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[PMID]:29197590
[Au] Autor:Li X; Wang Y; Guo J; Zhong T; Li L; Zhang H; Wang L
[Ad] Endereço:Institute of Animal Genetics and Breeding, College of Animal Science and Technology, Sichuan Agricultural University, Chengdu, Sichuan, PR China; Farm Animal Genetic Resources Exploration and Innovation Key Laboratory of Sichuan Province, Sichuan Agricultural University, Chengdu, Sichuan, PR China.
[Ti] Título:Identification and expression patterns of adipokine genes during adipocyte differentiation in the Tibetan goat (Capra hircus).
[So] Source:Gene;643:17-25, 2018 Feb 15.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Adipokines are secreted by adipose tissue and play an important role in the regulation of lipid metabolism. However, the information regarding adipokines in goats is limited. PPARγ is a key gene in adipocyte differentiation and activates adipokine genes. Rosiglitazone is a PPARγ agonist and can promote the expression of PPARγ to increase the expression of lipogenesis-related genes. Therefore, investigation of the relationship between rosiglitazone and adipokines will help us to better understand the function of PPARγ in lipid metabolism in Tibetan goats. In this study, we cloned the resistin (RETN), apelin (APLN), fibroblast growth factor 21 (FGF21), and visfatin (NAMPT) genes from non-pregnant female Tibetan goat adipose tissue. APLN and NAMPT were predominantly expressed in the kidney, and FGF21 was expressed at the highest levels in the liver in vivo. In fat tissues, the highest expression levels of FGF21 and RETN were detected in omental fat, whereas their expression in perirenal and subcutaneous fat was extremely weak. APLN and NAMPT were abundantly expressed in omental and subcutaneous fat in vivo. In addition, the four adipokines had different expression profiles during goat adipocyte differentiation in vitro. Oil red O staining showed that rosiglitazone could promote adipocyte differentiation and lipid droplet formation. In addition, rosiglitazone significantly increased the expression of FGF21 and RETN (p<0.05) but decreased the expression of APLN and NAMPT (p<0.05). These results suggest that the four adipocytokine genes may have different roles during goat adipocyte differentiation. And PPARγ could regulate the expression of the four adipokines, but the detailed regulatory mechanism still needs to be elucidated.
[Mh] Termos MeSH primário: Adipocinas/genética
Cabras/genética
[Mh] Termos MeSH secundário: Células 3T3-L1
Adipócitos/metabolismo
Adipogenia/genética
Adipocinas/metabolismo
Tecido Adiposo/metabolismo
Animais
Apelina/genética
Apelina/metabolismo
Diferenciação Celular/genética
Feminino
Fatores de Crescimento de Fibroblastos/genética
Fatores de Crescimento de Fibroblastos/metabolismo
Cabras/metabolismo
Metabolismo dos Lipídeos
Camundongos
Nicotinamida Fosforribosiltransferase/genética
Nicotinamida Fosforribosiltransferase/metabolismo
Obesidade/genética
Resistina/genética
Resistina/metabolismo
Gordura Subcutânea/metabolismo
Tiazolidinedionas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adipokines); 0 (Apelin); 0 (Resistin); 0 (Thiazolidinediones); 0 (fibroblast growth factor 21); 05V02F2KDG (rosiglitazone); 62031-54-3 (Fibroblast Growth Factors); EC 2.4.2.12 (Nicotinamide Phosphoribosyltransferase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180123
[Lr] Data última revisão:
180123
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171204
[St] Status:MEDLINE


  2 / 622 MEDLINE  
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[PMID]:29101069
[Au] Autor:Ghafarian-Alipour F; Ziaee S; Ashoori MR; Zakeri MS; Boroumand MA; Aghamohammadzadeh N; Abbasi-Majdi M; Shool F; Asbaghi NS; Mohammadi A; Zarghami N
[Ad] Endereço:Nutrition Research Center, Tabriz University of Medical Sciences, Tabriz, Iran; Department of Clinical Biochemistry and Laboratory Sciences, Faculty of Medicine, Tabriz University of Medical Sciences, Tabriz, Iran.
[Ti] Título:Association between FTO gene polymorphisms and type 2 diabetes mellitus, serum levels of apelin and androgen hormones among Iranian obese women.
[So] Source:Gene;641:361-366, 2018 Jan 30.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND AND AIMS: Recent studies show that FTO single nucleotide polymorphisms (SNPs) are associated with obesity and type 2 diabetes mellitus (T2DM). On the other hand, many animal models and clinical studies have demonstrated that apelin, an adipocytokine, is related to the obesity and T2DM. Additionally, obese women are at risk of Hyperandrogenemia. So, the aim of this study was to investigate the relationship between FTO variants (rs763967273, rs759031579, rs141115189, rs9926289, rs76804286 and rs9939609) with T2DM, serum apelin and androgenic hormones in Iranian obese women. SUBJECTS AND METHODS: 197 obese women (123 women with T2DM and 74 women as healthy control) were participated in this study. Anthropometrical and biochemical characteristics were measured. Serum apelin and androgen hormones levels were determined in 66 subjects consisting of 33 cases and 33 controls. PCR were carried out and subsequently, the PCR production was genotyped by Sanger sequencing assay. RESULTS: Our observations showed that all SNPs are related to T2DM. The rs9926289 FTO variant had a strong association with serum apelin and dehydroepiandrosterone-sulfate levels (P=0.04 and P=0.03, respectively) among SNPs. In addition, apelin and androgenic hormones were correlated with T2DM. Two polymorphisms including rs9939609 and rs9926289 had a strong Linkage disequilibrium (r =1). CONCLUSION: FTO variants not only were associated with T2DM, but also some variants had a strong association with apelin and androgenic hormones profile.
[Mh] Termos MeSH primário: Dioxigenase FTO Dependente de alfa-Cetoglutarato/genética
Androgênios/sangue
Apelina/sangue
Diabetes Mellitus Tipo 2/sangue
Diabetes Mellitus Tipo 2/genética
Polimorfismo de Nucleotídeo Único/genética
[Mh] Termos MeSH secundário: Estudos de Casos e Controles
Feminino
Estudos de Associação Genética/métodos
Seres Humanos
Irã (Geográfico)
Desequilíbrio de Ligação/genética
Meia-Idade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Androgens); 0 (Apelin); EC 1.14.11.33 (Alpha-Ketoglutarate-Dependent Dioxygenase FTO); EC 1.14.11.33 (FTO protein, human)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171105
[St] Status:MEDLINE


  3 / 622 MEDLINE  
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[PMID]:29053791
[Au] Autor:Harford-Wright E; Andre-Gregoire G; Jacobs KA; Treps L; Le Gonidec S; Leclair HM; Gonzalez-Diest S; Roux Q; Guillonneau F; Loussouarn D; Oliver L; Vallette FM; Foufelle F; Valet P; Davenport AP; Glen RC; Bidere N; Gavard J
[Ad] Endereço:CRCINA, Inserm, Team SOAP, CNRS, Universite de Nantes, Nantes, France.
[Ti] Título:Pharmacological targeting of apelin impairs glioblastoma growth.
[So] Source:Brain;140(11):2939-2954, 2017 Nov 01.
[Is] ISSN:1460-2156
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Glioblastoma are highly aggressive brain tumours that are associated with an extremely poor prognosis. Within these tumours exists a subpopulation of highly plastic self-renewing cancer cells that retain the ability to expand ex vivo as tumourspheres, induce tumour growth in mice, and have been implicated in radio- and chemo-resistance. Although their identity and fate are regulated by external cues emanating from endothelial cells, the nature of such signals remains unknown. Here, we used a mass spectrometry proteomic approach to characterize the factors released by brain endothelial cells. We report the identification of the vasoactive peptide apelin as a central regulator for endothelial-mediated maintenance of glioblastoma patient-derived cells with stem-like properties. Genetic and pharmacological targeting of apelin cognate receptor abrogates apelin- and endothelial-mediated expansion of glioblastoma patient-derived cells with stem-like properties in vitro and suppresses tumour growth in vivo. Functionally, selective competitive antagonists of apelin receptor were shown to be safe and effective in reducing tumour expansion and lengthening the survival of intracranially xenografted mice. Therefore, the apelin/apelin receptor signalling nexus may operate as a paracrine signal that sustains tumour cell expansion and progression, suggesting that apelin is a druggable factor in glioblastoma.
[Mh] Termos MeSH primário: Neoplasias Encefálicas/metabolismo
Glioblastoma/metabolismo
Peptídeos e Proteínas de Sinalização Intercelular/metabolismo
Receptores Acoplados a Proteínas-G/antagonistas & inibidores
[Mh] Termos MeSH secundário: Animais
Apelina
Receptores de Apelina
Neoplasias Encefálicas/tratamento farmacológico
Proliferação Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Células Endoteliais
Glioblastoma/tratamento farmacológico
Células HEK293
Seres Humanos
Técnicas In Vitro
Espectrometria de Massas
Camundongos
Terapia de Alvo Molecular
Proteômica
RNA Interferente Pequeno
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (APLN protein, human); 0 (APLNR protein, human); 0 (Apelin); 0 (Apelin Receptors); 0 (Intercellular Signaling Peptides and Proteins); 0 (RNA, Small Interfering); 0 (Receptors, G-Protein-Coupled)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:171021
[St] Status:MEDLINE
[do] DOI:10.1093/brain/awx253


  4 / 622 MEDLINE  
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[PMID]:28817612
[Au] Autor:O'Carroll AM; Salih S; Griffiths PR; Bijabhai A; Knepper MA; Lolait SJ
[Ad] Endereço:Bristol Medical School, HW-LINE, University of Bristol, Bristol, United Kingdom.
[Ti] Título:Expression and functional implications of the renal apelinergic system in rodents.
[So] Source:PLoS One;12(8):e0183094, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Apelin binds to the G protein-coupled apelin receptor (APJ; gene name aplnr) to modulate diverse physiological systems including cardiovascular function, and hydromineral and metabolic balance. Recently a second endogenous ligand for APJ, named apela, has been discovered. We confirm that apela activates signal transduction pathways (ERK activation) in cells expressing the cloned rat APJ. Previous studies suggest that exogenous apela is diuretic, attributable wholly or in part to an action on renal APJ. Thus far the cellular distribution of apela in the kidney has not been reported. We have utilized in situ hybridization histochemistry to reveal strong apela labelling in the inner medulla (IM), with lower levels observed in the inner stripe of the outer medulla (ISOM), of rat and mouse kidneys. This contrasts with renal aplnr expression where the converse is apparent, with intense labelling in the ISOM (consistent with vasa recta labelling) and low-moderate hybridization in the IM, in addition to labelling of glomeruli. Apelin is found in sparsely distributed cells amongst more prevalent aplnr-labelled cells in extra-tubular regions of the medulla. This expression profile is supported by RNA-Seq data that shows that apela, but not apelin or aplnr, is highly expressed in microdissected rat kidney tubules. If endogenous tubular apela promotes diuresis in the kidney it could conceivably do this by interacting with APJ in vasculature, or via an unknown receptor in the tubules. The comparative distribution of apela, apelin and aplnr in the rodent kidney lays the foundation for future work on how the renal apelinergic system interacts.
[Mh] Termos MeSH primário: Adipocinas/metabolismo
Peptídeos e Proteínas de Sinalização Intercelular/metabolismo
Rim/metabolismo
[Mh] Termos MeSH secundário: Animais
Apelina
Células CHO
Cricetinae
Cricetulus
Rim/fisiologia
Masculino
Camundongos
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adipokines); 0 (Apelin); 0 (Apln protein, mouse); 0 (Apln protein, rat); 0 (Intercellular Signaling Peptides and Proteins)
[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:170818
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183094


  5 / 622 MEDLINE  
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[PMID]:28546009
[Au] Autor:Shin K; Chapman NA; Sarker M; Kenward C; Huang SK; Weatherbee-Martin N; Pandey A; Dupré DJ; Rainey JK
[Ad] Endereço:Department of Biochemistry & Molecular Biology, Dalhousie University, Halifax, Nova Scotia B3H 4R2, Canada.
[Ti] Título:Bioactivity of the putative apelin proprotein expands the repertoire of apelin receptor ligands.
[So] Source:Biochim Biophys Acta;1861(8):1901-1912, 2017 08.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Apelin is a peptide ligand for a class A G-protein coupled receptor called the apelin receptor (AR or APJ) that regulates angiogenesis, the adipoinsular axis, and cardiovascular functions. Apelin has been shown to be bioactive as 13, 17, and 36 amino acid isoforms, C-terminal fragments of the putatively inactive 55-residue proprotein (proapelin or apelin-55). Although intracellular proprotein processing has been proposed, isolation of apelin-55 from colostrum and milk demonstrates potential for secretion prior to processing and the possibility of proapelin-AR interaction. METHODS: Apelin isoform activity and potency were compared by an In-Cell Western™ assay for ERK phosphorylation using a stably AR-transfected HEK293A cell line. Conformational comparison of apelin isoforms was carried out by circular dichroism and heteronuclear solution-state nuclear magnetic resonance spectroscopy. RESULTS: Apelin-55 is shown to activate the AR, with similar maximum ERK phophorylation response and potency to the shorter isoforms except for apelin-13, which exhibited a greater potency. Correlating to this shared activity, highly similar conformations are exhibited in all apelin isoforms for the shared C-terminal region responsible for receptor binding and activation. CONCLUSIONS: AR activation by all apelin isoforms likely hinges upon shared conformation and dynamics in the C-terminus, with apelin-55 providing an alternative bioactive isoform despite the addition of 19N-terminal residues relative to apelin-36. GENERAL SIGNIFICANCE: Beyond providing novel insight into the physiology of this system, re-annotation of proapelin to the bioactive apelin-55 isoform adds to the molecular toolkit for dissection of apelin-AR interactions and expands the repertoire of therapeutic targets for the apelinergic system.
[Mh] Termos MeSH primário: Peptídeos e Proteínas de Sinalização Intercelular/fisiologia
Precursores de Proteínas/fisiologia
Receptores Acoplados a Proteínas-G/fisiologia
[Mh] Termos MeSH secundário: Apelina
Receptores de Apelina
MAP Quinases Reguladas por Sinal Extracelular/metabolismo
Células HEK293
Seres Humanos
Peptídeos e Proteínas de Sinalização Intercelular/química
Ligantes
Espectroscopia de Ressonância Magnética
Fosforilação
Conformação Proteica
Isoformas de Proteínas
Receptores Acoplados a Proteínas-G/química
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (APLN protein, human); 0 (APLNR protein, human); 0 (Apelin); 0 (Apelin Receptors); 0 (Intercellular Signaling Peptides and Proteins); 0 (Ligands); 0 (Protein Isoforms); 0 (Protein Precursors); 0 (Receptors, G-Protein-Coupled); EC 2.7.11.24 (Extracellular Signal-Regulated MAP Kinases)
[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:170527
[St] Status:MEDLINE


  6 / 622 MEDLINE  
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[PMID]:28299332
[Au] Autor:Xu S; Zhang J; Xu YL; Wu HB; Xue XD; Wang HS
[Ad] Endereço:Department of Cardiovascular Surgery, Xijing Hospital, Fourth Military Medical University, Xi'an, Shaanxi 710032, China; Department of Cardiovascular Surgery, General Hospital of Shenyang Military Region, No. 83, Wenhua Road, Shenhe District, Shenyang, Liaoning 110016, China.
[Ti] Título:Relationship between Angiotensin Converting Enzyme, Apelin, and New-Onset Atrial Fibrillation after Off-Pump Coronary Artery Bypass Grafting.
[So] Source:Biomed Res Int;2017:7951793, 2017.
[Is] ISSN:2314-6141
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:It has been shown that inflammation and oxidative stress are important factors in postoperative atrial fibrillation (POAF). Angiotensin converting enzyme (ACE) and apelin have a close relationship with inflammation and oxidative stress. The effect of ACE and apelin on POAF after off-pump coronary artery bypass grafting (OPCABG) remains a question. The concentrations of serum ACE, angiotensin II (Ang II), apelin, bradykinin (BK), malondialdehyde (MDA), and C reactive protein (CRP) were measured in the perioperative period of OPCABG. The levels of serum ACE in the POAF group were higher than in the no POAF group both preoperatively and postoperatively. Apelin in the POAF group was lower than in the no POAF group. There was a correlation between serum ACE and apelin. Postoperatively, CRP and MDA in the POAF group were higher than in the no POAF group; however, there was no difference before the operation. Preoperative ACE and apelin were both significant and independent risk factors for POAF. In conclusion, the high ACE and low apelin preoperatively led to CRP and MDA being increased postoperatively, which was probably associated with POAF after OPCABG. Apelin may be a new predictor for POAF.
[Mh] Termos MeSH primário: Fibrilação Atrial/etiologia
Ponte de Artéria Coronária sem Circulação Extracorpórea/efeitos adversos
Peptídeos e Proteínas de Sinalização Intercelular/sangue
Peptidil Dipeptidase A/sangue
[Mh] Termos MeSH secundário: Idoso
Angiotensina II/sangue
Apelina
Fibrilação Atrial/fisiopatologia
Bradicinina/sangue
Proteína C-Reativa/metabolismo
Estudos de Casos e Controles
Feminino
Seres Humanos
Inflamação
Masculino
Malondialdeído/sangue
Meia-Idade
Análise Multivariada
Estresse Oxidativo
Complicações Pós-Operatórias
Período Pós-Operatório
Período Pré-Operatório
Estudos Retrospectivos
Fatores de Risco
[Pt] Tipo de publicação:CLINICAL TRIAL; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (APLN protein, human); 0 (Apelin); 0 (Intercellular Signaling Peptides and Proteins); 11128-99-7 (Angiotensin II); 4Y8F71G49Q (Malondialdehyde); 9007-41-4 (C-Reactive Protein); EC 3.4.15.1 (ACE protein, human); EC 3.4.15.1 (Peptidyl-Dipeptidase A); S8TIM42R2W (Bradykinin)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170317
[St] Status:MEDLINE
[do] DOI:10.1155/2017/7951793


  7 / 622 MEDLINE  
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[PMID]:28289180
[Au] Autor:Schinzari F; Veneziani A; Mores N; Barini A; Di Daniele N; Cardillo C; Tesauro M
[Ad] Endereço:From the Departments of Internal Medicine (F.S., C.C.), Surgery (A.V.), Pharmacology (N.M.), and Biochemistry (A.B.), Catholic University, Rome, Italy; and Department of Internal Medicine, University of Tor Vergata, Rome, Italy (N.D.D., M.T.).
[Ti] Título:Beneficial Effects of Apelin on Vascular Function in Patients With Central Obesity.
[So] Source:Hypertension;69(5):942-949, 2017 May.
[Is] ISSN:1524-4563
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Patients with central obesity have impaired insulin-stimulated vasodilation and increased ET-1 (endothelin 1) vasoconstriction, which may contribute to insulin resistance and vascular damage. Apelin enhances insulin sensitivity and glucose disposal but also acts as a nitric oxide (NO)-dependent vasodilator and a counter-regulator of AT (angiotensin [Ang] II type 1) receptor-induced vasoconstriction. We, therefore, examined the effects of exogenous (Pyr )apelin on NO-mediated vasodilation and Ang II- or ET-1-dependent vasoconstrictor tone in obese patients. In the absence of hyperinsulinemia, forearm blood flow responses to graded doses of acetylcholine and sodium nitroprusside were not different during saline or apelin administration (both >0.05). During intra-arterial infusion of regular insulin, however, apelin enhanced the vasodilation induced by both acetylcholine and nitroprusside (both <0.05). Interestingly, the vasodilator effect of concurrent blockade of AT (telmisartan) and AT (PD 123,319) receptors was blunted by apelin (3±5% versus 32±9%; <0.05). Similarly, during apelin administration, blockade of ET receptors (BQ-123) resulted in lower vasodilator response than during saline (23±10% versus 65±12%; <0.05). NO synthase inhibition by L-NMMA (l- -monometylarginine) during the concurrent blockade of either Ang II or ET receptors resulted in similar vasoconstriction in the absence or presence of apelin ( >0.05). In conclusion, in patients with central obesity, apelin has favorable effects not only to improve insulin-stimulated endothelium-dependent and endothelium-independent vasodilator responses but also to blunt Ang II- and ET-1-dependent vasoconstriction by a mechanism not involving NO. Taken together, our results suggest that targeting the apelin system might favorably impact some hemodynamic abnormalities of insulin-resistant states like obesity.
[Mh] Termos MeSH primário: Anexinas/efeitos dos fármacos
Endotélio Vascular/efeitos dos fármacos
Peptídeos e Proteínas de Sinalização Intercelular/farmacologia
Obesidade/fisiopatologia
Vasodilatação/efeitos dos fármacos
[Mh] Termos MeSH secundário: Acetilcolina/farmacologia
Adulto
Bloqueadores do Receptor Tipo 1 de Angiotensina II/farmacologia
Bloqueadores do Receptor Tipo 2 de Angiotensina II/farmacologia
Apelina
Benzimidazóis/farmacologia
Benzoatos/farmacologia
Feminino
Antebraço/irrigação sanguínea
Seres Humanos
Imidazóis/farmacologia
Masculino
Meia-Idade
Óxido Nítrico/metabolismo
Nitroprussiato/farmacologia
Piridinas/farmacologia
Fluxo Sanguíneo Regional/efeitos dos fármacos
ômega-N-Metilarginina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (APLN protein, human); 0 (Angiotensin II Type 1 Receptor Blockers); 0 (Angiotensin II Type 2 Receptor Blockers); 0 (Annexins); 0 (Apelin); 0 (Benzimidazoles); 0 (Benzoates); 0 (Imidazoles); 0 (Intercellular Signaling Peptides and Proteins); 0 (Pyridines); 0 (vasocortin); 130663-39-7 (PD 123319); 169D1260KM (Nitroprusside); 27JT06E6GR (omega-N-Methylarginine); 31C4KY9ESH (Nitric Oxide); N9YNS0M02X (Acetylcholine); U5SYW473RQ (telmisartan)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170315
[St] Status:MEDLINE
[do] DOI:10.1161/HYPERTENSIONAHA.116.08916


  8 / 622 MEDLINE  
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[PMID]:28218908
[Au] Autor:Langen UH; Pitulescu ME; Kim JM; Enriquez-Gasca R; Sivaraj KK; Kusumbe AP; Singh A; Di Russo J; Bixel MG; Zhou B; Sorokin L; Vaquerizas JM; Adams RH
[Ad] Endereço:Max Planck Institute for Molecular Biomedicine, Department of Tissue Morphogenesis, and University of Münster, Faculty of Medicine, D-48149 Münster, Germany.
[Ti] Título:Cell-matrix signals specify bone endothelial cells during developmental osteogenesis.
[So] Source:Nat Cell Biol;19(3):189-201, 2017 Mar.
[Is] ISSN:1476-4679
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Blood vessels in the mammalian skeletal system control bone formation and support haematopoiesis by generating local niche environments. While a specialized capillary subtype, termed type H, has been recently shown to couple angiogenesis and osteogenesis in adolescent, adult and ageing mice, little is known about the formation of specific endothelial cell populations during early developmental endochondral bone formation. Here, we report that embryonic and early postnatal long bone contains a specialized endothelial cell subtype, termed type E, which strongly supports osteoblast lineage cells and later gives rise to other endothelial cell subpopulations. The differentiation and functional properties of bone endothelial cells require cell-matrix signalling interactions. Loss of endothelial integrin ß1 leads to endothelial cell differentiation defects and impaired postnatal bone growth, which is, in part, phenocopied by endothelial cell-specific laminin α5 mutants. Our work outlines fundamental principles of vessel formation and endothelial cell differentiation in the developing skeletal system.
[Mh] Termos MeSH primário: Osso e Ossos/citologia
Células Endoteliais/metabolismo
Matriz Extracelular/metabolismo
Osteogênese
Transdução de Sinais
[Mh] Termos MeSH secundário: Adipocinas/metabolismo
Animais
Apelina
Osso e Ossos/irrigação sanguínea
Osso e Ossos/diagnóstico por imagem
Capilares/citologia
Adesão Celular
Citometria de Fluxo
Imuno-Histoquímica
Integrases/metabolismo
Integrina beta1/metabolismo
Peptídeos e Proteínas de Sinalização Intercelular/metabolismo
Camundongos Endogâmicos C57BL
Camundongos Mutantes
Neovascularização Fisiológica
Fenótipo
Microtomografia por Raio-X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adipokines); 0 (Apelin); 0 (Apln protein, mouse); 0 (Integrin beta1); 0 (Intercellular Signaling Peptides and Proteins); EC 2.7.7.- (Cre recombinase); EC 2.7.7.- (Integrases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170221
[St] Status:MEDLINE
[do] DOI:10.1038/ncb3476


  9 / 622 MEDLINE  
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[PMID]:28199472
[Au] Autor:Kelly TN; Li C; Hixson JE; Gu D; Rao DC; Huang J; Rice TK; Chen J; Cao J; Li J; Anderson CE; He J
[Ad] Endereço:Department of Epidemiology, Tulane University School of Public Health and Tropical Medicine, New Orleans, Louisiana, USA.
[Ti] Título:Resequencing Study Identifies Rare Renin-Angiotensin-Aldosterone System Variants Associated With Blood Pressure Salt-Sensitivity: The GenSalt Study.
[So] Source:Am J Hypertens;30(5):495-501, 2017 May 01.
[Is] ISSN:1941-7225
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The role of rare variants in blood pressure (BP) salt-sensitivity is unknown. We conducted a resequencing study of the renin-angiotensin-aldosterone system (RAAS) to identify rare variants associated with BP salt-sensitivity among participants of the Genetic Epidemiology Network of Salt-Sensitivity (GenSalt) study. METHODS: The GenSalt study was conducted among 1,906 participants who underwent a 7-day low-sodium (51.3 mmol sodium/day) followed by a 7-day high-sodium feeding study (307.8 mmol sodium/day). The 300 most salt-sensitive and 300 most salt-resistant GenSalt participants were selected for the resequencing study. Seven RAAS genes were resequenced using capillary-based sequencing methods. Rare variants were tested for association with BP salt-sensitivity using traditional burden tests. Single-marker analyses were employed to test associations of low-frequency and common variants. RESULTS: Aggregate rare variant analysis revealed an association of the RAAS pathway with BP salt-sensitivity. Carriers of rare RAAS variants had a 1.55-fold [95% confidence interval (CI): 1.15, 2.10] higher odds of salt-sensitivity compared to noncarriers (P = 0.004), a finding which was significant after Bonferroni correction. A nominal association of the APLN gene with salt-sensitivity was also identified, with rare APLN variants conferring a 2.22-fold (95% CI: 1.05, 6.58) higher odds of salt-sensitivity (P = 0.03). Single-marker analyses did not identify variant-BP salt-sensitivity associations after Bonferroni adjustment. A nominal association of a low-frequency, missense RENBP variant was identified. Each minor allele of rs78377269 conferred a 2.21-fold (95% CI: 1.10, 4.42) increased odds of salt-sensitivity (P = 0.03). CONCLUSIONS: This study presents of the first evidence of a contribution of rare RAAS variants to BP salt-sensitivity. Clinical Trial RegistryTrial Number: NCT00721721.
[Mh] Termos MeSH primário: Pressão Sanguínea/genética
Hipertensão/genética
Polimorfismo de Nucleotídeo Único
Sistema Renina-Angiotensina/genética
Cloreto de Sódio na Dieta/efeitos adversos
[Mh] Termos MeSH secundário: Adulto
Apelina
Carboidratos Epimerases/genética
Proteínas de Transporte/genética
Distribuição de Qui-Quadrado
China/epidemiologia
Dieta Hipossódica
Feminino
Frequência do Gene
Predisposição Genética para Doença
Seres Humanos
Hipertensão/diagnóstico
Hipertensão/epidemiologia
Hipertensão/fisiopatologia
Peptídeos e Proteínas de Sinalização Intercelular/genética
Modelos Lineares
Masculino
Meia-Idade
Análise Multivariada
Razão de Chances
Fenótipo
Medição de Risco
Fatores de Risco
Cloreto de Sódio na Dieta/administração & dosagem
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (APLN protein, human); 0 (Apelin); 0 (Carrier Proteins); 0 (Intercellular Signaling Peptides and Proteins); 0 (Sodium Chloride, Dietary); EC 5.1.3.- (Carbohydrate Epimerases); EC 5.1.3.8 (RENBP protein, human)
[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:170216
[St] Status:MEDLINE
[do] DOI:10.1093/ajh/hpx004


  10 / 622 MEDLINE  
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[PMID]:28137936
[Au] Autor:Yang P; Read C; Kuc RE; Buonincontri G; Southwood M; Torella R; Upton PD; Crosby A; Sawiak SJ; Carpenter TA; Glen RC; Morrell NW; Maguire JJ; Davenport AP
[Ad] Endereço:From Experimental Medicine and Immunotherapeutics, University of Cambridge, Centre for Clinical Investigation, Addenbrooke's Hospital, UK (P.Y., C.R., R.E.K., J.J.M., A.P.D.); Wolfson Brain Imaging Centre, Department of Clinical Neuroscience, University of Cambridge, UK (G.B., S.J.S., T.A.C.); Depar
[Ti] Título:Elabela/Toddler Is an Endogenous Agonist of the Apelin APJ Receptor in the Adult Cardiovascular System, and Exogenous Administration of the Peptide Compensates for the Downregulation of Its Expression in Pulmonary Arterial Hypertension.
[So] Source:Circulation;135(12):1160-1173, 2017 Mar 21.
[Is] ISSN:1524-4539
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Elabela/toddler (ELA) is a critical cardiac developmental peptide that acts through the G-protein-coupled apelin receptor, despite lack of sequence similarity to the established ligand apelin. Our aim was to investigate the receptor pharmacology, expression pattern, and in vivo function of ELA peptides in the adult cardiovascular system, to seek evidence for alteration in pulmonary arterial hypertension (PAH) in which apelin signaling is downregulated, and to demonstrate attenuation of PAH severity with exogenous administration of ELA in a rat model. METHODS: docking analysis, competition binding experiments, and downstream assays were used to characterize ELA receptor binding in human heart and signaling in cells expressing the apelin receptor. ELA expression in human cardiovascular tissues and plasma was determined using real-time quantitative polymerase chain reaction, dual-labeling immunofluorescent staining, and immunoassays. Acute cardiac effects of ELA-32 and [Pyr ]apelin-13 were assessed by MRI and cardiac catheterization in anesthetized rats. Cardiopulmonary human and rat tissues from PAH patients and monocrotaline- and Sugen/hypoxia-exposed rats were used to show changes in ELA expression in PAH. The effect of ELA treatment on cardiopulmonary remodeling in PAH was investigated in the monocrotaline rat model. RESULTS: ELA competed for binding of apelin in human heart with overlap for the 2 peptides indicated by modeling. ELA activated G-protein- and ß-arrestin-dependent pathways. We detected ELA expression in human vascular endothelium and plasma. Comparable to apelin, ELA increased cardiac contractility, ejection fraction, and cardiac output and elicited vasodilatation in rat in vivo. ELA expression was reduced in cardiopulmonary tissues from PAH patients and PAH rat models, respectively. ELA treatment significantly attenuated elevation of right ventricular systolic pressure and right ventricular hypertrophy and pulmonary vascular remodeling in monocrotaline-exposed rats. CONCLUSIONS: These results show that ELA is an endogenous agonist of the human apelin receptor, exhibits a cardiovascular profile comparable to apelin, and is downregulated in human disease and rodent PAH models, and exogenous peptide can reduce the severity of cardiopulmonary remodeling and function in PAH in rats. This study provides additional proof of principle that an apelin receptor agonist may be of therapeutic use in PAH in humans.
[Mh] Termos MeSH primário: Hipertensão Pulmonar/tratamento farmacológico
Hormônios Peptídicos/uso terapêutico
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Apelina
Sítios de Ligação
Cateterismo
Modelos Animais de Doenças
Regulação para Baixo/efeitos dos fármacos
Endotélio Vascular/efeitos dos fármacos
Endotélio Vascular/metabolismo
Ventrículos do Coração/efeitos dos fármacos
Ventrículos do Coração/metabolismo
Seres Humanos
Hipertensão Pulmonar/fisiopatologia
Peptídeos e Proteínas de Sinalização Intercelular/agonistas
Peptídeos e Proteínas de Sinalização Intercelular/química
Peptídeos e Proteínas de Sinalização Intercelular/metabolismo
Peptídeos e Proteínas de Sinalização Intercelular/farmacologia
Peptídeos e Proteínas de Sinalização Intercelular/uso terapêutico
Masculino
Simulação de Dinâmica Molecular
Hormônios Peptídicos/química
Hormônios Peptídicos/metabolismo
Hormônios Peptídicos/farmacologia
Estrutura Terciária de Proteína
Ratos
Ratos Sprague-Dawley
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (APLN protein, human); 0 (Apelin); 0 (ELA peptide, human); 0 (Intercellular Signaling Peptides and Proteins); 0 (Peptide Hormones); 0 (apelin-13 peptide)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170201
[St] Status:MEDLINE
[do] DOI:10.1161/CIRCULATIONAHA.116.023218



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