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Key Laboratory of Molecular Epigenetics of Ministry of Education, Northeast Normal University, Changchun, China
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Key Laboratory of Molecular Epigenetics of Ministry of Education, Northeast Normal University, Changchun, China
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Key Laboratory of Molecular Epigenetics of Ministry of Education, Northeast Normal University, Changchun, China
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certain condition, bAT can develop from BAT as well ( Kreuger et al. 2006 ). As bAT can transform energy to heat as efficiently as BAT, understanding of development and regulatory mechanism of bAT is important in fighting obesity. VEGFB is a member of
Transgenic Research Center, Northeast Normal University, Changchun, Jilin, China
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, Chen et al. 2020 ). Since bAT can transform energy to heat as efficiently as BAT, understanding of the regulatory mechanism of transformation between WAT and bAT is important in body weight control and obesity prevention. VEGFB is a family member of
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Angiogenesis and vascular transformation are important processes in the normal development of the placenta. Vascular endothelial growth factor (VEGF) is a potent angiogenic growth factor and is thought to be important for placental development. Recently several new members of this family have been described. In this study we used in situ hybridisation to localise which cells in the placenta expressed mRNA for VEGF, placenta growth factor (PlGF), VEGF-B and VEGF-C. We were unable to find any message for either VEGF-B or VEGF-C in the placenta, suggesting that only low levels are produced which this method was unable to detect. The mRNA encoding VEGF was found to be produced by cells within the villous mesenchyme, decidual macrophages and decidual glands but, in contrast to our previous findings, not by trophoblast. The mRNA encoding PlGF was produced in large amounts by villous cytotrophoblast, syncytiotrophoblast and extravillous trophoblast. The mRNAs encoding VEGF and PlGF were thus not co-localised and it appears that there is unlikely to be any significant production of VEGF/PlGF heterodimer in the placenta.
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family is composed of VEGFA, VEGFB, VEGFC, VEGFD, and PGF (Placental Growth Factor, previously known as PlGF). VEGFA is the most studied family member and is critical for angiogenic processes ( Ferrara et al . 2003 ). Even the disruption of one allele
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growth and ulcer healing. Nature Medicine 5 1418 –1423. Laitinen M , Ristimaki A, Honkasalo M, Narko K, Paavonen K & Ritvos O 1997 Differential hormonal regulation of vascular endothelial growth factors VEGF, VEGF-B, and
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Department of Paediatrics, Department of Women's and Children's Health, Division of Endocrinology, Department of Tissue Regeneration, Department of Endocrinology and Metabolism, Leiden University Medical Center, 2300 ZA Leiden, The Netherlands
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chondrocytes and osteoblasts in different species including humans ( Gerber et al . 1999 , Carlevaro et al . 2000 , Garcia-Ramirez et al . 2000 , Haeusler et al . 2005 ). Human VEGF is present in six different proteins, VEGF-A, VEGF-B, VEGF-C, VEGF
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Department of Clinical Science and Education, Division of Drug Research, Center of Medical Image Science and Visualization, Department of Biochemistry and Molecular Biology, Södersjukhuset, Karolinska Institutet, SE-118 83 Stockholm, Sweden
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Department of Clinical Science and Education, Division of Drug Research, Center of Medical Image Science and Visualization, Department of Biochemistry and Molecular Biology, Södersjukhuset, Karolinska Institutet, SE-118 83 Stockholm, Sweden
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) Hagberg CE Mehlem A Falkevall A Muhl L Fam BC Ortsater H Scotney P Nyqvist D Samen E Lu L 2012 Targeting VEGF-B as a novel treatment for insulin resistance and type 2 diabetes . Nature 490 426 – 430 . ( doi:10.1038/nature
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Physiology and Biophysics, Arkansas Children's Nutrition Center, Departments of
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Physiology and Biophysics, Arkansas Children's Nutrition Center, Departments of
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Physiology and Biophysics, Arkansas Children's Nutrition Center, Departments of
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1.80 1.82 XM_224720 Arrdc2 Arrestin domain-containing 2 – 1.74 0.63 NM_053549 Vegfb Vascular endothelial growth factor B Angiogenesis 1.73 1.63 NM_130408 Cyp26a1 Cytochrome P450, family 26, subfamily A, polypeptide 1 Electron transport 1.59 1.88 XM
Istituto San Raffaele, Neurosurgical Department, Milano, Italy
Ludwig-Maximilians University, Neurosurgical Department, Munich, Germany
Klinikum Villingen-Schwenningen, Neurosurgical Department, Villingen-Schwenningen, Germany
Laboratorio de Fisiología y Biología Molecular, Departamento Ciencias Biológicas, FCEN-Universidad de Buenos Aires and CONICET, Buenos Aires, Argentina
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Istituto San Raffaele, Neurosurgical Department, Milano, Italy
Ludwig-Maximilians University, Neurosurgical Department, Munich, Germany
Klinikum Villingen-Schwenningen, Neurosurgical Department, Villingen-Schwenningen, Germany
Laboratorio de Fisiología y Biología Molecular, Departamento Ciencias Biológicas, FCEN-Universidad de Buenos Aires and CONICET, Buenos Aires, Argentina
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Istituto San Raffaele, Neurosurgical Department, Milano, Italy
Ludwig-Maximilians University, Neurosurgical Department, Munich, Germany
Klinikum Villingen-Schwenningen, Neurosurgical Department, Villingen-Schwenningen, Germany
Laboratorio de Fisiología y Biología Molecular, Departamento Ciencias Biológicas, FCEN-Universidad de Buenos Aires and CONICET, Buenos Aires, Argentina
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Istituto San Raffaele, Neurosurgical Department, Milano, Italy
Ludwig-Maximilians University, Neurosurgical Department, Munich, Germany
Klinikum Villingen-Schwenningen, Neurosurgical Department, Villingen-Schwenningen, Germany
Laboratorio de Fisiología y Biología Molecular, Departamento Ciencias Biológicas, FCEN-Universidad de Buenos Aires and CONICET, Buenos Aires, Argentina
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Istituto San Raffaele, Neurosurgical Department, Milano, Italy
Ludwig-Maximilians University, Neurosurgical Department, Munich, Germany
Klinikum Villingen-Schwenningen, Neurosurgical Department, Villingen-Schwenningen, Germany
Laboratorio de Fisiología y Biología Molecular, Departamento Ciencias Biológicas, FCEN-Universidad de Buenos Aires and CONICET, Buenos Aires, Argentina
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Istituto San Raffaele, Neurosurgical Department, Milano, Italy
Ludwig-Maximilians University, Neurosurgical Department, Munich, Germany
Klinikum Villingen-Schwenningen, Neurosurgical Department, Villingen-Schwenningen, Germany
Laboratorio de Fisiología y Biología Molecular, Departamento Ciencias Biológicas, FCEN-Universidad de Buenos Aires and CONICET, Buenos Aires, Argentina
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Istituto San Raffaele, Neurosurgical Department, Milano, Italy
Ludwig-Maximilians University, Neurosurgical Department, Munich, Germany
Klinikum Villingen-Schwenningen, Neurosurgical Department, Villingen-Schwenningen, Germany
Laboratorio de Fisiología y Biología Molecular, Departamento Ciencias Biológicas, FCEN-Universidad de Buenos Aires and CONICET, Buenos Aires, Argentina
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Istituto San Raffaele, Neurosurgical Department, Milano, Italy
Ludwig-Maximilians University, Neurosurgical Department, Munich, Germany
Klinikum Villingen-Schwenningen, Neurosurgical Department, Villingen-Schwenningen, Germany
Laboratorio de Fisiología y Biología Molecular, Departamento Ciencias Biológicas, FCEN-Universidad de Buenos Aires and CONICET, Buenos Aires, Argentina
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of the most important angiogenetic factors stimulating endothelial cell proliferation, motility and permeability ( Ferrara 2004 , Tammela et al. 2005 ). The VEGF protein family further comprises VEGF-B, -C, -D, -E and placenta growth factor (PlGF
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Department of Applied Biology, Department of Anatomy and Neuroscience, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan
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affinity for VEGFA and VEGFB and an inhibitory effect on proliferation of endothelial cells ( Keyt et al . 1996 , Fong et al . 1999 ). Our previous study has demonstrated continuous proliferation of endothelial cells and the expression of angiogenesis