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[PMID]:27143370
[Au] Autor:Timofeev АV
[Ad] Endereço:Russian Research Institute of Haematology and Transfusiology, Saint Petersburg, Russia.
[Ti] Título:[Basic carboxypeptidases of blood: significance for coagulology].
[So] Source:Biomed Khim;62(2):141-9, 2016 Mar-Apr.
[Is] ISSN:2310-6972
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:This review considers the basic metallocarboxypeptidases of human blood and their role in coagulologic disorders. In includes information on the history of the discovery and biological characteristics of potential enzymes-regulators of the fibrinolytic process: carboxypeptidase U and carboxypeptidase N. Certain attention is paid to the biochemical mechanisms and the main modern concepts of the antifibrinolytic effects of these enzymes.
[Mh] Termos MeSH primário: Coagulação Sanguínea/fisiologia
Carboxipeptidases/sangue
[Mh] Termos MeSH secundário: Transtornos da Coagulação Sanguínea/diagnóstico
Transtornos da Coagulação Sanguínea/enzimologia
Carboxipeptidase B2/química
Carboxipeptidase B2/metabolismo
Carboxipeptidases/metabolismo
Fibrina/metabolismo
Fibrinólise/fisiologia
Seres Humanos
Lisina Carboxipeptidase/química
Lisina Carboxipeptidase/metabolismo
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
9001-31-4 (Fibrin); EC 3.4.- (Carboxypeptidases); EC 3.4.17.20 (CPB2 protein, human); EC 3.4.17.20 (Carboxypeptidase B2); EC 3.4.17.3 (Lysine Carboxypeptidase)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:160504
[Lr] Data última revisão:
160504
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160505
[St] Status:MEDLINE
[do] DOI:10.18097/PBMC20166202141


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[PMID]:26860443
[Au] Autor:Cui R; Zhang P; Li Y
[Ti] Título:Role of Carboxypeptidase N Invasion and Migration in Breast Cancer.
[So] Source:Anticancer Agents Med Chem;16(9):1198-202, 2016.
[Is] ISSN:1875-5992
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Carboxypeptidase N (CPN) is highly expressed in breast cancer and plays an important role in cleaving specific polypeptide fragments within the tumor microenvironment, so here we studied the important role of its invasion and migration in breast cancer. METHODS: MDA-MB-231, MDA-MB-468, and MCF-7 cells were selected for cell culture. We used real-time polymerase chain reaction (PCR) and western blotting to determine CPN gene and protein expression. If CPN was obviously expressed, we designed and synthesized a molecular sequence using an RNA interference approach to remove the CPN and observed its proliferation, migration, and invasion within tumor cells. RESULTS: Real-time PCR and western blotting show the following CPN expression: minimal in MDA-MB-468 cells but obvious in MDA-MB-231 and MCF7 cells. MDA-MB-231 breast cancer cell lines were selected for the control group and CPN was knocked out for the experimental group. Compared to the control group, the experimental group had significantly less migration and invasion. CONCLUSION: CPN may play an important biological function in breast cancer and will provide a new target for the effective diagnosis and treatment of breast cancer.
[Mh] Termos MeSH primário: Neoplasias da Mama/genética
Mama/patologia
Regulação Neoplásica da Expressão Gênica
Lisina Carboxipeptidase/genética
Invasividade Neoplásica/genética
[Mh] Termos MeSH secundário: Mama/metabolismo
Neoplasias da Mama/patologia
Linhagem Celular Tumoral
Movimento Celular
Feminino
Seres Humanos
Lisina Carboxipeptidase/análise
Células MCF-7
Invasividade Neoplásica/patologia
Interferência de RNA
RNA Interferente Pequeno/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Small Interfering); EC 3.4.17.3 (Lysine Carboxypeptidase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170619
[Lr] Data última revisão:
170619
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160211
[St] Status:MEDLINE


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[PMID]:25720836
[Au] Autor:Dessart P; Defendi F; Humeau H; Nicolie B; Sarre ME; Charignon D; Ponard D; Cichon S; Drouet C; Martin L
[Ad] Endereço:Department of Dermatology, Angers Hospital, L'UNAM University, Angers, France.
[Ti] Título:Distinct conditions support a novel classification for bradykinin-mediated angio-oedema.
[So] Source:Dermatology;230(4):324-31, 2015.
[Is] ISSN:1421-9832
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Angio-oedema (AO) can be attributable to bradykinin (BK) accumulation, as is the case for prototypical hereditary AO (HAO) due to C1 inhibitor (C1-INH) deficiency. However, our clinical experience in a reference centre has shown that some patients display a clinical history suggestive of HAO, but exhibit normal C1-INH function, have no mutation in the causative genes associated with HAO (SERPING1, F12), and report no intake of drugs known to promote AO. OBJECTIVE: We sought to determine the frequency and distribution of different AO subtypes suspected to be BK-mediated AO (BK-AO) and defined by clinical, history and biological criteria (enzyme activities implicated in BK formation and catabolism). METHODS: The files of all patients referred to our centre for suspected BK-AO were retrospectively analysed. RESULTS: The distribution of patients (n = 162) was 16 and 4% with a hereditary deficiency of C1-INH or a gain of factor XII function, respectively, 29% with iatrogenic BK-AO, 21% with non-iatrogenic defective kininase activity and 30% with idiopathic increased kinin formation. CONCLUSION: BK-AO may be caused by multiple inherited or acquired factors triggering BK accumulation. Therefore, we propose a novel typology for BK-AO based on the imbalance of production/catabolism of BK.
[Mh] Termos MeSH primário: Angioedema/classificação
Angioedema/metabolismo
Bradicinina/metabolismo
Proteína Inibidora do Complemento C1/metabolismo
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Idoso de 80 Anos ou mais
Amidoidrolases/metabolismo
Aminopeptidases/genética
Aminopeptidases/metabolismo
Angioedema/etiologia
Antagonistas de Receptores de Angiotensina/efeitos adversos
Inibidores da Enzima Conversora de Angiotensina/efeitos adversos
Criança
Pré-Escolar
Proteínas Inativadoras do Complemento 1/genética
Fator XII/genética
Feminino
Angioedema Hereditário Tipos I e II/complicações
Angioedema Hereditário Tipos I e II/enzimologia
Angioedema Hereditário Tipos I e II/genética
Hormônios/efeitos adversos
Seres Humanos
Lisina Carboxipeptidase/metabolismo
Masculino
Meia-Idade
Peptidil Dipeptidase A/metabolismo
Polimorfismo de Nucleotídeo Único
Recidiva
Estudos Retrospectivos
Urticária/etiologia
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Angiotensin Receptor Antagonists); 0 (Angiotensin-Converting Enzyme Inhibitors); 0 (Complement C1 Inactivator Proteins); 0 (Complement C1 Inhibitor Protein); 0 (Hormones); 0 (SERPING1 protein, human); 9001-30-3 (Factor XII); EC 3.4.11.- (Aminopeptidases); EC 3.4.11.9 (X-Pro aminopeptidase); EC 3.4.15.1 (Peptidyl-Dipeptidase A); EC 3.4.17.3 (Lysine Carboxypeptidase); EC 3.5.- (Amidohydrolases); EC 3.5.1.4 (amidase); S8TIM42R2W (Bradykinin)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:150513
[Lr] Data última revisão:
150513
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150228
[St] Status:MEDLINE
[do] DOI:10.1159/000371814


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[PMID]:25019402
[Au] Autor:Petrushova OP; Mikuliak NI
[Ti] Título:[Proteolytic activity of fetoplacental complex in norm and pathology].
[So] Source:Biomed Khim;60(3):389-96, 2014 May-Jun.
[Is] ISSN:2310-6972
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:The activity of angiotensin converting enzyme (ACE), carboxypeptidase N (CPN), and leucine aminopeptidase (LAP) has been investigated in the fetoplacental complex (FPC) in normal and placental insufficiency (FPI). ACE and LAP activities were significantly higher in the placental tissue than in maternal serum and umbilical vein serum. CPN activity was significantly lower in umbilical vein serum as compared to that of women in childbirth. Probably, the studied enzymes are involved in formation of reduced sensitivity of FPC of blood vessels during physiological pregnancy. In cases of placental insufficiency a significant increase of LAP activity was found in the placental tissue and umbilical vein serum. In addition, the pathological course of pregnancy caused a significant increase of CPN activity in serum of pregnant women in comparison to the norm. The obtained data suggest that during FPI proteolytic enzymes participate in the formation of compensatoty-adaptive reactions in the FPC. Results of this study are interesting in context of development of methods for prevention and correction of metabolic disorders in pathologies of pregnancy.
[Mh] Termos MeSH primário: Feto/enzimologia
Leucil Aminopeptidase/metabolismo
Lisina Carboxipeptidase/metabolismo
Peptidil Dipeptidase A/metabolismo
Placenta/enzimologia
Insuficiência Placentária/enzimologia
[Mh] Termos MeSH secundário: Adulto
Feminino
Feto/irrigação sanguínea
Feto/patologia
Seres Humanos
Placenta/irrigação sanguínea
Placenta/patologia
Insuficiência Placentária/patologia
Gravidez
Proteólise
Veias Umbilicais/química
Veias Umbilicais/enzimologia
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.4.11.1 (Leucyl Aminopeptidase); EC 3.4.15.1 (ACE protein, human); EC 3.4.15.1 (Peptidyl-Dipeptidase A); EC 3.4.17.3 (Lysine Carboxypeptidase)
[Em] Mês de entrada:1408
[Cu] Atualização por classe:140715
[Lr] Data última revisão:
140715
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140715
[St] Status:MEDLINE


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[PMID]:24853572
[Au] Autor:Beaudouin E; Defendi F; Picaud J; Drouet C; Ponard D; Moneret-Vautrin DA
[Ad] Endereço:Service d'Allergologie, Centre Hospitalier E Durkheim, Epinal, France.
[Ti] Título:Iatrogenic angioedema associated with ACEi, sitagliptin, and deficiency of 3 enzymes catabolizing bradykinin.
[So] Source:Eur Ann Allergy Clin Immunol;46(3):119-22, 2014 May.
[Is] ISSN:1764-1489
[Cp] País de publicação:Italy
[La] Idioma:eng
[Ab] Resumo:New concepts of idiopathic and iatrogenic angioedema underline the role of bradykinin, and the importance of catabolizing enzymes. A case is described of Angiotensin converting enzyme inhibitor (ACEi) and sitagliptin induced angioedema, where AO attacks decreased after the withdrawal of lisinopril but resolved only after the withdrawal of sitagliptin, an inhibitor of dipeptylpeptidase IV. ACE, aminopeptidase P and carboxypeptidase N were decreased down to 17%, 42%, 64% of median references values, and remained low one year after the interruption of these drugs: 56%, 28% and 50%, respectively. The combined deficiency of APP and CPN might enhance the inhibiting effect of the DPP IV inhibitor. The fact that this triple deficiency remained latent before and after the treatment indicates that searching for latent enzyme deficiencies should be carried out when there is intention to treat with a combination of drugs interfering with the bradykinin metabolism.
[Mh] Termos MeSH primário: Erros Inatos do Metabolismo dos Aminoácidos/complicações
Aminopeptidases/deficiência
Angioedema/induzido quimicamente
Angioedema/enzimologia
Inibidores da Enzima Conversora de Angiotensina/efeitos adversos
Bradicinina/metabolismo
Inibidores da Dipeptidil Peptidase IV/efeitos adversos
Doença Iatrogênica
Lisinopril/efeitos adversos
Lisina Carboxipeptidase/deficiência
Peptidil Dipeptidase A/deficiência
Pirazinas/efeitos adversos
Triazóis/efeitos adversos
[Mh] Termos MeSH secundário: Erros Inatos do Metabolismo dos Aminoácidos/diagnóstico
Erros Inatos do Metabolismo dos Aminoácidos/enzimologia
Angioedema/diagnóstico
Regulação para Baixo
Interações Medicamentosas
Seres Humanos
Masculino
Meia-Idade
Polimedicação
Fatores de Risco
Fosfato de Sitagliptina
Fatores de Tempo
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Angiotensin-Converting Enzyme Inhibitors); 0 (Dipeptidyl-Peptidase IV Inhibitors); 0 (Pyrazines); 0 (Triazoles); E7199S1YWR (Lisinopril); EC 3.4.11.- (Aminopeptidases); EC 3.4.11.9 (X-Pro aminopeptidase); EC 3.4.15.1 (ACE protein, human); EC 3.4.15.1 (Peptidyl-Dipeptidase A); EC 3.4.17.3 (Lysine Carboxypeptidase); S8TIM42R2W (Bradykinin); TS63EW8X6F (Sitagliptin Phosphate)
[Em] Mês de entrada:1409
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140524
[St] Status:MEDLINE


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[PMID]:24146311
[Au] Autor:Li Y; Li Y; Chen T; Kuklina AS; Bernard P; Esteva FJ; Shen H; Ferrari M; Hu Y
[Ad] Endereço:Department of Nanomedicine, The Methodist Hospital Research Institute, Houston, TX;
[Ti] Título:Circulating proteolytic products of carboxypeptidase N for early detection of breast cancer.
[So] Source:Clin Chem;60(1):233-42, 2014 Jan.
[Is] ISSN:1530-8561
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Carboxypeptidase N (CPN) is important in regulating vasoactive peptide hormones, growth factors, and cytokines by specifically cleaving their C-terminal basic residues. We investigated whether circulating peptides specifically cleaved by CPN in the tumor microenvironment can be stage-specific indicators of breast cancer. METHODS: CPN activity was measured using an ex vivo peptide cleavage assay by incubating synthesized C3f peptide (His6-C3f_S1304-R1320-His6) in interstitial fluids of breast tumors and adjacent normal breast tissues in mice with orthotopic implantation of the human cell line MDA-MB-231. The nature and extent of peptide cleavage by CPN was investigated by fragment profiling using nanopore fractionation and mass spectrometry. The fragment profiles in interstitial fluid correlated with concentrations of CPN-catalyzed peptides in blood samples taken from the tumor-bearing mice, healthy women, and breast cancer patients. CPN expression in the same set of samples was further examined by immunohistochemistry and immunoblotting. RESULTS: We showed that generation of C3f_R1310-L1319 specifically correlated with the CPN expression level. In both the mouse and clinical patient samples, CPN was clearly increased in tumor tissues compared with normal breast tissue, whereas corresponding CPN abundance in blood remained constant. Concentrations of 6 CPN-catalyzed peptides predominantly increased in sera taken from the mice (n = 8) at 2 weeks after orthotopic implantation. Six homologous peptides displayed significantly higher expression in the patients' plasma as early as the first pathologic stage of breast cancer. CONCLUSIONS: Circulating CPN-catalyzed peptide concentrations reflect the CPN activity in tumors. These biomarkers show strong potential for the noninvasive and early diagnosis of breast cancer.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/sangue
Neoplasias da Mama/diagnóstico
Detecção Precoce de Câncer
Lisina Carboxipeptidase/sangue
Peptídeos/sangue
[Mh] Termos MeSH secundário: Animais
Biomarcadores Tumorais/antagonistas & inibidores
Neoplasias da Mama/enzimologia
Modelos Animais de Doenças
Feminino
Seres Humanos
Lisina Carboxipeptidase/metabolismo
Camundongos
Peptídeos/antagonistas & inibidores
Peptidomiméticos
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
Microambiente Tumoral
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (Peptides); 0 (Peptidomimetics); EC 3.4.17.3 (Lysine Carboxypeptidase)
[Em] Mês de entrada:1403
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131023
[St] Status:MEDLINE
[do] DOI:10.1373/clinchem.2013.211953


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[PMID]:24028840
[Au] Autor:Hu X; Wetsel RA; Ramos TN; Mueller-Ortiz SL; Schoeb TR; Barnum SR
[Ad] Endereço:Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
[Ti] Título:Carboxypeptidase N-deficient mice present with polymorphic disease phenotypes on induction of experimental autoimmune encephalomyelitis.
[So] Source:Immunobiology;219(2):104-8, 2014 Feb.
[Is] ISSN:1878-3279
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Carboxypeptidase N (CPN) is a member of the carboxypeptidase family of enzymes that cleave carboxy-terminal lysine and arginine residues from a large number of biologically active peptides and proteins. These enzymes are best known for their roles in modulating the activity of kinins, complement anaphylatoxins and coagulation proteins. Although CPN makes important contributions to acute inflammatory events, little is known about its role in autoimmune disease. In this study we used CPN(-/-) mice in experimental autoimmune encephalomyelitis (EAE), the animal model for multiple sclerosis. Unexpectedly, we observed several EAE disease phenotypes in CPN(-/-) mice compared to wild type mice. The majority of CPN(-/-) mice died within five to seven days after disease induction, before displaying clinical signs of disease. The remaining mice presented with either mild EAE or did not develop EAE. In addition, CPN(-/-) mice injected with complete or incomplete Freund's adjuvant died within the same time frame and in similar numbers as those induced for EAE. Overall, the course of EAE in CPN(-/-) mice was significantly delayed and attenuated compared to wild type mice. Spinal cord histopathology in CPN(-/-) mice revealed meningeal, but not parenchymal leukocyte infiltration, and minimal demyelination. Our results indicate that CPN plays an important role in EAE development and progression and suggests that multiple CPN ligands contribute to the disease phenotypes we observed.
[Mh] Termos MeSH primário: Encefalomielite Autoimune Experimental/metabolismo
Leucócitos/imunologia
Lisina Carboxipeptidase/metabolismo
Meninges/patologia
Esclerose Múltipla/metabolismo
[Mh] Termos MeSH secundário: Animais
Movimento Celular/genética
Doenças Desmielinizantes/genética
Modelos Animais de Doenças
Progressão da Doença
Encefalomielite Autoimune Experimental/genética
Seres Humanos
Inflamação/genética
Lisina Carboxipeptidase/genética
Camundongos Endogâmicos C57BL
Esclerose Múltipla/genética
Fenótipo
Medula Espinal/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
EC 3.4.17.3 (Lysine Carboxypeptidase)
[Em] Mês de entrada:1409
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130914
[St] Status:MEDLINE


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[PMID]:23000409
[Au] Autor:Talens S; Lebbink JH; Malfliet JJ; Demmers JA; Uitte de Willige S; Leebeek FW; Rijken DC
[Ad] Endereço:Department of Hematology, Erasmus Medical Center, Rotterdam, The Netherlands.
[Ti] Título:Binding of carboxypeptidase N to fibrinogen and fibrin.
[So] Source:Biochem Biophys Res Commun;427(2):421-5, 2012 Oct 19.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The ultimate step in the blood coagulation cascade is the formation of fibrin. Several proteins are known to bind to fibrin and may thereby change clot properties or clot function. Our previous studies identified carboxypeptidase N (CPN) as a novel plasma clot component. CPN cleaves C-terminal lysine and arginine residues from several proteins. The activity of CPN is increased upon its proteolysis by several proteases. The aim of this study is to investigate the presence of CPN in a plasma clot in more detail. Plasma clots were formed by adding thrombin, CaCl(2) and aprotinin to citrated plasma. Unbound proteins were washed away and non-covalently bound proteins were extracted and analyzed with 2D gel electrophoresis and mass spectrometry. The identification of CPN as a fibrin clot-bound protein was verified using Western blotting. Clot-bound CPN consisted of the same molecular forms as CPN in plasma and its content was approximately 30 ng/ml plasma clot. Using surface plasmon resonance we showed that CPN can bind to fibrinogen as well as to fibrin. In conclusion, CPN binds to fibrinogen and is present in a fibrin clot prepared from plasma. Because CPN binds to a fibrin clot, there could be a possible role for CPN as a fibrinolysis inhibitor.
[Mh] Termos MeSH primário: Coagulação Sanguínea
Fibrina/química
Fibrinogênio/química
Lisina Carboxipeptidase/química
[Mh] Termos MeSH secundário: Fibrinólise
Seres Humanos
Ligação Proteica
Ressonância de Plasmônio de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
9001-31-4 (Fibrin); 9001-32-5 (Fibrinogen); EC 3.4.17.3 (Lysine Carboxypeptidase)
[Em] Mês de entrada:1303
[Cu] Atualização por classe:121023
[Lr] Data última revisão:
121023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120925
[St] Status:MEDLINE


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[PMID]:22708514
[Au] Autor:Darley MM; Ramos TN; Wetsel RA; Barnum SR
[Ad] Endereço:Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
[Ti] Título:Deletion of carboxypeptidase N delays onset of experimental cerebral malaria.
[So] Source:Parasite Immunol;34(8-9):444-7, 2012 Aug-Sep.
[Is] ISSN:1365-3024
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Complement contributes to inflammation during pathogen infections; however, less is known regarding its role during malaria and in the severest form of the disease, cerebral malaria. Recent studies have shown that deletion of the complement anaphylatoxins receptors, C3aR and C5aR, does not alter disease susceptibility in experimental cerebral malaria (ECM). This does not, however, preclude C3a- and C5a-mediated contributions to inflammation in ECM and raises the possibility that carboxypeptidase regulation of anaphylatoxin activity rapidly over rides their functions. To address this question, we performed ECM using carboxypeptidase N-deficient (CPN(-/-)) mice. Unexpectedly, we found that CPN(-/-) mice survived longer than wild-type mice, but they were fully susceptible to ECM. CD4(+) and CD8(+) T cell infiltration was not reduced at the peak of disease in CPN(-/-) mice, and there was no corresponding reduction in pro-inflammatory cytokine production. Our results indicate that carboxypeptidases contribute to the pathogenesis of ECM and that studies examining the contribution of other carboxypeptidase families and family members may provide greater insight into the role these enzymes play in malaria.
[Mh] Termos MeSH primário: Lisina Carboxipeptidase/deficiência
Lisina Carboxipeptidase/metabolismo
Malária Cerebral/patologia
Malária Cerebral/parasitologia
[Mh] Termos MeSH secundário: Animais
Encéfalo/imunologia
Encéfalo/patologia
Linfócitos T CD4-Positivos/imunologia
Linfócitos T CD8-Positivos/imunologia
Citocinas/secreção
Camundongos
Camundongos Knockout
Análise de Sobrevida
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Cytokines); EC 3.4.17.3 (Lysine Carboxypeptidase)
[Em] Mês de entrada:1301
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120620
[St] Status:MEDLINE
[do] DOI:10.1111/j.1365-3024.2012.01376.x


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[PMID]:19732738
[Au] Autor:Heylen E; Van Goethem S; Willemse J; Olsson T; Augustyns K; Hendriks D
[Ad] Endereço:Laboratory of Medical Biochemistry, University of Antwerp, B-2610 Wilrijk, Belgium.
[Ti] Título:Development of a sensitive and selective assay for the determination of procarboxypeptidase U (thrombin-activatable fibrinolysis inhibitor) in plasma.
[So] Source:Anal Biochem;396(1):152-4, 2010 Jan 01.
[Is] ISSN:1096-0309
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:To date, several assays for procarboxypeptidase U (proCPU) determination exist, all having their own inherent disadvantages and advantages. A drawback of activity-based assays is the interference of the constitutively active carboxypeptidase N (CPN) in plasma. Recent screening of Bz-Xaa-Arg peptides with modified aromatic amino acids at the P1 position revealed a selective CPU substrate, N-benzoyl-ortho-cyano-phenylalanyl-arginine (Bz-o-cyano-Phe-Arg), which will allow straightforward determination of proCPU in plasma. Our assay shows an excellent linearity in the concentration range of 20-2600 U/L, with within- and between-run precision values of 2.7% and 4.6%, respectively. A good correlation with our high-performance liquid chromatography (HPLC)-assisted proCPU activity assay using hippuryl-l-arginine (HipArg) as substrate was found. Besides the major improvement regarding the selectivity, the assay is much easier to perform and far less time-consuming compared with the proCPU activity assay using HipArg as substrate.
[Mh] Termos MeSH primário: Carboxipeptidase B2/sangue
Ensaios Enzimáticos/métodos
[Mh] Termos MeSH secundário: Calibragem
Cromatografia Líquida de Alta Pressão
Seres Humanos
Lisina Carboxipeptidase/sangue
Padrões de Referência
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.4.17.20 (Carboxypeptidase B2); EC 3.4.17.3 (Lysine Carboxypeptidase)
[Em] Mês de entrada:1001
[Cu] Atualização por classe:141120
[Lr] Data última revisão:
141120
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090908
[St] Status:MEDLINE
[do] DOI:10.1016/j.ab.2009.08.037



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