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Pesquisa : D08.811.913.696.620.682.700.062.500 [Categoria DeCS]
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[PMID]:28977600
[Au] Autor:Bai L; Chang HM; Cheng JC; Chu G; Leung PCK; Yang G
[Ad] Endereço:College of Animal Science and Technology, Northwest A&F University, Yangling, Shaanxi 712100, People's Republic of China.
[Ti] Título:ALK2/ALK3-BMPR2/ACVR2A Mediate BMP2-Induced Downregulation of Pentraxin 3 Expression in Human Granulosa-Lutein Cells.
[So] Source:Endocrinology;158(10):3501-3511, 2017 Oct 01.
[Is] ISSN:1945-7170
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bone morphogenetic protein 2 (BMP2) belongs to the transforming growth factor-ß superfamily and plays a critical role in regulating ovarian follicle function. Currently, the role of BMP2 during cumulus expansion remains to be determined. The aim of this study was to investigate the effect of BMP2 on the regulation of pentraxin 3 (PTX3) expression (the major component of cumulus expansion) and the underlying mechanisms in human granulosa-lutein (hGL) cells. Both primary and immortalized hGL cells were used as research models. Our results showed that treatment with BMP2 significantly suppressed the basal and luteinizing hormone-induced upregulation of PTX3. In addition, BMP2 stimulated the phosphorylation of SMAD1/5/8, and this effect was abolished by the addition of BMP type I receptor inhibitors, dorsomorphin homolog 1, and dorsomorphin but not SB431542. Moreover, the knockdown of activin receptorlike kinase 2/3 or BMP receptor type II/activin receptor type IIB receptors completely reversed the BMP2-induced phosphorylation of SMAD1/5/8 and restored PTX3 expression. Similarly, the knockdown of SMAD4 completely reversed the suppressive effect of BMP2 on the expression of PTX3. These results improve our understanding of the molecular mechanisms of BMP2 signaling. Our findings suggest that BMP2 may be involved in the regulation of cumulus expansion during the periovulatory stage.
[Mh] Termos MeSH primário: Proteína Morfogenética Óssea 2/farmacologia
Proteína C-Reativa/efeitos dos fármacos
Células Lúteas/efeitos dos fármacos
Componente Amiloide P Sérico/efeitos dos fármacos
[Mh] Termos MeSH secundário: Receptores de Ativinas Tipo I/genética
Receptores de Activinas Tipo II/genética
Benzamidas/farmacologia
Western Blotting
Receptores de Proteínas Morfogenéticas Ósseas Tipo I/genética
Receptores de Proteínas Morfogenéticas Ósseas Tipo II/genética
Proteína C-Reativa/genética
Proteína C-Reativa/metabolismo
Dioxóis/farmacologia
Regulação para Baixo
Ensaio de Imunoadsorção Enzimática
Feminino
Técnicas de Silenciamento de Genes
Seres Humanos
Células Lúteas/metabolismo
Indução da Ovulação
Fosforilação/efeitos dos fármacos
Inibidores de Proteínas Quinases/farmacologia
Pirazóis/farmacologia
Pirimidinas/farmacologia
RNA Interferente Pequeno
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Componente Amiloide P Sérico/genética
Componente Amiloide P Sérico/metabolismo
Proteína Smad1/efeitos dos fármacos
Proteína Smad1/metabolismo
Proteína Smad4/genética
Proteína Smad5/efeitos dos fármacos
Proteína Smad5/metabolismo
Proteína Smad8/efeitos dos fármacos
Proteína Smad8/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide); 0 (BMP2 protein, human); 0 (Benzamides); 0 (Bone Morphogenetic Protein 2); 0 (Dioxoles); 0 (Protein Kinase Inhibitors); 0 (Pyrazoles); 0 (Pyrimidines); 0 (RNA, Small Interfering); 0 (SMAD1 protein, human); 0 (SMAD4 protein, human); 0 (SMAD5 protein, human); 0 (SMAD8 protein, human); 0 (Serum Amyloid P-Component); 0 (Smad1 Protein); 0 (Smad4 Protein); 0 (Smad5 Protein); 0 (Smad8 Protein); 10K52CIC1Z ((6-(4-(2-piperidin-1-ylethoxy)phenyl))-3-pyridin-4-ylpyrazolo(1,5-a)pyrimidine); 148591-49-5 (PTX3 protein); 9007-41-4 (C-Reactive Protein); EC 2.7.11.30 (ACVR1 protein, human); EC 2.7.11.30 (ACVR2B protein, human); EC 2.7.11.30 (Activin Receptors, Type I); EC 2.7.11.30 (Activin Receptors, Type II); EC 2.7.11.30 (BMPR1A protein, human); EC 2.7.11.30 (BMPR2 protein, human); EC 2.7.11.30 (Bone Morphogenetic Protein Receptors, Type I); EC 2.7.11.30 (Bone Morphogenetic Protein Receptors, Type II); EC 2.7.11.30 (activin receptor type II-A)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:171005
[St] Status:MEDLINE
[do] DOI:10.1210/en.2017-00436


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[PMID]:28782519
[Au] Autor:Kim M; Choi O; Pyo S; Choi SU; Park CH
[Ad] Endereço:Bio & Drug Discovery Division, Korea Research Institute of Chemical Technology, PO Box 107, Daejeon 305-600, Republic of Korea; School of Pharmacy, Sungkyunkwan University, Suwon City, Kyunggi-do, 440-746, Republic of Korea.
[Ti] Título:Identification of novel ALK2 inhibitors and their effect on cancer cells.
[So] Source:Biochem Biophys Res Commun;492(1):121-127, 2017 Oct 07.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bone morphogenetic protein 9 (BMP9), a member of the TGF-ß superfamily, is considered a regulator of glucose homeostasis as well as a neuronal differentiation factor. BMP9 induces phosphorylation of Smad1/5 through activin receptor-like kinase 1 and 2 (ALK1 and ALK2). Recently, many studies have shown that BMP9 contributes to tumorigenesis, and aberrant ALK2 expression is involved in many diseases. To investigate the role of BMP9-ALK2 signaling in cancer cells, we used TF-1 cells that require granulocyte-macrophage colony-stimulating factor (GM-CSF) for cell proliferation. BMP9 promoted the proliferation of TF-1 cells in media lacking GM-CSF. TF-1 cells overexpressing ALK2 resulted in the autophosphorylation of Smad1/5, leading to consequent increase in cell growth. Through high-throughput screening (HTS), we found two ALK2-specific inhibitors, KRC203 and KRC360, with IC values of 0.9 nM and 0.3 nM. These compounds were more potent and specific for the inhibition of ALK2 when compared to LDN193189. In cell-based assays, these compounds effectively inhibited the proliferation and migration of cancer cells induced by ALK2 and BMP9. Therefore, we propose that our compounds are promising candidates for the treatment of cancer or diseases with abnormal ALK2 or BMP9 signaling.
[Mh] Termos MeSH primário: Receptores de Ativinas Tipo I/antagonistas & inibidores
Neoplasias/enzimologia
Neoplasias/patologia
Inibidores de Proteínas Quinases/farmacologia
[Mh] Termos MeSH secundário: Receptores de Ativinas Tipo I/metabolismo
Animais
Movimento Celular/efeitos dos fármacos
Proliferação Celular/efeitos dos fármacos
Células Cultivadas
Relação Dose-Resposta a Droga
Células Hep G2
Seres Humanos
Camundongos
Estrutura Molecular
Células NIH 3T3
Inibidores de Proteínas Quinases/química
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Kinase Inhibitors); EC 2.7.11.30 (ACVR1 protein, human); EC 2.7.11.30 (Activin Receptors, Type I)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170808
[St] Status:MEDLINE


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[PMID]:28668833
[Au] Autor:Hu T; Su F; Jiang W; Dart DA
[Ad] Endereço:Cardiff China Medical Research Collaborative, Cardiff University School of Medicine, Henry Wellcome Building, Heath Park, Cardiff, U.K.
[Ti] Título:Overexpression of Activin Receptor-like Kinase 7 in Breast Cancer Cells Is Associated with Decreased Cell Growth and Adhesion.
[So] Source:Anticancer Res;37(7):3441-3451, 2017 07.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:AIM: To examine the expression and function of activin receptor-like kinase 7 (ALK7) in breast cancer, its association with disease prognosis, and its impact on breast cancer cell function. PATIENTS AND METHODS: A cohort of patients with breast cancer were examined for ALK7 expression in association with pathological and clinical aspects. In vitro cell assays of ALK7 were investigated using an expression plasmid. RESULTS: Overall higher levels of ALK7 transcripts were seen in the breast cancer samples vs. normal tissue. However, within the cancer cohort, lower levels of ALK7 transcript were associated with poor prognosis. Patients with lower expression of ALK7 also had shorter survival. Overexpression of ALK7 reduced proliferation and adhesion of breast cancer cells in vitro. We found that overexpressed ALK7 had complex effects on the MCF-7 cell sensitivity to chemotherapy drugs. CONCLUSION: Decreased expression of ALK7 in breast cancer is correlated with poor prognosis. ALK7 is a negative regulator of adhesion and proliferation of breast cancer cells. This suggests that ALK7 is a potential tumor suppressor in breast cancer.
[Mh] Termos MeSH primário: Receptores de Ativinas Tipo I/genética
Neoplasias da Mama/genética
Neoplasias da Mama/patologia
Adesão Celular/genética
Proliferação Celular/genética
[Mh] Termos MeSH secundário: Antineoplásicos/farmacologia
Neoplasias da Mama/tratamento farmacológico
Adesão Celular/efeitos dos fármacos
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Feminino
Seres Humanos
Células MCF-7
Prognóstico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); EC 2.7.11.30 (ACVR1C protein, human); EC 2.7.11.30 (Activin Receptors, Type I)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170703
[St] Status:MEDLINE


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[PMID]:28646109
[Au] Autor:Mitrofan CG; Appleby SL; Nash GB; Mallat Z; Chilvers ER; Upton PD; Morrell NW
[Ad] Endereço:From the Department of Medicine, University of Cambridge School of Clinical Medicine, Cambridge CB2 0QQ and.
[Ti] Título:Bone morphogenetic protein 9 (BMP9) and BMP10 enhance tumor necrosis factor-α-induced monocyte recruitment to the vascular endothelium mainly via activin receptor-like kinase 2.
[So] Source:J Biol Chem;292(33):13714-13726, 2017 Aug 18.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bone morphogenetic proteins 9 and 10 (BMP9/BMP10) are circulating cytokines with important roles in endothelial homeostasis. The aim of this study was to investigate the roles of BMP9 and BMP10 in mediating monocyte-endothelial interactions using an flow adhesion assay. Herein, we report that whereas BMP9/BMP10 alone had no effect on monocyte recruitment, at higher concentrations both cytokines synergized with tumor necrosis factor-α (TNFα) to increase recruitment to the vascular endothelium. The BMP9/BMP10-mediated increase in monocyte recruitment in the presence of TNFα was associated with up-regulated expression levels of E-selectin, vascular cell adhesion molecule (VCAM-1), and intercellular adhesion molecule 1 (ICAM-1) on endothelial cells. Using siRNAs to type I and II BMP receptors and the signaling intermediaries (Smads), we demonstrated a key role for ALK2 in the BMP9/BMP10-induced surface expression of E-selectin, and both ALK1 and ALK2 in the up-regulation of VCAM-1 and ICAM-1. The type II receptors, BMPR-II and ACTR-IIA were both required for this response, as was Smad1/5. The up-regulation of cell surface adhesion molecules by BMP9/10 in the presence of TNFα was inhibited by LDN193189, which inhibits ALK2 but not ALK1. Furthermore, LDN193189 inhibited monocyte recruitment induced by TNFα and BMP9/10. BMP9/10 increased basal IκBα protein expression, but did not alter p65/RelA levels. Our findings suggest that higher concentrations of BMP9/BMP10 synergize with TNFα to induce the up-regulation of endothelial selectins and adhesion molecules, ultimately resulting in increased monocyte recruitment to the vascular endothelium. This process is mediated mainly via the ALK2 type I receptor, BMPR-II/ACTR-IIA type II receptors, and downstream Smad1/5 signaling.
[Mh] Termos MeSH primário: Receptores de Ativinas Tipo I/metabolismo
Proteínas Morfogenéticas Ósseas/metabolismo
Endotélio Vascular/metabolismo
Fatores de Diferenciação de Crescimento/metabolismo
Monócitos/metabolismo
Fator de Necrose Tumoral alfa/metabolismo
[Mh] Termos MeSH secundário: Receptores de Ativinas Tipo I/antagonistas & inibidores
Receptores de Ativinas Tipo I/genética
Receptores de Activinas Tipo II/antagonistas & inibidores
Receptores de Activinas Tipo II/genética
Receptores de Activinas Tipo II/metabolismo
Aorta
Adesão Celular/efeitos dos fármacos
Células Cultivadas
Selectina E/química
Selectina E/genética
Selectina E/metabolismo
Endotélio Vascular/citologia
Endotélio Vascular/efeitos dos fármacos
Endotélio Vascular/imunologia
Seres Humanos
Molécula 1 de Adesão Intercelular/química
Molécula 1 de Adesão Intercelular/genética
Molécula 1 de Adesão Intercelular/metabolismo
Cinética
Monócitos/citologia
Monócitos/efeitos dos fármacos
Monócitos/imunologia
Fosforilação/efeitos dos fármacos
Inibidores de Proteínas Quinases/farmacologia
Processamento de Proteína Pós-Traducional/efeitos dos fármacos
Pirazóis/farmacologia
Pirimidinas/farmacologia
Interferência de RNA
Transdução de Sinais/efeitos dos fármacos
Fator de Necrose Tumoral alfa/agonistas
Regulação para Cima/efeitos dos fármacos
Molécula 1 de Adesão de Célula Vascular/química
Molécula 1 de Adesão de Célula Vascular/genética
Molécula 1 de Adesão de Célula Vascular/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BMP10 protein, human); 0 (Bone Morphogenetic Proteins); 0 (E-Selectin); 0 (GDF2 protein, human); 0 (Growth Differentiation Factors); 0 (ICAM1 protein, human); 0 (LDN 193189); 0 (Protein Kinase Inhibitors); 0 (Pyrazoles); 0 (Pyrimidines); 0 (SELE protein, human); 0 (TNF protein, human); 0 (Tumor Necrosis Factor-alpha); 0 (Vascular Cell Adhesion Molecule-1); 126547-89-5 (Intercellular Adhesion Molecule-1); EC 2.7.11.30 (ACVR1 protein, human); EC 2.7.11.30 (ACVRL1 protein, human); EC 2.7.11.30 (Activin Receptors, Type I); EC 2.7.11.30 (Activin Receptors, Type II)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170625
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.778506


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[PMID]:28642261
[Au] Autor:Zhang H; Du L; Zhong Y; Flanders KC; Roberts JD
[Ad] Endereço:Cardiovascular Research Center of the General Medical Services, Massachusetts General Hospital, Boston, Massachusetts.
[Ti] Título:Transforming growth factor-ß stimulates Smad1/5 signaling in pulmonary artery smooth muscle cells and fibroblasts of the newborn mouse through ALK1.
[So] Source:Am J Physiol Lung Cell Mol Physiol;313(3):L615-L627, 2017 Sep 01.
[Is] ISSN:1522-1504
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The intracellular signaling mechanisms through which TGF-ß regulates pulmonary development are incompletely understood. Canonical TGF-ß signaling involves Smad2/3 phosphorylation, Smad2/3·Smad4 complex formation and nuclear localization, and gene regulation. Here, we show that physiologically relevant TGF-ß1 levels also stimulate Smad1/5 phosphorylation, which is typically a mediator of bone morphogenetic protein (BMP) signaling, in mouse pup pulmonary artery smooth muscle cells (mPASMC) and lung fibroblasts and other interstitial lung cell lines. This cross-talk mechanism likely has in vivo relevance because mixed Smad1/5/8·Smad2/3 complexes, which are indicative of TGF-ß-stimulated Smad1/5 activation, were detected in the developing mouse lung using a proximity ligation assay. Although mixed Smad complexes have been shown not to transduce nuclear signaling, we determined that TGF-ß stimulates nuclear localization of phosphorylated Smad1/5 and induces the expression of prototypical BMP-regulated genes in the mPASMC. Small-molecule kinase inhibitor studies suggested that TGF-ß-regulated Smad1/5 phosphorylation in these cells is mediated by TGF-ß-type I receptors, not BMP-type I receptors, but possibly the accessory activin-like kinase (ALK1) receptor. Although work by others suggested that ALK1 is expressed exclusively in endothelial cells in the vasculature, we detected ALK1 mRNA and protein expression in mPASMC in vitro and in mouse pup lungs. Moreover, using an antimurine ALK1 antibody and mPASMC, we determined that ALK1 regulates Smad1/5 phosphorylation by TGF-ß. Together, these studies characterize an accessory TGF-ß-stimulated BMP R-Smad signaling mechanism in interstitial cells of the developing lung. They also indicate the importance of considering alternate Smad pathways in studies directed at determining how TGF-ß regulates newborn lung development.
[Mh] Termos MeSH primário: Receptores de Ativinas Tipo I/metabolismo
Fibroblastos/metabolismo
Miócitos de Músculo Liso/metabolismo
Artéria Pulmonar/citologia
Transdução de Sinais/efeitos dos fármacos
Proteína Smad1/metabolismo
Proteína Smad5/metabolismo
Fator de Crescimento Transformador beta/farmacologia
[Mh] Termos MeSH secundário: Animais
Animais Recém-Nascidos
Benzodioxóis/farmacologia
Receptores de Proteínas Morfogenéticas Ósseas/metabolismo
Linhagem Celular
Núcleo Celular/efeitos dos fármacos
Núcleo Celular/metabolismo
Seres Humanos
Imidazóis/farmacologia
Pulmão/crescimento & desenvolvimento
Pulmão/metabolismo
Camundongos
Miócitos de Músculo Liso/efeitos dos fármacos
Fosforilação/efeitos dos fármacos
Proteínas Serina-Treonina Quinases/metabolismo
Piridinas/farmacologia
Ratos
Receptores de Fatores de Crescimento Transformadores beta/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (2-(5-benzo(1,3)dioxol-5-yl-2-tert-butyl-3H-imidazol-4-yl)-6-methylpyridine hydrochloride); 0 (Benzodioxoles); 0 (Imidazoles); 0 (Pyridines); 0 (Receptors, Transforming Growth Factor beta); 0 (Smad1 Protein); 0 (Smad5 Protein); 0 (Transforming Growth Factor beta); EC 2.7.1.11 (TGF-beta type I receptor); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.30 (Activin Receptors, Type I); EC 2.7.11.30 (Acvr1 protein, mouse); EC 2.7.11.30 (Acvrl1 protein, mouse); EC 2.7.11.30 (Bone Morphogenetic Protein Receptors)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170624
[St] Status:MEDLINE
[do] DOI:10.1152/ajplung.00079.2017


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[PMID]:28641928
[Au] Autor:Pan H; Zhang H; Abraham P; Komatsu Y; Lyons K; Kaartinen V; Mishina Y
[Ad] Endereço:Department of Biologic & Materials Sciences, School of Dentistry, University of Michigan, 1011 N. University Ave., Ann Arbor, MI 48109, USA.
[Ti] Título:BmpR1A is a major type 1 BMP receptor for BMP-Smad signaling during skull development.
[So] Source:Dev Biol;429(1):260-270, 2017 09 01.
[Is] ISSN:1095-564X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Craniosynostosis is caused by premature fusion of one or more sutures in an infant skull, resulting in abnormal facial features. The molecular and cellular mechanisms by which genetic mutations cause craniosynostosis are incompletely characterized, and many of the causative genes for diverse types of syndromic craniosynostosis have not yet been identified. We previously demonstrated that augmentation of BMP signaling mediated by a constitutively active BMP type IA receptor (ca-BmpR1A) in neural crest cells (ca1A hereafter) causes craniosynostosis and superimposition of heterozygous null mutation of Bmpr1a rescues premature suture fusion (ca1A;1aH hereafter). In this study, we superimposed heterozygous null mutations of the other two BMP type I receptors, Bmpr1b and Acvr1 (ca1A;1bH and ca1A;AcH respectively hereafter) to further dissect involvement of BMP-Smad signaling. Unlike caA1;1aH, ca1A;1bH and ca1A;AcH did not restore the craniosynostosis phenotypes. In our in vivo study, Smad-dependent BMP signaling was decreased to normal levels in mut;1aH mice. However, BMP receptor-regulated Smads (R-Smads; pSmad1/5/9 hereafter) levels were comparable between ca1A, ca1A;1bH and ca1A;AcH mice, and elevated compared to control mice. Bmpr1a, Bmpr1b and Acvr1 null cells were used to examine potential mechanisms underlying the differences in ability of heterozygosity for Bmpr1a vs. Bmpr1b or Acvr1 to rescue the mut phenotype. pSmad1/5/9 level was undetectable in Bmpr1a homozygous null cells while pSmad1/5/9 levels did not decrease in Bmpr1b or Acvr1 homozygous null cells. Taken together, our study indicates that different levels of expression and subsequent activation of Smad signaling differentially contribute each BMP type I receptor to BMP-Smad signaling and craniofacial development. These results also suggest differential involvement of each type 1 receptor in pathogenesis of syndromic craniosynostoses.
[Mh] Termos MeSH primário: Receptores de Proteínas Morfogenéticas Ósseas Tipo I/metabolismo
Proteínas Morfogenéticas Ósseas/metabolismo
Transdução de Sinais
Crânio/embriologia
Crânio/metabolismo
Proteínas Smad/metabolismo
[Mh] Termos MeSH secundário: Receptores de Ativinas Tipo I/genética
Receptores de Ativinas Tipo I/metabolismo
Animais
Receptores de Proteínas Morfogenéticas Ósseas Tipo I/genética
Craniossinostoses/genética
Craniossinostoses/patologia
Regulação da Expressão Gênica no Desenvolvimento
Heterozigoto
Camundongos Endogâmicos C57BL
Mutação/genética
Osteoblastos/metabolismo
Fenótipo
Transdução de Sinais/genética
Crânio/anormalidades
Crânio/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Bone Morphogenetic Proteins); 0 (Smad Proteins); EC 2.7.11.30 (Activin Receptors, Type I); EC 2.7.11.30 (Acvr1 protein, mouse); EC 2.7.11.30 (Bone Morphogenetic Protein Receptors, Type I)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170624
[St] Status:MEDLINE


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[PMID]:28473268
[Au] Autor:Towler OW; Shore EM; Xu M; Bamford A; Anderson I; Pignolo RJ; Kaplan FS
[Ad] Endereço:Department of Orthopaedic Surgery, The Perelman School of Medicine at The University of Pennsylvania, Philadelphia, PA 19104, USA; The Center for Research in FOP & Related Disorders, The Perelman School of Medicine at The University of Pennsylvania, Philadelphia, PA 19104, USA.
[Ti] Título:The congenital great toe malformation of fibrodysplasia ossificans progressiva? - A close call.
[So] Source:Eur J Med Genet;60(7):399-402, 2017 Jul.
[Is] ISSN:1878-0849
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Congenital bilateral hallux valgus with associated absence or fusion of the interphalangeal joint is a classic diagnostic feature of fibrodysplasia ossificans progressiva (FOP), a human genetic disease of extra-skeletal bone formation caused in nearly all cases by a gain-of-function mutation in Activin A Receptor I/Activin-like Kinase 2 (ACVR1/ALK2), which encodes a bone morphogenetic protein (BMP) Type 1 receptor. This toe malformation prompts the suspicion of FOP even before the appearance of extra-skeletal bone. Here we report the case of a four-month-old child who was suspected of having FOP on the basis of a great toe malformation identical to that seen in children with the disease. METHODS: The patient's genomic DNA of the coding region of ACVR1 was sequenced and analyzed for mutations known to cause FOP and novel mutations. Subsequent comparative genomic hybridization (CGH) and single nucleotide polymorphism (SNP) analyses were performed to detect mutations elsewhere in the genome. RESULTS: Genetic testing exonerated ACVR1 as culpable for the patient's toe malformation. CGH and SNP analyses identified a large intragenic deletion in a different BMP Type 1 receptor gene, BMP Receptor 1B/Activin-like kinase 6 (BMPR1B/ALK6), a gene associated with a variable spectrum of autosomal dominant brachydactyly phenotypes. CONCLUSIONS: This report illustrates that while toe morphology remains the earliest indicator of FOP, toe morphology alone is not an unequivocal clinical diagnostic feature of FOP, and supports that embryonic development of the great toe is highly sensitive to dysregulated signaling from at least two BMP type I receptors.
[Mh] Termos MeSH primário: Miosite Ossificante/genética
Dedos do Pé/anormalidades
[Mh] Termos MeSH secundário: Receptores de Ativinas Tipo I/genética
Seres Humanos
Lactente
Masculino
Mutação
Miosite Ossificante/diagnóstico
Polimorfismo de Nucleotídeo Único
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.7.11.30 (ACVR1 protein, human); EC 2.7.11.30 (Activin Receptors, Type I)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170928
[Lr] Data última revisão:
170928
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170506
[St] Status:MEDLINE


  8 / 1234 MEDLINE  
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[PMID]:28232325
[Au] Autor:Lee HW; Chong DC; Ola R; Dunworth WP; Meadows S; Ka J; Kaartinen VM; Qyang Y; Cleaver O; Bautch VL; Eichmann A; Jin SW
[Ad] Endereço:From the Yale Cardiovascular Research Center, Section of Cardiovascular Medicine, Department of Internal Medicine, Yale University School of Medicine, New Haven, CT (H.-W.L., R.O., W.P.D., Y.Q., A.E., S.-W.J.); Department of Biology and McAllister Heart Institute, University of North Carolina, Chape
[Ti] Título:Alk2/ACVR1 and Alk3/BMPR1A Provide Essential Function for Bone Morphogenetic Protein-Induced Retinal Angiogenesis.
[So] Source:Arterioscler Thromb Vasc Biol;37(4):657-663, 2017 Apr.
[Is] ISSN:1524-4636
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Increasing evidence suggests that bone morphogenetic protein (BMP) signaling regulates angiogenesis. Here, we aimed to define the function of BMP receptors in regulating early postnatal angiogenesis by analysis of inducible, endothelial-specific deletion of the BMP receptor components (BMP type 2 receptor), (activin receptor-like kinase 1), , and in mouse retinal vessels. APPROACH AND RESULTS: Expression analysis of several BMP ligands showed that proangiogenic BMP ligands are highly expressed in postnatal retinas. Consistently, BMP receptors are also strongly expressed in retina with a distinct pattern. To assess the function of BMP signaling in retinal angiogenesis, we first generated mice carrying an endothelial-specific inducible deletion of . Postnatal deletion of in endothelial cells substantially decreased the number of angiogenic sprouts at the vascular front and branch points behind the front, leading to attenuated radial expansion. To identify critical BMPR1s (BMP type 1 receptors) associated with BMPR2 in retinal angiogenesis, we generated endothelial-specific inducible deletion of 3 BMPR1s abundantly expressed in endothelial cells and analyzed the respective phenotypes. Among these, endothelial-specific deletion of either / or / caused a delay in radial expansion, reminiscent of vascular defects associated with postnatal endothelial-specific deletion of BMPR2, suggesting that ALK2/ACVR1 and ALK3/BMPR1A are likely to be the critical BMPR1s necessary for proangiogenic BMP signaling in retinal vessels. CONCLUSIONS: Our data identify BMP signaling mediated by coordination of ALK2/ACVR1, ALK3/BMPR1A, and BMPR2 as an essential proangiogenic cue for retinal vessels.
[Mh] Termos MeSH primário: Receptores de Ativinas Tipo I/metabolismo
Receptores de Proteínas Morfogenéticas Ósseas Tipo I/metabolismo
Proteínas Morfogenéticas Ósseas/metabolismo
Células Endoteliais/efeitos dos fármacos
Artéria Retiniana/efeitos dos fármacos
Neovascularização Retiniana
[Mh] Termos MeSH secundário: Receptores de Ativinas Tipo I/deficiência
Receptores de Ativinas Tipo I/genética
Animais
Receptores de Proteínas Morfogenéticas Ósseas Tipo I/deficiência
Receptores de Proteínas Morfogenéticas Ósseas Tipo I/genética
Receptores de Proteínas Morfogenéticas Ósseas Tipo II/deficiência
Receptores de Proteínas Morfogenéticas Ósseas Tipo II/genética
Células Endoteliais/metabolismo
Regulação da Expressão Gênica no Desenvolvimento
Genótipo
Ligantes
Camundongos Endogâmicos C57BL
Camundongos Knockout
Fenótipo
Artéria Retiniana/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bone Morphogenetic Proteins); 0 (Ligands); EC 2.7.11.30 (Activin Receptors, Type I); EC 2.7.11.30 (Acvr1 protein, mouse); EC 2.7.11.30 (Acvrl1 protein, mouse); EC 2.7.11.30 (Bmpr1a protein, mouse); EC 2.7.11.30 (Bmpr2 protein, mouse); EC 2.7.11.30 (Bone Morphogenetic Protein Receptors, Type I); EC 2.7.11.30 (Bone Morphogenetic Protein Receptors, Type II)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170621
[Lr] Data última revisão:
170621
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170225
[St] Status:MEDLINE
[do] DOI:10.1161/ATVBAHA.116.308422


  9 / 1234 MEDLINE  
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[PMID]:28219934
[Au] Autor:Yu HF; Yue ZP; Wang K; Yang ZQ; Zhang HL; Geng S; Guo B
[Ad] Endereço:College of Veterinary MedicineJilin University, Changchun, People's Republic of China.
[Ti] Título: acts downstream of to regulate uterine decidualization via in mice.
[So] Source:J Endocrinol;233(2):145-157, 2017 May.
[Is] ISSN:1479-6805
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Although has been proved to play an important role in uterine decidualization, its regulatory mechanism remains largely unknown. Here, we showed that was highly expressed in the decidual cells and promoted the proliferation of uterine stromal cells and expression of and , which were two well-known differentiation markers for decidualization. Further analysis revealed that might act downstream of and cAMP to regulate the differentiation of uterine stromal cells. Administration of cAMP analog 8-Br-cAMP to siRNA-transfected stromal cells resulted in an obvious increase of expression, whereas PKA inhibitor H89 impeded the induction of elicited by overexpression, indicating that cAMP-PKA signal mediates the regulation of on expression. In uterine stromal cells, knockdown of blocked the cAMP induction of Moreover, siRNA-mediated downregulation of impaired the stimulatory effects of overexpression on the expression of and , whereas constitutive expression of reversed the inhibitory effects of siRNA on stromal differentiation. Meanwhile, might play a vital role in the crosstalk between and Collectively, may act downstream of cAMP-PKA signal to mediate the effects of on the differentiation of uterine stromal cells through targeting .
[Mh] Termos MeSH primário: Receptores de Ativinas Tipo I/metabolismo
Fatores de Transcrição Hélice-Alça-Hélice Básicos/metabolismo
Conexina 43/metabolismo
Regulação da Expressão Gênica/fisiologia
Útero/fisiologia
[Mh] Termos MeSH secundário: Receptores de Ativinas Tipo I/genética
Animais
Fatores de Transcrição Hélice-Alça-Hélice Básicos/genética
Diferenciação Celular
Proliferação Celular
Conexina 43/genética
AMP Cíclico/metabolismo
Proteínas Quinases Dependentes de AMP Cíclico/metabolismo
Feminino
Camundongos
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Células Estromais/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Basic Helix-Loop-Helix Transcription Factors); 0 (Connexin 43); 0 (GJA1 protein, mouse); 0 (Hand2 protein, mouse); 0 (RNA, Messenger); E0399OZS9N (Cyclic AMP); EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases); EC 2.7.11.30 (Activin Receptors, Type I); EC 2.7.11.30 (Acvr1 protein, mouse)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170522
[Lr] Data última revisão:
170522
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170222
[St] Status:MEDLINE
[do] DOI:10.1530/JOE-16-0583


  10 / 1234 MEDLINE  
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[PMID]:28214889
[Au] Autor:Chen H; Liu C; Jiang H; Gao Y; Xu M; Wang J; Liu S; Fu Y; Sun X; Xu J; Zhang J; Dai L
[Ti] Título:Regulatory Role of miRNA-375 in Expression of BMP15/GDF9 Receptors and its Effect on Proliferation and Apoptosis of Bovine Cumulus Cells.
[So] Source:Cell Physiol Biochem;41(2):439-450, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Bone morphogenetic protein 15 (BMP15) and growth differentiation factor 9 (GDF9) are members of the transforming growth factor beta (TGF-ß) superfamily. Through autocrine and paracrine mechanisms, these two factors can regulate cell differentiation, proliferation, and other functions in the ovary locally. Furthermore, GDF9 and BMP15 play vital roles in follicular growth, atresia, ovulation, fertilization, reproduction, and maintenance. Numerous studies have demonstrated a synergy between BMP15 and GDF9. Studies in humans and mice have indicated that the synergy between BMP15 and GDF9 is primarily mediated by the bone morphogenetic protein type II receptor (BMPR2). The BMP15/GDF9 heterodimer needs to bind to the BMPR2-ALK4/5/7-ALK6 receptor complex to activate the SMAD2/3 signaling pathway. However, it is not clear which genes mediate and regulate the effects of the BMP15/GDF9 proteins on bovine cumulus cells (CCs). METHODS: Our earlier study showed that BMPR2 is a gene that is directly targeted and regulated by miR-375. Therefore, we designed and synthesized an miR-375 mimics/inhibitor and regulated BMPR2 expression in bovine CCs by the overexpression or inhibition of miR-375. After the overexpression or inhibition of miR-375, the apoptosis rate of bovine CCs was measured by flow cytometry; changes in critical gene expression were measured by RT-qPCR and western blot assays; and the proliferation of bovine CCs was measured by CCK-8 assay. RESULTS: In bovine CCs, the overexpression of miR-375 resulted in decreased BMPR2 and ALK7 expression, whereas the inhibition of miR-375 caused increased BMPR2 and ALK7 expression. The overexpression of miR-375 attenuated the proliferation ability and significantly increased the apoptosis rate of bovine CCs, whereas the inhibition of miR-375 did not significantly change the proliferation ability or apoptosis rate. CONCLUSIONS: BMPR2, a target of miR-375, is regulated by this molecule, thereby affecting expression of BMP15/GDF9 receptors, and the proliferation and apoptosis of bovine CCs.
[Mh] Termos MeSH primário: Proteína Morfogenética Óssea 15/metabolismo
Fator 9 de Diferenciação de Crescimento/metabolismo
MicroRNAs/metabolismo
[Mh] Termos MeSH secundário: Receptores de Ativinas Tipo I/genética
Receptores de Ativinas Tipo I/metabolismo
Animais
Antagomirs/metabolismo
Apoptose
Receptores de Proteínas Morfogenéticas Ósseas Tipo II/antagonistas & inibidores
Receptores de Proteínas Morfogenéticas Ósseas Tipo II/genética
Receptores de Proteínas Morfogenéticas Ósseas Tipo II/metabolismo
Bovinos
Proliferação Celular
Sobrevivência Celular
Células Cultivadas
Células do Cúmulo/citologia
Células do Cúmulo/metabolismo
Feminino
MicroRNAs/antagonistas & inibidores
MicroRNAs/genética
Folículo Ovariano/citologia
Proteínas Proto-Oncogênicas c-bcl-2/genética
Proteínas Proto-Oncogênicas c-bcl-2/metabolismo
Interferência de RNA
RNA Mensageiro/metabolismo
RNA Interferente Pequeno/metabolismo
Proteína X Associada a bcl-2/genética
Proteína X Associada a bcl-2/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antagomirs); 0 (Bone Morphogenetic Protein 15); 0 (Growth Differentiation Factor 9); 0 (MicroRNAs); 0 (Proto-Oncogene Proteins c-bcl-2); 0 (RNA, Messenger); 0 (RNA, Small Interfering); 0 (bcl-2-Associated X Protein); EC 2.7.11.30 (Activin Receptors, Type I); EC 2.7.11.30 (Bone Morphogenetic Protein Receptors, Type II)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170606
[Lr] Data última revisão:
170606
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170220
[St] Status:MEDLINE
[do] DOI:10.1159/000456597



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