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Placental growth factor gene silencing mitigates the epithelial‑to‑mesenchymal transition via the p38 MAPK pathway in rats with hyperoxia‑induced lung injury.

08:00 EDT 30th October 2019 | BioPortfolio

Summary of "Placental growth factor gene silencing mitigates the epithelial‑to‑mesenchymal transition via the p38 MAPK pathway in rats with hyperoxia‑induced lung injury."

Hyperoxia may cause pulmonary fibrosis in neonates and is characterized by the epithelial‑to‑mesenchymal transition (EMT) of alveolar epithelial cells. The placental growth factor (PLGF) gene is a member of the vascular endothelial growth factor family and is highly expressed in lung tissues that have been exposed to hyperoxia. The aim of the present study was to assess the role of PLGF in the EMT of lung tissue. Lung tissue exhibiting low PLGF expression was obtained by injecting rats exposed to hyperoxia with a PLGF‑silencing lentiviral plasmid. Western blot analysis and immunohistochemistry revealed that expression levels of the EMT‑related protein epithelial‑cadherin were increased, whereas its inhibitor protein zinc‑finger E‑box binding homeobox 2 was decreased in these rats. These data demonstrated that PLGF silencing may significantly mitigate hyperoxia‑induced EMT in rat lung tissue. Additionally, an increase in phosphorylated‑p38 MAPK protein expression indicated that PLGF may be able to regulate hyperoxia‑induced lung injury in rats via the p38 MAPK pathway.

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Name: Molecular medicine reports
ISSN: 1791-3004
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Medical and Biotech [MESH] Definitions

A 6-kDa polypeptide growth factor initially discovered in mouse submaxillary glands. Human epidermal growth factor was originally isolated from urine based on its ability to inhibit gastric secretion and called urogastrone. EPIDERMAL GROWTH FACTOR exerts a wide variety of biological effects including the promotion of proliferation and differentiation of mesenchymal and epithelial cells.

A fibroblast growth factor receptor that is found in two isoforms. One receptor isoform is found in the MESENCHYME and is activated by FIBROBLAST GROWTH FACTOR 2. A second isoform of fibroblast growth factor receptor 2 is found mainly in EPITHELIAL CELLS and is activated by FIBROBLAST GROWTH FACTOR 7 and FIBROBLAST GROWTH FACTOR 10. Mutation of the gene for fibroblast growth factor receptor 2 can result in APERT SYNDROME.

An angiogenic protein belonging to the Vascular Endothelial Growth Factor family of growth factors originally isolated and cloned from human placental cDNA library. There are four isoforms of PLGF 1-4 which result from alternative splicing. Placenta Growth Factor is secreted as a glycosylated homodimer which acts as a mitogen for endothelial cells, and its expression is markedly upregulated during hypoxia and in tissue inflammation and cancer.

A fibroblast growth factor that is a specific mitogen for EPITHELIAL CELLS. It binds a complex of HEPARAN SULFATE and FIBROBLAST GROWTH FACTOR RECEPTOR 2B.

A single-chain polypeptide growth factor that plays a significant role in the process of WOUND HEALING and is a potent inducer of PHYSIOLOGIC ANGIOGENESIS. Several different forms of the human protein exist ranging from 18-24 kDa in size due to the use of alternative start sites within the fgf-2 gene. It has a 55 percent amino acid residue identity to FIBROBLAST GROWTH FACTOR 1 and has potent heparin-binding activity. The growth factor is an extremely potent inducer of DNA synthesis in a variety of cell types from mesoderm and neuroectoderm lineages. It was originally named basic fibroblast growth factor based upon its chemical properties and to distinguish it from acidic fibroblast growth factor (FIBROBLAST GROWTH FACTOR 1).

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