PMID- 37635482
OWN - NLM
STAT- MEDLINE
DCOM- 20231102
LR  - 20231102
IS  - 0304-4920 (Print)
IS  - 0304-4920 (Linking)
VI  - 66
IP  - 4
DP  - 2023 Jul-Aug
TI  - Ring-finger protein 5 attenuates oxygen-glucose deprivation and 
      reperfusion-induced mitochondrial dysfunction and inflammation in cardiomyocytes 
      by inhibiting the S100A8/MYD88/NF-kappaB axis.
PG  - 228-238
LID - 10.4103/cjop.CJOP-D-22-00140 [doi]
AB  - Mitochondrial dysfunction is closely intertwined with the progression of heart 
      failure (HF). Ring-finger protein 5 (RNF5) is an E3 ubiquitin ligase, whose 
      deletion induces the enhanced S100A8 expression. S100A8 regulates the 
      mitochondrial dysfunction and S100A8/myeloid differentiation factor 88 
      (MYD88)/nuclear factor-kappa B (NF-kappaB) pathway promotes an inflammatory response; 
      however, whether RNF5 modulated mitochondrial dysregulation and inflammation 
      through the S100A8/MYD88/NF-kappaB axis remains unknown. Here, H9c2 cells were 
      stimulated with oxygen-glucose deprivation/reperfusion (OGD/R) to build a HF 
      model in vitro. RNF5 level was assessed in gene expression omnibus database and 
      in OGD/R-induced H9c2 cells with reverse transcriptase quantitative polymerase 
      chain reaction and western blot. The RNF5 level was overexpressed via 
      transfecting RNF5 overexpression plasmids into H9c2 cells. The role and mechanism 
      of RNF5 in OGD/R-elicited H9c2 cells were determined by 
      3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide, spectrophotometry, 
      flow cytometry, mitochondrial membrane potential (MMP) measurement, enzyme-linked 
      immunosorbent assay and western blot assays. The RNF5 expression was 
      downregulated both in silico and in OGD/R-stimulated H9c2 cells. OGD/R treatment 
      caused a decrease in the cell viability, the MMP level, and the translational 
      expression of mito-cyt-c and NF-kappaB-cyto, and an elevation in the concentrations 
      of lactate dehydrogenase and creatine kinase myocardial band, the apoptosis rate, 
      the inflammatory factor release, and the relative protein expression of 
      cyto-cyt-c, S100A8, MYD88 and NF-kappaB-nuc in H9c2 cells. Upregulation of RNF5 
      reversed these indicators in OGD/R-stimulated H9c2 cells. Altogether, based on 
      these outcomes, we concluded that RNF5 impeded mitochondrial dysfunction and 
      inflammation through attenuating the S100A8/MYD88/NF-kappaB axis in OGD/R-stimulated 
      H9c2 cells.
FAU - Chen, Xuesi
AU  - Chen X
AD  - Department of Cardiovascular, The Affiliated People's Hospital of Ningbo 
      University, Ningbo, Zhejiang, China.
FAU - Wu, Yingjie
AU  - Wu Y
AD  - Department of Cardiovascular, The Affiliated People's Hospital of Ningbo 
      University, Ningbo, Zhejiang, China.
FAU - Bao, Yingchun
AU  - Bao Y
AD  - Department of Cardiovascular, The Affiliated People's Hospital of Ningbo 
      University, Ningbo, Zhejiang, China.
LA  - eng
PT  - Journal Article
PL  - India
TA  - Chin J Physiol
JT  - The Chinese journal of physiology
JID - 7804502
RN  - 0 (NF-kappa B)
RN  - S88TT14065 (Oxygen)
RN  - 0 (Myeloid Differentiation Factor 88)
RN  - IY9XDZ35W2 (Glucose)
RN  - EC 2.3.2.27 (Ubiquitin-Protein Ligases)
SB  - IM
MH  - Humans
MH  - *NF-kappa B/metabolism
MH  - *Oxygen/metabolism
MH  - Myeloid Differentiation Factor 88/metabolism
MH  - Signal Transduction
MH  - Myocytes, Cardiac/metabolism
MH  - Glucose/metabolism
MH  - Apoptosis
MH  - Reperfusion
MH  - Ubiquitin-Protein Ligases/genetics/metabolism
MH  - Mitochondria
MH  - Inflammation
OTO - NOTNLM
OT  - Heart failure
OT  - S100A8/MYD88/NF-kappaB axis
OT  - inflammation
OT  - mitochondrial dysfunction
OT  - ring-finger protein 5
COIS- None
EDAT- 2023/08/28 06:42
MHDA- 2023/08/28 06:43
CRDT- 2023/08/28 03:10
PHST- 2023/08/28 06:43 [medline]
PHST- 2023/08/28 06:42 [pubmed]
PHST- 2023/08/28 03:10 [entrez]
AID - ChinJPhysiol_2023_66_4_228_379840 [pii]
AID - 10.4103/cjop.CJOP-D-22-00140 [doi]
PST - ppublish
SO  - Chin J Physiol. 2023 Jul-Aug;66(4):228-238. doi: 10.4103/cjop.CJOP-D-22-00140.