About: Overexpression of PTEN suppresses lipopolysaccharide-induced lung fibroblast proliferation, differentiation and collagen secretion through inhibition of the PI3-K-Akt-GSK3beta pathway

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About: Overexpression of PTEN suppresses lipopolysaccharide-induced lung fibroblast proliferation, differentiation and collagen secretion through inhibition of the PI3-K-Akt-GSK3beta pathway Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Overexpression of PTEN suppresses lipopolysaccharide-induced lung fibroblast proliferation, differentiation and collagen secretion through inhibition of the PI3-K-Akt-GSK3beta pathway
Creator	Li, Wen Gao, Yuan Chen, Yongming Deng, Yuxiao Ding, Jia He, Zhengyu Wang, Xiangrui Xing, Shunpeng Zhao, Xianyuan
Source	PMC
abstract	BACKGROUND: Abnormal and uncontrolled proliferation of lung fibroblasts may contribute to pulmonary fibrosis. Lipopolysaccharide (LPS) can induce fibroblast proliferation and differentiation through activation of phosphoinositide3-Kinase (PI3-K) pathway. However, the detail mechanism by which LPS contributes to the development of lung fibrosis is not clearly understood. To investigate the role of phosphatase and tensin homolog (PTEN), a PI3-K pathway suppressor, on LPS-induced lung fibroblast proliferation, differentiation, collagen secretion and activation of PI3-K, we transfected PTEN overexpression lentivirus into cultured mouse lung fibroblasts with or without LPS treatment to evaluate proliferation by MTT and Flow cytometry assays. Expression of PTEN, alpha-smooth muscle actin (alpha-SMA), glycogen synthase kinase 3 beta (GSK3beta) and phosphorylation of Akt were determined by Western-blot or real-time RT-PCR assays. The PTEN phosphorylation activity was measured by a malachite green-based assay. The content of C-terminal propeptide of type I procollagen (PICP) in cell culture supernatants was examined by ELISA. RESULTS: We found that overexpression of PTEN effectively increased expression and phosphatase activity of PTEN, and concomitantly inhibited LPS-induced fibroblast proliferation, differentiation and collagen secretion. Phosphorylation of Akt and GSK3beta protein expression levels in the LPS-induced PTEN overexpression transfected cells were significantly lower than those in the LPS-induced non-transfected cells, which can be reversed by the PTEN inhibitor, bpV(phen). CONCLUSIONS: Collectively, our results show that overexpression and induced phosphatase activity of PTEN inhibits LPS-induced lung fibroblast proliferation, differentiation and collagen secretion through inactivation of PI3-K-Akt-GSK3beta signaling pathways, which can be abrogated by a selective PTEN inhibitor. Thus, expression and phosphatase activity of PTEN could be a potential therapeutic target for LPS-induced pulmonary fibrosis. Compared with PTEN expression level, phosphatase activity of PTEN is more crucial in affecting lung fibroblast proliferation, differentiation and collagen secretion.
has issue date	2014-01-06(xsd:dateTime)
bibo:doi	10.1186/2045-3701-4-2
bibo:pmid	24387036
has license	cc-by
sha1sum (hex)	62f5dc6a3bf7eaffcf4a955b6358e27dd13d0fa5
schema:url	https://doi.org/10.1186/2045-3701-4-2
resource representing a document's title	Overexpression of PTEN suppresses lipopolysaccharide-induced lung fibroblast proliferation, differentiation and collagen secretion through inhibition of the PI3-K-Akt-GSK3beta pathway
has PubMed Central identifier	PMC3892003
has PubMed identifier	24387036
schema:publication	Cell Biosci
resource representing a document's body	covid:62f5dc6a3bf7eaffcf4a955b6358e27dd13d0fa5#body_text
is schema:about of	named entity 'PTEN' named entity 'MTT' named entity 'PTEN' named entity 'beta' named entity 'induce' named entity 'DEVELOPMENT' named entity 'INDUCED' named entity 'TREATMENT' named entity 'TO INVESTIGATE' named entity 'SMA' named entity 'PROPEPTIDE' named entity 'cell culture' named entity 'investigate' named entity 'type I' named entity 'phosphatase' named entity 'content' named entity 'transfected' named entity 'malachite' named entity 'differentiation' named entity 'Akt' named entity 'RT-PCR' named entity 'lung' named entity 'fibrosis' named entity 'phosphorylation' named entity 'procollagen' named entity 'PI3' named entity 'inhibition' named entity 'glycogen synthase kinase 3 beta' named entity 'Lipopolysaccharide' named entity 'Western-blot' named entity 'assay' named entity 'lung' named entity 'LPS' named entity 'MTT' named entity 'smooth muscle actin' named entity 'PI3-K' named entity 'phosphatase and tensin homolog' named entity 'secretion' named entity 'activation' named entity 'PI3-K' named entity 'PTEN' named entity 'collagen' named entity 'fibroblasts' named entity 'fibroblast' named entity 'lung' named entity 'fibroblasts' named entity 'procollagen' named entity 'supernatants' named entity 'propeptide' named entity 'PTEN' named entity 'LPS' named entity 'transfected' named entity 'PTEN' named entity 'LPS' named entity 'phosphorylation' named entity 'pulmonary fibrosis' named entity 'SUPPRESSOR' named entity 'KINASE' named entity 'real-time RT-PCR' named entity 'PI3-K' named entity 'PTEN' named entity 'lentivirus' named entity 'GSK3beta' named entity 'phosphorylation' named entity 'PTEN' named entity 'Akt' named entity 'fibroblast' named entity 'PROCOLLAGEN' named entity 'ACTIVITY' named entity 'UNCONTROLLED' named entity 'LUNG FIBROBLAST' named entity 'TYPE I' named entity 'DETERMINED BY'

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