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Your search keyword '"Prolyl 3‐hydroxylase 2"' showing total 2 results
Start Over Descriptor "Prolyl 3‐hydroxylase 2" Topic neovascularization, pathologic
2 results on '"Prolyl 3‐hydroxylase 2"'

1. Prolyl 3-Hydroxylase 2 Is a Molecular Player of Angiogenesis.

Author

Pignata P, Apicella I, Cicatiello V, Puglisi C, Magliacane Trotta S, Sanges R, Tarallo V, and De Falco S

Subjects
Animals, Choroidal Neovascularization diagnostic imaging, Choroidal Neovascularization etiology, Choroidal Neovascularization metabolism, Choroidal Neovascularization pathology, Collagen Type IV genetics, Collagen Type IV metabolism, Disease Models, Animal, Fluorescent Antibody Technique, Gene Expression Regulation, Human Umbilical Vein Endothelial Cells metabolism, Humans, Mice, Protein Binding, Signal Transduction, Vascular Endothelial Growth Factor A genetics, Vascular Endothelial Growth Factor A metabolism, p38 Mitogen-Activated Protein Kinases metabolism, Neovascularization, Pathologic genetics, Neovascularization, Pathologic metabolism, Neovascularization, Physiologic, Procollagen-Proline Dioxygenase genetics, Procollagen-Proline Dioxygenase metabolism, Vascular Endothelial Growth Factor Receptor-2 metabolism
Abstract

Prolyl 3-hydroxylase 2 ( P3H2 ) catalyzes the post-translational formation of 3-hydroxyproline on collagens, mainly on type IV. Its activity has never been directly associated to angiogenesis. Here, we identified P3H2 gene through a deep-sequencing transcriptome analysis of human umbilical vein endothelial cells (HUVECs) stimulated with vascular endothelial growth factor A (VEGF-A). Differently from many previous studies we carried out the stimulation not on starved HUVECs, but on cells grown to maintain the best condition for their in vitro survival and propagation. We showed that P3H2 is induced by VEGF-A in two primary human endothelial cell lines and that its transcription is modulated by VEGF-A/VEGF receptor 2 (VEGFR-2) signaling pathway through p38 mitogen-activated protein kinase (MAPK). Then, we demonstrated that P3H2 , through its activity on type IV Collagen, is essential for angiogenesis properties of endothelial cells in vitro by performing experiments of gain- and loss-of-function. Immunofluorescence studies showed that the overexpression of P3H2 induced a more condensed status of Collagen IV, accompanied by an alignment of the cells along the Collagen IV bundles, so towards an evident pro-angiogenic status. Finally, we found that P3H2 knockdown prevents pathological angiogenesis in vivo, in the model of laser-induced choroid neovascularization. Together these findings reveal that P3H2 is a new molecular player involved in new vessels formation and could be considered as a potential target for anti-angiogenesis therapy.

Published
2021
Full Text
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2. Prolyl 3-Hydroxylase 2 Is a Molecular Player of Angiogenesis

Author

Valeria Tarallo, Sandro De Falco, Remo Sanges, Valeria Cicatiello, Caterina Puglisi, Ivana Apicella, Paola Pignata, and Sara Magliacane Trotta

Subjects
MAPK/ERK pathway, Angiogenesis, Fluorescent Antibody Technique, p38 Mitogen-Activated Protein Kinases, Umbilical vein, lcsh:Chemistry, Neovascularization, Mice, Type IV collagen, angiogenesis, Settore BIO/13 - Biologia Applicata, lcsh:QH301-705.5, Spectroscopy, Prolyl 3‐hydroxylase 2, Collagen IV, Neovascularization, Pathologic, Chemistry, prolyl 3-hydroxylase 2, General Medicine, Computer Science Applications, Cell biology, Endothelial stem cell, Vascular endothelial growth factor A, medicine.symptom, Signal transduction, Protein Binding, Signal Transduction, Collagen Type IV, Procollagen-Proline Dioxygenase, Neovascularization, Physiologic, choroidal neovascularization, Catalysis, Article, Inorganic Chemistry, Human Umbilical Vein Endothelial Cells, medicine, Animals, Humans, Physical and Theoretical Chemistry, Physiologic, Molecular Biology, age-related macular degeneration, Age‐related macular degeneration, Pathologic, Animal, Organic Chemistry, vascular endothelial growth factor A, Vascular Endothelial Growth Factor Receptor-2, Disease Models, Animal, lcsh:Biology (General), lcsh:QD1-999, Gene Expression Regulation, angiogenesisprolyl 3-hydroxylase 2Collagen IVvascular endothelial growth factor Achoroidal neovascularizationage-related macular degeneration, Disease Models
Abstract

Prolyl 3-hydroxylase 2 (P3H2) catalyzes the post-translational formation of 3-hydroxyproline on collagens, mainly on type IV. Its activity has never been directly associated to angiogenesis. Here, we identified P3H2 gene through a deep-sequencing transcriptome analysis of human umbilical vein endothelial cells (HUVECs) stimulated with vascular endothelial growth factor A (VEGF-A). Differently from many previous studies we carried out the stimulation not on starved HUVECs, but on cells grown to maintain the best condition for their in vitro survival and propagation. We showed that P3H2 is induced by VEGF-A in two primary human endothelial cell lines and that its transcription is modulated by VEGF-A/VEGF receptor 2 (VEGFR-2) signaling pathway through p38 mitogen-activated protein kinase (MAPK). Then, we demonstrated that P3H2, through its activity on type IV Collagen, is essential for angiogenesis properties of endothelial cells in vitro by performing experiments of gain- and loss-of-function. Immunofluorescence studies showed that the overexpression of P3H2 induced a more condensed status of Collagen IV, accompanied by an alignment of the cells along the Collagen IV bundles, so towards an evident pro-angiogenic status. Finally, we found that P3H2 knockdown prevents pathological angiogenesis in vivo, in the model of laser-induced choroid neovascularization. Together these findings reveal that P3H2 is a new molecular player involved in new vessels formation and could be considered as a potential target for anti-angiogenesis therapy.

Published
2021
Full Text
View/download PDF

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