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Pesquisa : D08.811.277.656.350.350.126 [Categoria DeCS]
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Texto completo SciELO Brasil
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Id: biblio-837655
Autor: Tang, Zheng; Wang, Zhiwei; Hu, Zhipeng; Zhang, Min; Li, Luocheng; Li, Bowen.
Título: The role of bradykinin in lung ischemia-reperfusion injury in a rat lung transplantation model
Fonte: Acta cir. bras;31(12):807-812, Dec. 2016. graf.
Idioma: en.
Resumo: ABSTRACT PURPOSE: To investigate the role of bradykinin in a rat lung transplantation (LTx) model and preliminarily discuss the relationship between bradykinin and CD26/DPP-4. METHODS: Rats were randomly divided into four groups: Control (CON), Sham, low potassium dextranglucose (LPD), and AB192 (n=15/group). Orthotopic single LTx was performed in the LPD and AB192 groups. The donor lungs were flush-perfused and preserved with low potassium dextranglucose (LPD) or LPD+CD26/DPP-4 catalytic inhibitor (AB192). LTx was performed after 18 h cold ischemia time and harvested two days post-LTx. Blood gas analysis (PO2), wet/dry weight ratio (W/D), myeloperoxidase activity (MPO), and lipid peroxidation (MDA) were analyzed at 48 hr after transplantation. Immunohistochemical (IHC) analysis was performed in the same sample and validated by Western-Blot. RESULTS: Compared to the LPD group, the AB192 group showed higher PO2, lower W/D ratio, and decreased MPO and MDA. IHC studies showed strong bradykinin β2 receptor (B2R) staining in the LPD group, especially in inflammatory cells, alveolar macrophages, and respiratory epithelial cells. Expression of B2R by Western-Blot was significantly different between the AB192 and LPD groups. CONCLUSION: Bradykinin may be a competitive substrate of DPP-4, and decreased bradykinin levels may enhance protective effects against ischemia/reperfusion injury during LTx.
Descritores: Bradicinina/fisiologia
Traumatismo por Reperfusão/patologia
Transplante de Pulmão
Dipeptidil Peptidase 4/fisiologia
Disfunção Primária do Enxerto/patologia
Pulmão/irrigação sanguínea
-Imuno-Histoquímica
Peroxidação de Lipídeos
Traumatismo por Reperfusão/fisiopatologia
Traumatismo por Reperfusão/metabolismo
Distribuição Aleatória
Western Blotting
Modelos Animais de Doenças
Disfunção Primária do Enxerto/fisiopatologia
Antagonistas de Receptor B2 da Bradicinina/metabolismo
Pulmão/efeitos dos fármacos
Limites: Animais
Masculino
Ratos
Responsável: BR1.1 - BIREME


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Id: lil-641977
Autor: Bayón, Claudia; Barriga, Mercedes Araceli; Litwak, León.
Título: Incretinas, incretinomiméticos, inhibidores de DPP IV: (2ª parte) / Incretins, Incretinmimetics, Inhibitors (2nd part)
Fonte: Rev. argent. endocrinol. metab;47(3):39-54, jul.-set. 2010. ilus, tab.
Idioma: es.
Resumo: En los últimos años se reconoce un nuevo mecanismo involucrado en la fisiopatología de la Diabetes Mellitus tipo 2: el déficit de producción y/o acción de las incretinas. Las incretinas son enterohormonas que estimulan la secreción de insulina en respuesta a la ingesta de nutrientes. Glucagon like peptide-1 (GLP1) y Polipéptido insulinotrópico glucosa dependiente (GIP) son las principales incretinas descubiertas hasta hoy. Ambas presentan también efecto trófico sobre las células beta de los islotes pancreáticos. GLP-1 presenta otras acciones como son la inhibición de la secreción de glucagón, enlentecimiento del vaciamiento gástrico e inhibición del apetito. Ambas incretinas son rápidamente clivadas por la enzima dipeptidil peptidasa 4 (DPP-4). Nuevas drogas como los incretinomiméticos, análogos y los inhibidores de DPP-4 se presentan como una terapéutica prometedora para los pacientes con diabetes tipo 2. Conflicto de intereses: Dr. León Litwak - Miembro del Board Latinoamericano de Eli Lilly y Sanofi Aventis - Miembro del Board Nacional de los laboratorios Novo Nordisk, Novartis, GlaxoSmithKline, Sanofi Aventis, Boheringer Ingelheim, Bristol Myers, Astra Zeneca - Investigador principal de protocolos pertenecientes a Eli Lilly, Novo Nordisk, Novartis, GlaxoSmithKline, Takeda, PPDF, Pfizer, Merck Sharp and Dôhme, Amger, Roche, Minimed, Quintiles - Conferencista de los laboratorios mencionados.

Two main pathophysiological mechanisms are currently involved in Type 2 Diabetes (T2DM), insulin resistance and impairment of beta cell function. However, in recent years a new mechanism was reported: a significant decrease in incretins production and/or action. Incretins are gastrointestinal hormones whose main action is stimulating insulin secretion in response to nutrients. The best known incretins are glucagon like peptide-1 (GLP-1) and Gastric insulinotropic peptide (GIP). GLP-1 and GIP not only increase insulin secretion, but also decrease glucagon secretion, slow gastric emptying and reduce apetite, generating weight loss. Both incretins are rapidly clived by the enzyme dipeptidil peptidase 4 (DPP4). In order to emulate incretins action, several drugs were developed: GLP-1 receptor agonists, GLP-1 mimetics, and DPP4 inhibitors. All of them seem to became a very promising tool for the treatment of T2DM. Financial Interests: Dr. León Litwak - Member of the Latin American Board of Eli Lilly and Sanofi Aventis - Member of the National Board of the following laboratories: Novo Nordisk, Novartis, GlaxoSmithKlein Sanofi, Aventis, Boheringer Ingelheim, Bristol Myers, Astra Zeneca - Principal Investigator of Protocols from: Eli Lilly, Novo Nordisk, Novartis, GlaxoSmithKlein, Takeda, PPDF, Pfizer, Merck Sharp and Dôhme, Amgen, Roche, Minimed, Quintiles - Lecturer for the former laboratories.
Descritores: Dipeptidil Peptidase 4/metabolismo
Diabetes Mellitus Tipo 2/terapia
Incretinas/uso terapêutico
-Peptídeo 1 Semelhante ao Glucagon/agonistas
Incretinas/metabolismo
Limites: Humanos
Masculino
Feminino
Tipo de Publ: Revisão
Responsável: AR635.1 - FCVyS - Servicio de Información y Documentación


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Borojevic, R
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Id: lil-331454
Autor: Pereira, D. A; Gomes, L; El-Cheikh, M. C; Borojevic, R.
Título: Dipeptidyl peptidase IV (CD26) activity in the hematopoietic system: differences between the membrane-anchored and the released enzyme activity
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;36(5):567-578, May 2003. ilus, tab, graf.
Idioma: en.
Resumo: Dipeptidyl peptidase IV (DPP-IV; CD26) (EC 3.4.14.5) is a membrane-anchored ectoenzyme with N-terminal exopeptidase activity that preferentially cleaves X-Pro-dipeptides. It can also be spontaneously released to act in the extracellular environment or associated with the extracellular matrix. Many hematopoietic cytokines and chemokines contain DPP-IV-susceptible N-terminal sequences. We monitored DPP-IV expression and activity in murine bone marrow and liver stroma cells which sustain hematopoiesis, myeloid precursors, skin fibroblasts, and myoblasts. RT-PCR analysis showed that all these cells produced mRNA for DPP-IV. Partially purified protein reacted with a commercial antibody to CD26. The K M values for Gly-Pro-p-nitroanilide ranged from 0.43 to 0.98 mM for the membrane-associated enzyme of connective tissue stromas, and from 6.76 to 8.86 mM for the enzyme released from the membrane, corresponding to a ten-fold difference, but only a two-fold difference in K M was found in myoblasts. K M of the released soluble enzyme decreased in the presence of glycosaminoglycans, nonsulfated polysaccharide polymers (0.8-10 æg/ml) or simple sugars (320-350 æg/ml). Purified membrane lipid rafts contained nearly 3/4 of the total cell enzyme activity, whose K M was three-fold decreased as compared to the total cell membrane pool, indicating that, in the hematopoietic environment, DPP-IV activity is essentially located in the lipid rafts. This is compatible with membrane-associated events and direct cell-cell interactions, whilst the long-range activity depending upon soluble enzyme is less probable in view of the low affinity of this form
Descritores: Células da Medula Óssea
Dipeptidil Peptidase 4
Células Estromais
-Linhagem Celular
Dipeptidil Peptidase 4
Expressão Gênica
Sistema Hematopoético
Immunoblotting
Fígado
Reação em Cadeia da Polimerase Via Transcriptase Reversa
RNA Mensageiro
Limites: Animais
Camundongos
Ratos
Responsável: BR1.1 - BIREME



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