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  1 / 1822 MEDLINE  
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[PMID]:28744580
[Au] Autor:Wester A; Devocelle M; Tallant EA; Chappell MC; Gallagher PE; Paradisi F
[Ad] Endereço:School of Chemistry, University College Dublin, Dublin, Ireland.
[Ti] Título:Stabilization of Angiotensin-(1-7) by key substitution with a cyclic non-natural amino acid.
[So] Source:Amino Acids;49(10):1733-1742, 2017 10.
[Is] ISSN:1438-2199
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:Angiotensin-(1-7) [Ang-(1-7)], a heptapeptide hormone of the renin-angiotensin-aldosterone system, is a promising candidate as a treatment for cancer that reflects its anti-proliferative and anti-angiogenic properties. However, the peptide's therapeutic potential is limited by the short half-life and low bioavailability resulting from rapid enzymatic metabolism by peptidases including angiotensin-converting enzyme (ACE) and dipeptidyl peptidase 3 (DPP 3). We report the facile assembly of three novel Ang-(1-7) analogues by solid-phase peptide synthesis which incorporates the cyclic non-natural δ-amino acid ACCA. The analogues containing the ACCA substitution at the site of ACE cleavage exhibit complete resistance to human ACE, while substitution at the DDP 3 cleavage site provided stability against DPP 3 hydrolysis. Furthermore, the analogues retain the anti-proliferative properties of Ang-(1-7) against the 4T1 and HT-1080 cancer cell lines. These results suggest that ACCA-substituted Ang-(1-7) analogues which show resistance against proteolytic degradation by peptidases known to hydrolyze the native heptapeptide may be novel therapeutics in the treatment of cancer.
[Mh] Termos MeSH primário: Substituição de Aminoácidos
Angiotensina I
Dipeptidil Peptidases e Tripeptidil Peptidases/química
Fragmentos de Peptídeos
Peptidil Dipeptidase A/química
Proteólise
[Mh] Termos MeSH secundário: Angiotensina I/síntese química
Angiotensina I/química
Seres Humanos
Fragmentos de Peptídeos/síntese química
Fragmentos de Peptídeos/química
Estabilidade Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Peptide Fragments); 9041-90-1 (Angiotensin I); EC 3.4.14.- (Dipeptidyl-Peptidases and Tripeptidyl-Peptidases); EC 3.4.14.4 (DPP3 protein, human); EC 3.4.15.1 (Peptidyl-Dipeptidase A); IJ3FUK8MOF (angiotensin I (1-7))
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1007/s00726-017-2471-9


  2 / 1822 MEDLINE  
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[PMID]:29304092
[Au] Autor:Diaz JR; Ramírez CA; Nocua PA; Guzman F; Requena JM; Puerta CJ
[Ad] Endereço:Laboratorio de Parasitología Molecular, Departamento de Microbiología, Facultad de Ciencias, Pontificia Universidad Javeriana, Bogotá, Colombia.
[Ti] Título:Dipeptidyl peptidase 3, a novel protease from Leishmania braziliensis.
[So] Source:PLoS One;13(1):e0190618, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The increase of leishmaniasis cases worldwide and the emergence of Leishmania strains resistant to current treatments make necessary to find new therapeutic targets. Proteases are appealing drug targets because they play pivotal roles in facilitating parasite survival and promoting pathogenesis. Enzymes belonging to the dipeptidyl peptidase 3 (DPP3) group have been described in different organisms such as mammals, insects and yeast, in which these enzymes have been involved in both protein turnover and protection against oxidative damage. The aim of this work was to characterize the structure and function of the Leishmania braziliensis DPP3 (LbDPP3) protein as the first step to elucidate its suitability as a potential drug target. Sequence alignment showed 43% of identity between LbDPP3 and its human orthologous (hDPP3) enzyme. Although the modeled protein adopted a globally conserved three-dimensional (3D) structure, structural differences were found in the vicinity of the active site and the substrate binding-cleft. In addition, the Leishmania protein was expressed as a soluble recombinant protein and its kinetics parameters were determined using the z-Arginine-Arginine-AMC substrate. The LbDPP3 activity was maximal at pH values between 8.0-8.5. Interestingly, classical enzyme inhibitors such as the tynorphin and its derivative peptide IVYPW were found to actively inhibit the LbDPP3 activity. Moreover, these DPP3 inhibitors showed a detrimental effect upon parasite survival, decreasing the viability of promastigotes by up to 29%. Finally, it was observed that LbDPP3 was equally expressed along the in vitro differentiation from promastigotes to axenic amastigotes. In conclusion, these findings suggest that the L. brazileinsis DPP3 could be a promising drug target.
[Mh] Termos MeSH primário: Dipeptidil Peptidases e Tripeptidil Peptidases/metabolismo
Leishmania braziliensis/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Clonagem Molecular
Dipeptidil Peptidases e Tripeptidil Peptidases/química
Dipeptidil Peptidases e Tripeptidil Peptidases/genética
Seres Humanos
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.4.14.- (Dipeptidyl-Peptidases and Tripeptidyl-Peptidases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180106
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190618


  3 / 1822 MEDLINE  
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[PMID]:29190734
[Au] Autor:Hromic-Jahjefendic A; Jajcanin Jozic N; Kazazic S; Grabar Branilovic M; Karacic Z; Schrittwieser JH; Das KMP; Tomin M; Oberer M; Gruber K; Abramic M; Tomic S
[Ad] Endereço:Institute of Molecular Biosciences, University of Graz, Graz, Austria.
[Ti] Título:A novel Porphyromonas gingivalis enzyme: An atypical dipeptidyl peptidase III with an ARM repeat domain.
[So] Source:PLoS One;12(11):e0188915, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Porphyromonas gingivalis, an asaccharolytic Gram-negative oral anaerobe, is a major pathogen associated with adult periodontitis, a chronic infective disease that a significant percentage of the human population suffers from. It preferentially utilizes dipeptides as its carbon source, suggesting the importance of dipeptidyl peptidase (DPP) types of enzyme for its growth. Until now DPP IV, DPP5, 7 and 11 have been extensively investigated. Here, we report the characterization of DPP III using molecular biology, biochemical, biophysical and computational chemistry methods. In addition to the expected evolutionarily conserved regions of all DPP III family members, PgDPP III possesses a C-terminal extension containing an Armadillo (ARM) type fold similar to the AlkD family of bacterial DNA glycosylases, implicating it in alkylation repair functions. However, complementation assays in a DNA repair-deficient Escherichia coli strain indicated the absence of alkylation repair function for PgDPP III. Biochemical analyses of recombinant PgDPP III revealed activity similar to that of DPP III from Bacteroides thetaiotaomicron, and in the range between activities of human and yeast counterparts. However, the catalytic efficiency of the separately expressed DPP III domain is ~1000-fold weaker. The structure and dynamics of the ligand-free enzyme and its complex with two different diarginyl arylamide substrates was investigated using small angle X-ray scattering, homology modeling, MD simulations and hydrogen/deuterium exchange (HDX). The correlation between the experimental HDX and MD data improved with simulation time, suggesting that the DPP III domain adopts a semi-closed or closed form in solution, similar to that reported for human DPP III. The obtained results reveal an atypical DPP III with increased structural complexity: its superhelical C-terminal domain contributes to peptidase activity and influences DPP III interdomain dynamics. Overall, this research reveals multifunctionality of PgDPP III and opens direction for future research of DPP III family proteins.
[Mh] Termos MeSH primário: Dipeptidil Peptidases e Tripeptidil Peptidases/metabolismo
Porphyromonas gingivalis/enzimologia
[Mh] Termos MeSH secundário: Calorimetria
Dicroísmo Circular
Dipeptidil Peptidases e Tripeptidil Peptidases/química
Dipeptidil Peptidases e Tripeptidil Peptidases/genética
Eletroforese em Gel de Poliacrilamida
Cinética
Simulação de Dinâmica Molecular
Conformação Proteica
Proteólise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.4.14.- (Dipeptidyl-Peptidases and Tripeptidyl-Peptidases); EC 3.4.14.4 (dipeptidyl peptidase III)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180101
[Lr] Data última revisão:
180101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188915


  4 / 1822 MEDLINE  
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[PMID]:29049217
[Au] Autor:Hu B; Shi C; Jiang HX; Qin SY
[Ad] Endereço:Department of Gastroenterology, the First Affiliated Hospital of Guangxi Medical University, Nanning, China.
[Ti] Título:Identification of novel therapeutic target genes and pathway in pancreatic cancer by integrative analysis.
[So] Source:Medicine (Baltimore);96(42):e8261, 2017 Oct.
[Is] ISSN:1536-5964
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Gene alterations are crucial to the molecular pathogenesis of pancreatic cancer. The present study was designed to identify the potential candidate genes in the pancreatic carcinogenesis. METHODS: Gene Expression Omnibus database (GEO) datasets of pancreatic cancer tissue were retrieval and the differentially expressed genes (DEGs) from individual microarray data were merged. Gene Ontology (GO) enrichment analysis, Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analysis, protein-protein interaction (PPI) networks, and gene coexpression analysis were performed. RESULTS: Three GEO datasets, including 74 pancreatic cancer samples and 55 controls samples were selected. A total of 2325 DEGs were identified, including 1383 upregulated and 942 downregulated genes. The GO terms for molecular functions, biological processes, and cellular component were protein binding, small molecule metabolic process, and integral to membrane, respectively. The most significant pathway in KEGG analysis was metabolic pathways. PPI network analysis indicated that the significant hub genes including cytochrome P450, family 2, subfamily E, polypeptide 1 (CYP2E1), mitogen-activated protein kinase 3 (MAPK3), and phospholipase C, gamma 1 (PLCG1). Gene coexpression network analysis identified 4 major modules, and the potassium channel tetramerization domain containing 10 (KCTD10), kin of IRRE like (KIRREL), dipeptidyl-peptidase 10 (DPP10), and unc-80 homolog (UNC80) were the hub gene of each modules, respectively. CONCLUSION: Our integrative analysis provides a comprehensive view of gene expression patterns associated with the pancreatic carcinogenesis.
[Mh] Termos MeSH primário: Carcinogênese/genética
Regulação Neoplásica da Expressão Gênica/genética
Neoplasias Pancreáticas/genética
[Mh] Termos MeSH secundário: Proteínas de Transporte/genética
Estudos de Casos e Controles
Citocromo P-450 CYP2E1/genética
Bases de Dados Genéticas
Dipeptidil Peptidases e Tripeptidil Peptidases/genética
Perfilação da Expressão Gênica/métodos
Ontologia Genética
Seres Humanos
Proteínas de Membrana/genética
Proteína Quinase 3 Ativada por Mitógeno/genética
Fosfolipase C gama/genética
Canais de Potássio de Abertura Dependente da Tensão da Membrana/genética
Mapas de Interação de Proteínas
Transdução de Sinais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (KCTD10 protein, human); 0 (KIRREL protein, human); 0 (Membrane Proteins); 0 (Potassium Channels, Voltage-Gated); 0 (Unc80 protein, human); EC 1.14.13.- (Cytochrome P-450 CYP2E1); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 3); EC 3.1.4.11 (PLCG1 protein, human); EC 3.1.4.3 (Phospholipase C gamma); EC 3.4.14.- (DPP10 protein, human); EC 3.4.14.- (Dipeptidyl-Peptidases and Tripeptidyl-Peptidases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171122
[Lr] Data última revisão:
171122
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:171020
[St] Status:MEDLINE
[do] DOI:10.1097/MD.0000000000008261


  5 / 1822 MEDLINE  
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[PMID]:28887018
[Au] Autor:Kim M; Minoux M; Piaia A; Kueng B; Gapp B; Weber D; Haller C; Barbieri S; Namoto K; Lorenz T; Wirsching J; Bassilana F; Dietrich W; Rijli FM; Ksiazek I
[Ad] Endereço:Novartis Institute for Biomedical Research, CH-4056 Basel, Switzerland.
[Ti] Título:DPP9 enzyme activity controls survival of mouse migratory tongue muscle progenitors and its absence leads to neonatal lethality due to suckling defect.
[So] Source:Dev Biol;431(2):297-308, 2017 11 15.
[Is] ISSN:1095-564X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dipeptidyl peptidase 9 (DPP9) is an intracellular N-terminal post-proline-cleaving enzyme whose physiological function remains largely unknown. We investigated the role of DPP9 enzyme in vivo by characterizing knock-in mice expressing a catalytically inactive mutant form of DPP9 (S729A; DPP9 mice). We show that DPP9 mice die within 12-18h after birth. The neonatal lethality can be rescued by manual feeding, indicating that a suckling defect is the primary cause of neonatal lethality. The suckling defect results from microglossia, and is characterized by abnormal formation of intrinsic muscles at the distal tongue. In DPP9 mice, the number of occipital somite-derived migratory muscle progenitors, forming distal tongue intrinsic muscles, is reduced due to increased apoptosis. In contrast, intrinsic muscles of the proximal tongue and extrinsic tongue muscles, which derive from head mesoderm, develop normally in DPP9 mice. Thus, lack of DPP9 activity in mice leads to impaired tongue development, suckling defect and subsequent neonatal lethality due to impaired survival of a specific subset of migratory tongue muscle progenitors.
[Mh] Termos MeSH primário: Dipeptidil Peptidases e Tripeptidil Peptidases/metabolismo
Músculo Esquelético/citologia
Células-Tronco/citologia
Células-Tronco/enzimologia
Língua/citologia
[Mh] Termos MeSH secundário: Alanina/genética
Animais
Animais Recém-Nascidos
Animais Lactentes
Domínio Catalítico
Contagem de Células
Sobrevivência Celular
Camundongos
Camundongos Transgênicos
Desenvolvimento Muscular
Proteínas Musculares/metabolismo
Mutação Puntual/genética
Receptores CXCR4/metabolismo
Serina/genética
Doenças da Língua/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CXCR4 protein, mouse); 0 (Lbx1h protein, mouse); 0 (Muscle Proteins); 0 (Receptors, CXCR4); 452VLY9402 (Serine); EC 3.4.14.- (Dipeptidyl-Peptidases and Tripeptidyl-Peptidases); EC 3.4.14.5 (dipeptidyl peptidase 9, mouse); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170910
[St] Status:MEDLINE


  6 / 1822 MEDLINE  
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[PMID]:28711492
[Au] Autor:Krepela E; Busek P; Hilser M; Vanickova Z; Sedo A
[Ad] Endereço:Laboratory of Cancer Cell Biology, Institute of Biochemistry and Experimental Oncology, First Faculty of Medicine, Charles University, Prague, Czech Republic. Electronic address: evzen.krepela@fl1.cuni.cz.
[Ti] Título:Species-specific real-time RT-PCR analysis of expression of stromal cell genes in a tumor xenotransplantation model in mice.
[So] Source:Biochem Biophys Res Commun;491(1):126-133, 2017 Sep 09.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human tumor xenografts in mice together with the species-specific analysis of expressed genes allow to study the molecular processes driving tumor growth and progression in vivo and help to develop and evaluate anticancer therapies. In the present work, we designed and validated species-specific real-time RT-PCR assays for discrimination and quantitation of expression of human and mouse transcripts in cancer and stromal cells including dipeptidyl peptidase (DPP) 4, DPP8, DPP9, fibroblast activation protein (FAP) and CXC chemokine receptor 4 in mixed human-mouse biological samples. Using single species RNA samples and mixed human-mouse RNA samples, we formulated and characterized two-step real-time RT-PCR assays to quantitate expression of the indicated transcripts and described analytical performance of the assays. We also demonstrated the applicability of these assays for species-specific quantitation of transcriptional expression of mouse stromal cell genes including Dpp4, Dpp8, Dpp9, Fap and Cxcr4 in mixed human-mouse RNA samples from human glioma cell-derived tumor xenografts growing in mouse brain.
[Mh] Termos MeSH primário: Neoplasias Encefálicas/metabolismo
Encéfalo/metabolismo
Dipeptidil Peptidases e Tripeptidil Peptidases/metabolismo
Regulação Neoplásica da Expressão Gênica
Glioma/metabolismo
Receptores CXCR4/metabolismo
Células Estromais/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Perfilação da Expressão Gênica
Seres Humanos
Camundongos
Proteoma/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Especificidade da Espécie
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proteome); 0 (Receptors, CXCR4); EC 3.4.14.- (Dipeptidyl-Peptidases and Tripeptidyl-Peptidases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170822
[Lr] Data última revisão:
170822
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170717
[St] Status:MEDLINE


  7 / 1822 MEDLINE  
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[PMID]:28589525
[Au] Autor:Markham A
[Ad] Endereço:Springer, Private Bag 65901, Mairangi Bay, 0754, Auckland, New Zealand. dru@adis.com.
[Ti] Título:Cerliponase Alfa: First Global Approval.
[So] Source:Drugs;77(11):1247-1249, 2017 Jul.
[Is] ISSN:1179-1950
[Cp] País de publicação:New Zealand
[La] Idioma:eng
[Ab] Resumo:Cerliponase alfa (Brineura™) is a recombinant human tripeptidyl peptidase-1 (TPP1) being developed by BioMarin Pharmaceutical Inc. for use in patients with neuronal ceroid lipofuscinosis type 2 (CLN2), a paediatric neurodegenerative disease caused by a deficiency in TPP1. CLN2 is characterised by progressive impairment of motor function, language deficiencies, seizures, ataxia, blindness and early death, and intracerebroventricular infusion of cerliponase alfa has been shown to reduce the progression of functional decline. This article summarizes the milestones in the development of cerliponase alfa leading to its first global approval in the USA for the treatment of motor function loss in paediatric patients ≥3 years of age with CLN2, and subsequent approval in the EU for CLN2 in all ages.
[Mh] Termos MeSH primário: Dipeptidil Peptidases e Tripeptidil Peptidases/uso terapêutico
Lipofuscinoses Ceroides Neuronais/tratamento farmacológico
Proteínas Recombinantes/uso terapêutico
[Mh] Termos MeSH secundário: Criança
Pré-Escolar
Dipeptidil Peptidases e Tripeptidil Peptidases/administração & dosagem
Dipeptidil Peptidases e Tripeptidil Peptidases/efeitos adversos
Dipeptidil Peptidases e Tripeptidil Peptidases/farmacocinética
Progressão da Doença
Aprovação de Drogas
Terapia de Reposição de Enzimas
Europa (Continente)
Feminino
Seres Humanos
Masculino
Proteínas Recombinantes/administração & dosagem
Proteínas Recombinantes/efeitos adversos
Proteínas Recombinantes/farmacocinética
Estados Unidos
United States Food and Drug Administration
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Recombinant Proteins); EC 3.4.14.- (Dipeptidyl-Peptidases and Tripeptidyl-Peptidases); EC 3.4.14.- (cerliponase alfa)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170608
[St] Status:MEDLINE
[do] DOI:10.1007/s40265-017-0771-8


  8 / 1822 MEDLINE  
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[PMID]:28448177
[Au] Autor:Stoimenis D; Karagiannis T; Katsoula A; Athanasiadou E; Kazakos K; Bekiari E; Matthews DR; Tsapas A
[Ad] Endereço:a Clinical Research and Evidence Based Medicine Unit, Second Medical Department , Aristotle University Thessaloniki , Thessaloniki , Greece.
[Ti] Título:Once-weekly dipeptidyl peptidase-4 inhibitors for type 2 diabetes: a systematic review and meta-analysis.
[So] Source:Expert Opin Pharmacother;18(9):843-851, 2017 Jun.
[Is] ISSN:1744-7666
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To assess the efficacy and safety of omarigliptin and trelagliptin, novel dipeptidyl peptidase-4 inhibitors administered once-weekly (DPP-4i QW). METHODS: We systematically searched for placebo- and active-controlled randomized trials in adults with type 2 diabetes mellitus. RESULTS: Fifteen primary studies with 5709 participants were included. DPP-4i QW were more effective than placebo in reducing hemoglobin A (HbA ) (Weighted Mean Difference (WMD) -0.63%; 95% CI -0.80, -0.46; I = 84%) and had a similar glucose-lowering effect with daily DPP-4i (WMD 0.01%; -0.08, 0.11%; I = 34%). Omarigliptin was less effective compared with oral antidiabetic agents, other than daily DPP-4i, (WMD 0.24%; 0.10, 0.38; I = 12%). Omarigliptin did not affect body weight (WMD versus placebo 0.60 kg; 0.25, 0.96; I = 0%). Risk for any hypoglycemia was similar between DPP-4i QW and placebo (Odds Ratio 1.32; 0.78, 2.22; I = 0%). Incidence of other adverse events did not differ between DPP-4i QW and control. CONCLUSIONS: DPP-4i QW were superior to placebo and similar to daily DPP-4i in terms of glycemic control, and were not associated with any specific adverse events. There is limited comparative effectiveness evidence against other agents, while their effect on hard clinical safety outcomes is unknown.
[Mh] Termos MeSH primário: Diabetes Mellitus Tipo 2/tratamento farmacológico
Inibidores da Dipeptidil Peptidase IV/uso terapêutico
Hipoglicemiantes/uso terapêutico
[Mh] Termos MeSH secundário: Glicemia/efeitos dos fármacos
Peso Corporal/efeitos dos fármacos
Diabetes Mellitus Tipo 2/metabolismo
Inibidores da Dipeptidil Peptidase IV/administração & dosagem
Inibidores da Dipeptidil Peptidase IV/efeitos adversos
Dipeptidil Peptidases e Tripeptidil Peptidases/metabolismo
Hemoglobina A Glicada/análise
Seres Humanos
Hipoglicemia/induzido quimicamente
Hipoglicemiantes/administração & dosagem
Hipoglicemiantes/efeitos adversos
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE; META-ANALYSIS; REVIEW
[Nm] Nome de substância:
0 (Blood Glucose); 0 (Dipeptidyl-Peptidase IV Inhibitors); 0 (Glycated Hemoglobin A); 0 (Hypoglycemic Agents); EC 3.4.14.- (Dipeptidyl-Peptidases and Tripeptidyl-Peptidases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1080/14656566.2017.1324848


  9 / 1822 MEDLINE  
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[PMID]:28416489
[Au] Autor:Lu K; Alcivar AL; Ma J; Foo TK; Zywea S; Mahdi A; Huo Y; Kensler TW; Gatza ML; Xia B
[Ad] Endereço:Department of Radiation Oncology, Rutgers Cancer Institute of New Jersey and Robert Wood Johnson Medical School, New Brunswick, New Jersey.
[Ti] Título:NRF2 Induction Supporting Breast Cancer Cell Survival Is Enabled by Oxidative Stress-Induced DPP3-KEAP1 Interaction.
[So] Source:Cancer Res;77(11):2881-2892, 2017 Jun 01.
[Is] ISSN:1538-7445
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:NRF2 is a transcription factor serving as a master regulator of the expression of many genes involved in cellular responses to oxidative and other stresses. In the absence of stress, NRF2 is constantly synthesized but maintained at low levels as it is targeted by KEAP1 for ubiquitination and proteasome-mediated degradation. NRF2 binds KEAP1 mainly through a conserved "ETGE" motif that has also been found in several other proteins, such as DPP3, which has been shown to bind KEAP1 and enhance NRF2 function upon overexpression. Here we demonstrate the interaction between endogenous DPP3 and endogenous KEAP1. We further show that the DPP3-KEAP1 interaction is strongly induced by hydrogen peroxide and that DPP3 is required for timely NRF2 induction and nuclear accumulation in the estrogen receptor (ER)-positive MCF7 breast cancer cells. Moreover, we present evidence that the binding of DPP3 to KEAP1 stabilizes the latter. Finally, we show that DPP3 is overexpressed in breast cancer and that elevated levels of mRNA correlate with increased NRF2 downstream gene expression and poor prognosis, particularly for ER-positive breast cancer. Our studies reveal novel insights into the regulation of NRF2 and identify DPP3 and an NRF2 transcriptional signature as potential biomarkers for breast cancer prognosis and treatment. .
[Mh] Termos MeSH primário: Neoplasias da Mama/genética
Dipeptidil Peptidases e Tripeptidil Peptidases/genética
Proteína 1 Associada a ECH Semelhante a Kelch/genética
Fator 2 Relacionado a NF-E2/metabolismo
[Mh] Termos MeSH secundário: Neoplasias da Mama/mortalidade
Sobrevivência Celular
Feminino
Células HeLa
Seres Humanos
Células MCF-7
Estresse Oxidativo
Transdução de Sinais
Análise de Sobrevida
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (KEAP1 protein, human); 0 (Kelch-Like ECH-Associated Protein 1); 0 (NF-E2-Related Factor 2); EC 3.4.14.- (Dipeptidyl-Peptidases and Tripeptidyl-Peptidases); EC 3.4.14.4 (DPP3 protein, human)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170419
[St] Status:MEDLINE
[do] DOI:10.1158/0008-5472.CAN-16-2204


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[PMID]:28356045
[Au] Autor:Sato A; Ogita H
[Ad] Endereço:Division of Molecular Medical Biochemistry, Department of Biochemistry and Molecular Biology, Shiga University of Medical Science, Otsu 520-2192. Japan.
[Ti] Título:Pathophysiological Implications of Dipeptidyl Peptidases.
[So] Source:Curr Protein Pept Sci;18(8):843-849, 2017.
[Is] ISSN:1875-5550
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Dipeptidyl peptidases (DPPs) belong to one of the protease families classified under EC 3.4.14 in the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. DPPs family consists of eight members in the mammalian species. They play a role in oligopeptide N-terminal processing and degradation of bioactive peptides. Over the past 20 years, most of the studies have been focused on DPP 4 that has important roles in metabolism and immunity. A large number of pharmacological inhibitors against DPP 4 have been tested rigorously and some of them are now used in the treatment of type 2 diabetes and obesity. In addition, current researches cast a spotlight on other physiological and pathological functions of DPP family members such as DPP 3 for the purpose of investigating their application as novel therapeutic compounds. In this review, we provide an update about the pathophysiological functions of DPPs, and discuss the future potential of the DPP family as pharmacological and therapeutic agents and targets.
[Mh] Termos MeSH primário: Diabetes Mellitus Tipo 2/enzimologia
Dipeptidil Peptidase 4/genética
Dipeptidil Peptidases e Tripeptidil Peptidases/farmacologia
Hipertensão/enzimologia
Obesidade/enzimologia
[Mh] Termos MeSH secundário: Animais
Diabetes Mellitus Tipo 2/tratamento farmacológico
Diabetes Mellitus Tipo 2/genética
Diabetes Mellitus Tipo 2/patologia
Dipeptidil Peptidase 4/metabolismo
Inibidores da Dipeptidil Peptidase IV/farmacologia
Dipeptidil Peptidases e Tripeptidil Peptidases/genética
Dipeptidil Peptidases e Tripeptidil Peptidases/metabolismo
Regulação da Expressão Gênica
Seres Humanos
Hipertensão/tratamento farmacológico
Hipertensão/genética
Hipertensão/patologia
Hipoglicemiantes/farmacologia
Isoenzimas/antagonistas & inibidores
Isoenzimas/genética
Isoenzimas/metabolismo
Camundongos
Obesidade/tratamento farmacológico
Obesidade/genética
Obesidade/patologia
Proteólise/efeitos dos fármacos
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Dipeptidyl-Peptidase IV Inhibitors); 0 (Hypoglycemic Agents); 0 (Isoenzymes); EC 3.4.14.- (Dipeptidyl-Peptidases and Tripeptidyl-Peptidases); EC 3.4.14.4 (DPP3 protein, human); EC 3.4.14.5 (DPP4 protein, human); EC 3.4.14.5 (Dipeptidyl Peptidase 4)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170331
[St] Status:MEDLINE
[do] DOI:10.2174/1389203718666170329104936



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