About: The role of C/EBPβ phosphorylation in modulating membrane phospholipids repairing in LPS-induced human lung/bronchial epithelial cells

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About: The role of C/EBPβ phosphorylation in modulating membrane phospholipids repairing in LPS-induced human lung/bronchial epithelial cells Goto Sponge NotDistinct Permalink

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	The role of C/EBPβ phosphorylation in modulating membrane phospholipids repairing in LPS-induced human lung/bronchial epithelial cells
Creator	Xu, Yan Ouyang, Yufang Shu, Shiyu Xie, Ling
Source	Elsevier; Medline; PMC
abstract	Abstract Acute lung injury/acute respiratory distress syndrome (ALI/ARDS) is a common critical emergency with high mortality in clinical practice. The key mechanism of ALI/ARDS is that the excessive inflammatory response damages the integrity of alveolar and bronchial cell membrane and thus affects their basic function. Phospholipids are the main component of cell membranes. Phospholipase A2 (PLA2), which catalyzes the cleavage of membrane phospholipids, is the most important inflammatory mediator of ALI. However, clara cell secretory protein 1 (CCSP1), an endogenous PLA2 inhibitor can increase the self-defense of membrane phospholipids. Thus, CCSP1 up-regulation and PLA2 inhibition constitutes an effective method for ensuring the stability of membrane phospholipids and for the treatment of ALI/ARDS. In the present study, we developed an in vitro model of ALI via lipopolysaccharide (LPS) stimulation of a human bronchial epithelial cell line, BEAS-2B, and assessed the mRNA and protein levels of CCSP1 and PLA2 in the model cells. The results demonstrated LPS induction inhibited the transcription and protein expression of CCSP1, but only the protein level of membrane associated PLA2 was increased, suggesting that in the in vitro ALI model, abnormally regulated CCSP1 transcription plays a crucial role in the damage of cell membrane. To find out the reason that CCSP1 expression was decreased in the ALI model, we predicted, by means of bioinformatics, putative transcription factors which would bind to CCSP1 promoter, examined their background and expression, and found that a transcription factor, CCAAT/enhancer binding protein β (C/EBP β), was correlated with the transcription of CCSP1 in the in vitro ALI model, and its phosphorylation in the model was decreased. CHIP-PCR and luciferase reporter assay revealed that C/EBP β bound to CCSP1 promoter and facilitated its transcription. Therefore, we conclude that there is a C/EBP β/CCSP1/PLA2 pathway in the in vitro ALI model. The study of underlying mechanism show that the activity of C/EBP β depends on its phosphorylation:LPS stimulation reduced C/EBP β phosphorylation and suppressed the transcription of CCSP1 in BEAS-2B cells, which resulted in enhanced PLA2 and the consequent membrane damage. And further study shows that overexpression of CDK2(Cyclindependent kinase 2), promoted the phosphorylation of C/EBP β and inhibited PLA2 through the C/EBP β/CCSP1/PLA2 pathway, so as to attenuate membrane damage. The significance of this study lies in that artificial C/EBP β phosphorylation regulation may ease the membrane damage in ALI and improve membrane repair.
has issue date	2017-09-20(xsd:dateTime)
bibo:doi	10.1016/j.gene.2017.07.076
bibo:pmid	28760550
has license	els-covid
sha1sum (hex)	0b9249faf42463eb8673c8635f33c34c5d8a8bfb
schema:url	https://doi.org/10.1016/j.gene.2017.07.076
resource representing a document's title	The role of C/EBPβ phosphorylation in modulating membrane phospholipids repairing in LPS-induced human lung/bronchial epithelial cells
has PubMed Central identifier	PMC7125708
has PubMed identifier	28760550
schema:publication	Gene
resource representing a document's body	covid:0b9249faf42463eb8673c8635f33c34c5d8a8bfb#body_text
is schema:about of	named entity 'INDUCED' named entity 'critical' named entity 'artificial' named entity 'However' named entity 'damages' named entity 'protein' named entity 'And' named entity 'PLA2' named entity 'luciferase' named entity 'high' named entity 'correlated' named entity 'catalyzes' named entity 'C/EBPβ' named entity 'RESULTS' named entity 'LPS' named entity 'BRONCHIAL EPITHELIAL CELL LINE' named entity 'EASE' named entity 'INFLAMMATORY MEDIATOR' named entity 'FUNCTION' named entity 'MORTALITY' named entity 'PROTEIN ' named entity 'REVEALED' named entity 'BINDING PROTEIN' named entity 'TRANSCRIPTION' named entity 'ASSOCIATED' named entity 'REPAIR' named entity 'ROLE' named entity 'MEMBRANE' named entity 'HIGH' named entity 'PLAYS' named entity 'BACKGROUND' named entity 'METHOD' named entity 'PATHWAY' named entity 'ATTENUATE' covid:arg/0b9249faf42463eb8673c8635f33c34c5d8a8bfb named entity 'MODEL' named entity 'UP-REGULATION' named entity 'CELL MEMBRANE' named entity 'REGULATION' named entity 'MRNA' named entity 'MODEL OF' named entity 'HUMAN' named entity 'RESPIRATORY DISTRESS SYNDROME' named entity 'INHIBITION' named entity 'STABILITY' named entity 'ACUTE LUNG INJURY' named entity 'PLA2' named entity 'MECHANISM' named entity 'PRESENT' named entity 'EMERGENCY' named entity 'PHOSPHORYLATION' named entity 'UNDERLYING' named entity 'INTEGRITY OF' named entity 'TREATMENT' named entity 'BASIC' named entity 'EXPRESSION' named entity 'ENDOGENOUS' named entity 'DEFENSE' named entity 'CRITICAL' named entity 'INCREASE' named entity 'DEMONSTRATED' named entity 'THEIR' named entity 'INHIBITOR' named entity 'REPORTER ASSAY' named entity 'STUDY' named entity 'SUPPRESSED' named entity 'BEAS-2B' named entity 'SELF' named entity 'LPS' named entity 'MODULATING' named entity 'ASSESSED' named entity 'BIND' named entity 'KEY' named entity 'REDUCED' named entity 'MAIN' named entity 'CLINICAL PRACTICE' named entity 'CORRELATED' named entity 'IN VITRO'

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