α6-helices may be responsible for the unusually slow folding of PCP-0SH.
[Mh] Termos MeSH primário: Temperatura Alta
Dobramento de Proteína
Pyrococcus furiosus/enzimologia
Piroglutamil-Peptidase I/química
[Mh] Termos MeSH secundário: Naftalenossulfonato de Anilina/química
Concentração de Íons de Hidrogênio
Interações Hidrofóbicas e Hidrofílicas
Modelos Moleculares
Mutagênese Sítio-Dirigida
Mutação
Estrutura Secundária de Proteína
Piroglutamil-Peptidase I/genética
Espectrometria de Fluorescência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (8-anilino-1-naphthalenesulfonic acid); 0 (Anilino Naphthalenesulfonates); EC 3.4.19.3 (Pyroglutamyl-Peptidase I)
[Em] Mês de entrada:1211
[Cu] Atualização por classe:120921
[Lr] Data última revisão:
120921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120718
[St] Status:MEDLINE


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[PMID]:22381154
[Au] Autor:Carrera-González Mdel P; Ramírez-Expósito MJ; Dueñas B; Martínez-Ferrol J; Mayas MD; Martínez-Martos JM
[Ad] Endereço:Experimental and Clinical Physiopathology Research Group, Department of Health Sciences, Faculty of Experimental and Health Sciences, University of Jaén, Jaén, Spain. pcarrera@ujaen.es
[Ti] Título:Putative relationship between hormonal status and serum pyrrolidone carboxypeptidase activity in pre- and post- menopausal women with breast cancer.
[So] Source:Breast;21(6):751-4, 2012 Dec.
[Is] ISSN:1532-3080
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:In breast cancer, hormonal changes are rather constant in post-menopausal women since they tend to vary only over long time spans. However, in pre-menopausal women, the development of breast cancer is associated with hormonal physiological variations. The aim of the present work was to analyse the changes in circulating levels of gonadotropin-releasing hormone (GnRH), follicle-stimulating hormone (FSH) and luteinizing hormone (LH) in pre- and post-menopausal women that were healthy or with breast cancer, and their connection to serum pyrrolidone carboxypeptidase (Pcp) activity. We observed significant changes in the hormonal profile in post-menopausal women with breast cancer compared to the control group. In pre-menopausal women, we found significant changes in circulating GnRH levels with respect to the healthy group. Our present results support the existence of neuroendocrine misregulation that could be involved in tumour progression, with Pcp being a potentially new pharmacological target in breast cancer treatments.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/sangue
Neoplasias da Mama/enzimologia
Carcinoma Ductal de Mama/enzimologia
Pós-Menopausa/sangue
Pré-Menopausa/sangue
Piroglutamil-Peptidase I/sangue
[Mh] Termos MeSH secundário: Adulto
Idoso
Idoso de 80 Anos ou mais
Neoplasias da Mama/sangue
Carcinoma Ductal de Mama/sangue
Estudos de Casos e Controles
Feminino
Hormônio Foliculoestimulante Humano/sangue
Hormônio Liberador de Gonadotropina/sangue
Seres Humanos
Hormônio Luteinizante/sangue
Meia-Idade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (Follicle Stimulating Hormone, Human); 33515-09-2 (Gonadotropin-Releasing Hormone); 9002-67-9 (Luteinizing Hormone); EC 3.4.19.3 (Pyroglutamyl-Peptidase I)
[Em] Mês de entrada:1305
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120303
[St] Status:MEDLINE


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[PMID]:21937126
[Au] Autor:Larrinaga G; Perez I; Sanz B; Irazusta A; Zarrazquin I; Sanchez CE; Sanchez CE; Rey AS; Zabala A; Santaolalla F
[Ad] Endereço:Department of Physiology, School of Medicine, University of the Basque Country, Spain.
[Ti] Título:Activity of soluble aminopeptidase A and dipeptidyl peptidase IV and membrane-bound aminopeptidase B and pyroglutamyl peptidase I in adenoid hyperplasia, tonsillar hyperplasia and chronic tonsillitis.
[So] Source:Int J Pediatr Otorhinolaryngol;75(11):1399-403, 2011 Nov.
[Is] ISSN:1872-8464
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To analyze soluble and membrane-bound peptidase activities in the tonsils and adenoids removed from patients with adenoid hyperplasia, tonsillar hyperplasia and chronic tonsillitis. METHODS: A total of 48 tissue samples from patients undergoing adenoidectomy and tonsillectomy for adenoid hyperplasia, tonsillar hyperplasia or chronic tonsillitis were analyzed. The catalytic activity of a pool of peptidases in the soluble (dipeptidyl peptidase IV, aminopeptidase A, aminopeptidase N and cystinyl aminopeptidase) and membrane-bound (prolyl endopeptidase, aspartyl aminopeptidase, aminopeptidase B and pyroglutamyl peptidase I) fractions was measured fluorometrically. RESULTS: The activity of membrane-bound aminopeptidase B was higher in cases of chronic tonsillitis and adenoid hyperplasia than in tonsillar hyperplasia, p=0.004. Soluble dipeptidyl peptidase IV and membrane-bound pyroglutamyl peptidase I were found to be more active in tissues from male chronic tonsillitis tissues, p<0.05, while membrane-bound aminopeptidase B activity was higher in tissues of females with tonsillar hyperplasia, p<0.001. In the case of chronic tonsillitis, soluble aminopeptidase A was found to have a higher level of activity in tissues from children than those from adults, p=0.005. CONCLUSIONS: Our results suggest a potential role of soluble aminopeptidase A, soluble dipeptidyl peptidase IV, membrane-bound aminopeptidase B and membrane-bound pyroglutamyl peptidase I in the pathobiology of adenoid hyperplasia, tonsillar hyperplasia and chronic tonsillitis that is differently regulated as a function of gender. These finfings may modify in the future the clinical approach to these diseases.
[Mh] Termos MeSH primário: Tonsila Faríngea/metabolismo
Aminopeptidases/metabolismo
Tonsila Palatina/metabolismo
[Mh] Termos MeSH secundário: Tonsila Faríngea/patologia
Aminopeptidases/análise
Análise de Variância
Biomarcadores/análise
Criança
Pré-Escolar
Doença Crônica
Estudos de Coortes
Dipeptidil Peptidase 4/análise
Dipeptidil Peptidase 4/metabolismo
Feminino
Glutamil Aminopeptidase/análise
Glutamil Aminopeptidase/metabolismo
Seres Humanos
Hiperplasia/metabolismo
Hiperplasia/patologia
Masculino
Tonsila Palatina/patologia
Piroglutamil-Peptidase I/análise
Piroglutamil-Peptidase I/metabolismo
Estudos Retrospectivos
Sensibilidade e Especificidade
Índice de Gravidade de Doença
Tonsilectomia/métodos
Tonsilite/metabolismo
Tonsilite/patologia
Tonsilite/cirurgia
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biomarkers); EC 3.4.11.- (Aminopeptidases); EC 3.4.11.6 (aminopeptidase B); EC 3.4.11.7 (Glutamyl Aminopeptidase); EC 3.4.14.5 (Dipeptidyl Peptidase 4); EC 3.4.19.3 (Pyroglutamyl-Peptidase I)
[Em] Mês de entrada:1202
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110923
[St] Status:MEDLINE
[do] DOI:10.1016/j.ijporl.2011.07.037


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[PMID]:21400688
[Au] Autor:Leone JW; Hampton B; Fowler E; Moyer M; Krishna RG; Chin CC
[Ad] Endereço:Pfizer VMRD, Kalamazoo, Michigan, USA.
[Ti] Título:Removal of N-terminal blocking groups from proteins.
[So] Source:Curr Protoc Protein Sci;Chapter 11:Unit11.7, 2011 Feb.
[Is] ISSN:1934-3663
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Two enzymatic methods commonly used in N-terminal sequence analysis of blocked proteins are presented: one uses pyroglutamate aminopeptidase for N(α)-pyrrolidone carboxyl-proteins in solution or blotted onto a membrane, and the other uses acylaminoacyl-peptide hydrolase for N(α)-acyl-proteins blocked with other acyl groups. A Support Protocol describes a colorimetric assay for pyroglutamate aminopeptidase activity. Sequencing with acylaminoacyl-peptide hydrolase must include fragmentation of the protein before unblocking, so procedures are provided for chemically blocking newly generated peptides with either succinic anhydride or phenylisothiocyanate/performic acid. The hydrolase is then applied to the total mixture of peptides, only one of which, the acylated N-terminal peptide, should be a substrate for hydrolase. After incubation, the mixture of peptides is subjected to sequence analysis.
[Mh] Termos MeSH primário: Bioquímica/métodos
Peptídeos/metabolismo
Proteínas/química
Proteínas/metabolismo
Análise de Sequência/métodos
[Mh] Termos MeSH secundário: Acilação
Colorimetria
Formiatos/metabolismo
Hidrolases/metabolismo
Isotiocianatos/metabolismo
Fragmentos de Peptídeos/metabolismo
Peptídeo Hidrolases/metabolismo
Piroglutamil-Peptidase I/metabolismo
Ácido Pirrolidonocarboxílico/química
Ácido Pirrolidonocarboxílico/isolamento & purificação
Soluções
Anidridos Succínicos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Formates); 0 (Isothiocyanates); 0 (Peptide Fragments); 0 (Peptides); 0 (Proteins); 0 (Solutions); 0 (Succinic Anhydrides); 0D58F84LSU (phenylisothiocyanate); 107-32-4 (peroxyformic acid); 6RF4O17Z8J (succinic anhydride); EC 3.- (Hydrolases); EC 3.4.- (Peptide Hydrolases); EC 3.4.19.1 (acylaminoacyl-peptidase); EC 3.4.19.3 (Pyroglutamyl-Peptidase I); SZB83O1W42 (Pyrrolidonecarboxylic Acid)
[Em] Mês de entrada:1106
[Cu] Atualização por classe:161021
[Lr] Data última revisão:
161021
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110315
[St] Status:MEDLINE
[do] DOI:10.1002/0471140864.ps1107s63


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[PMID]:21282104
[Au] Autor:Liu YD; Goetze AM; Bass RB; Flynn GC
[Ad] Endereço:Department of Process and Product Development, Amgen Inc., Thousand Oaks, California 91320, USA.
[Ti] Título:N-terminal glutamate to pyroglutamate conversion in vivo for human IgG2 antibodies.
[So] Source:J Biol Chem;286(13):11211-7, 2011 Apr 01.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Therapeutic proteins contain a large number of post-translational modifications, some of which could potentially impact their safety or efficacy. In one of these changes, pyroglutamate can form on the N terminus of the polypeptide chain. Both glutamine and glutamate at the N termini of recombinant monoclonal antibodies can cyclize spontaneously to pyroglutamate (pE) in vitro. Glutamate conversion to pyroglutamate occurs more slowly than from glutamine but has been observed under near physiological conditions. Here we investigated to what extent human IgG2 N-terminal glutamate converts to pE in vivo. Pyroglutamate levels increased over time after injection into humans, with the rate of formation differing between polypeptide chains. These changes were replicated for the same antibodies in vitro under physiological pH and temperature conditions, indicating that the changes observed in vivo were due to chemical conversion not differential clearance. Differences in the conversion rates between the light chain and heavy chain on an antibody were eliminated by denaturing the protein, revealing that structural elements affect pE formation rates. By enzymatically releasing pE from endogenous antibodies isolated from human serum, we could estimate the naturally occurring levels of this post-translational modification. Together, these techniques and results can be used to predict the exposure of pE for therapeutic antibodies and to guide criticality assessments for this attribute.
[Mh] Termos MeSH primário: Anticorpos Monoclonais/química
Ácido Glutâmico/química
Imunoglobulina G/química
Ácido Pirrolidonocarboxílico/química
[Mh] Termos MeSH secundário: Animais
Anticorpos Monoclonais/metabolismo
Anticorpos Monoclonais/uso terapêutico
Proteínas Arqueais/química
Células CHO
Cricetinae
Cricetulus
Ácido Glutâmico/metabolismo
Seres Humanos
Imunoglobulina G/metabolismo
Imunoglobulina G/uso terapêutico
Processamento de Proteína Pós-Traducional
Pyrococcus furiosus/enzimologia
Piroglutamil-Peptidase I/química
Ácido Pirrolidonocarboxílico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Archaeal Proteins); 0 (Immunoglobulin G); 3KX376GY7L (Glutamic Acid); EC 3.4.19.3 (Pyroglutamyl-Peptidase I); SZB83O1W42 (Pyrrolidonecarboxylic Acid)
[Em] Mês de entrada:1106
[Cu] Atualização por classe:150205
[Lr] Data última revisão:
150205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110202
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M110.185041


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[PMID]:19329603
[Au] Autor:Tappe D; Pukall R; Schumann P; Gronow S; Spiliotis M; Claus H; Brehm K; Vogel U
[Ad] Endereço:Institute of Hygiene and Microbiology, University of Würzburg, Josef-Schneider-Strasse 2, D-97080 Würzburg, Germany.
[Ti] Título:Streptococcus merionis sp. nov., isolated from Mongolian jirds (Meriones unguiculatus).
[So] Source:Int J Syst Evol Microbiol;59(Pt 4):766-70, 2009 Apr.
[Is] ISSN:1466-5026
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Gram-positive, catalase-negative, chain-forming, coccus-shaped organisms were isolated both from intraperitoneally grown vesicles of the fox tapeworm Echinococcus multilocularis and the oropharynges of laboratory-kept Mongolian jirds (Meriones unguiculatus). The strains displayed no haemolytic activity on Columbia sheep blood agar, pyrrolidonyl arylamidase activity was negative and the organisms reacted weakly with Lancefield group D antiserum. On the basis of phenotypic characteristics, the strains were tentatively identified as members of the genus Streptococcus. Comparative 16S rRNA gene sequencing studies confirmed their assignment to the genus Streptococcus and revealed that Streptococcus hyointestinalis DSM 20770(T) was their closest phylogenetic neighbour (96.5 % sequence similarity). The levels of 16S rRNA gene sequence similarity between the isolates and representatives of species of the genus Streptococcus were only 95.7-96.2 %. On the basis of the phenotypic and molecular data presented, the isolates from Mongolian jirds represent a novel species of the genus Streptococcus, for which the name Streptococcus merionis sp. nov. is proposed. The type strain is WUE3771(T) (=DSM 19192(T)=CCUG 54871(T)).
[Mh] Termos MeSH primário: Echinococcus multilocularis/microbiologia
Gerbillinae/microbiologia
Streptococcus/classificação
Streptococcus/isolamento & purificação
[Mh] Termos MeSH secundário: Animais
Técnicas de Tipagem Bacteriana
Análise por Conglomerados
DNA Bacteriano/química
DNA Bacteriano/genética
DNA Ribossômico/química
DNA Ribossômico/genética
Hemólise
Dados de Sequência Molecular
Mongólia
Filogenia
Piroglutamil-Peptidase I/metabolismo
RNA Ribossômico 16S/genética
Análise de Sequência de DNA
Homologia de Sequência do Ácido Nucleico
Streptococcus/genética
Streptococcus/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (DNA, Ribosomal); 0 (RNA, Ribosomal, 16S); EC 3.4.19.3 (Pyroglutamyl-Peptidase I)
[Em] Mês de entrada:0905
[Cu] Atualização por classe:090330
[Lr] Data última revisão:
090330
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090331
[St] Status:MEDLINE
[do] DOI:10.1099/ijs.0.65823-0


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[PMID]:18501515
[Au] Autor:Mayas MD; Ramírez-Expósito MJ; García-López MJ; Carrera MP; Martínez-Martos JM
[Ad] Endereço:Fundación IMABIS, Hospital Carlos Haya, Málaga, Spain.
[Ti] Título:Chronic ethanol intake modifies pyrrolidon carboxypeptidase activity in mouse frontal cortex synaptosomes under resting and K+ -stimulated conditions: role of calcium.
[So] Source:Neurosci Lett;439(1):75-8, 2008 Jul 04.
[Is] ISSN:0304-3940
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Pyrrolidon carboxypeptidase (Pcp) is an omega peptidase that removes pyroglutamyl N-terminal residues of peptides such as thyrotrophin-releasing hormone (TRH), which is one of the neuropeptides that has been localized into many areas of the brain and acts as an endogenous neuromodulator of several parameters related to ethanol (EtOH) consumption. In this study, we analysed the effects of chronic EtOH intake on Pcp activity on mouse frontal cortex synaptosomes and their corresponding supernatant under basal and K+ -stimulated conditions, in presence and absence of calcium (Ca2+) to know the regulation of Pcp on TRH. In basal conditions, chronic EtOH intake significantly decreased synaptosomes Pcp activity but only in absence of Ca2+. However, supernatant Pcp activity is also decreased in presence and absence of calcium. Under K+-stimulated conditions, chronic EtOH intake decreased synaptosomes Pcp activity but only in absence of Ca2+, whereas supernatant Pcp activity was significantly decreased only in presence of Ca2+. The general inhibitory effect of chronic EtOH intake on Pcp activity suggests an inhibition of TRH metabolism and an enhancement of TRH neurotransmitter/neuromodulator functions, which could be related to putative processes of tolerance to EtOH in which TRH has been involved. Our data may also indicate that active peptides and their degrading peptidases are released together to the synaptic cleft to regulate the neurotransmitter/neuromodulator functions of these peptides, through a Ca2+ -dependent mechanism.
[Mh] Termos MeSH primário: Cálcio/fisiologia
Depressores do Sistema Nervoso Central/administração & dosagem
Etanol/administração & dosagem
Lobo Frontal/ultraestrutura
Piroglutamil-Peptidase I/metabolismo
Sinaptossomos/metabolismo
[Mh] Termos MeSH secundário: Animais
Comportamento Animal
Lobo Frontal/efeitos dos fármacos
Lobo Frontal/enzimologia
Masculino
Camundongos
Camundongos Endogâmicos BALB C
Potássio/farmacologia
Sinaptossomos/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Central Nervous System Depressants); 3K9958V90M (Ethanol); EC 3.4.19.3 (Pyroglutamyl-Peptidase I); RWP5GA015D (Potassium); SY7Q814VUP (Calcium)
[Em] Mês de entrada:0809
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:080527
[St] Status:MEDLINE
[do] DOI:10.1016/j.neulet.2008.04.093



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