Insulin Receptor Substrate p53 Ameliorates High-Glucose-Induced Activation of NF-κB and Impaired Mobility of HUVECs.

Diabetes-related macrovascular and microvascular complications lead to poor prognosis. Insulin receptor substrate p53 (IRSp53) is known to act as a substrate for the insulin receptor tyrosine kinase, but its role in endothelial dysfunction remains unclear. Human umbilical vein endothelial cells (HUV...

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Publicado en:BioMed Research International pp. 1 - 12
Autores principales: Liu, Fen, Chen, Yubin, Zhao, Shi, Li, Mei, Luo, Fanyan, Tang, Can-e
Formato: pictorial research tables/charts Journal Article
Publicado: Wiley-Blackwell 1/12/2021
Acceso en línea:Ver este registro en EBSCOhost
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      dt: 1/12/2021
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      pub: Wiley-Blackwell
      place: Malden, Massachusetts
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        10.1155/2021/3210586
        148071222
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        atl: Insulin Receptor Substrate p53 Ameliorates High-Glucose-Induced Activation of NF-κB and Impaired Mobility of HUVECs.
      aug:
        au:
          Liu, Fen
          Chen, Yubin
          Zhao, Shi
          Li, Mei
          Luo, Fanyan
          Tang, Can-e
        affil: The Institute of Medical Science Research, Xiangya Hospital, Central South University, Changsha, 410008 Hunan, China
      sug:
        subj:
          Insulin
          NF-kappa B
          Blood Glucose
          Umbilical Veins
          Endothelial Cells
          Animal Studies
          Rats
          Diabetes Mellitus
          Hyperglycemia
          Gene Expression
          RNA
      ab: Diabetes-related macrovascular and microvascular complications lead to poor prognosis. Insulin receptor substrate p53 (IRSp53) is known to act as a substrate for the insulin receptor tyrosine kinase, but its role in endothelial dysfunction remains unclear. Human umbilical vein endothelial cells (HUVECs) treated with D-glucose at different concentrations and a streptozocin-induced rat diabetes mellitus (DM) model were used to investigate the effects of hyperglycemia on the expression levels of IRSp53 and galectin-3 (gal-3) and the inflammatory state and mobility of HUVECs. Thereafter, IRSp53-overexpressing HUVECs and IRSp53-knockdown HUVECs were established using IRSp53-overexpressing lentivirus or IRSp53-siRNA to explore the role of IRSp53 in the HUVEC inflammatory state and HUVEC mobility. D-glucose at high concentration (HG) and hyperglycemia were found to induce downregulation of IRSp53 and upregulation of gal-3 in vitro and in vivo. Treatment with HG resulted in activation of NF-κB in HUVECs and impaired HUVEC mobility. Insulin restored HG-induced changes in the expression levels of IRSp53 and gal-3 in HUVECs and protected the cells from NF-κB activation and impaired mobility. Overexpression of IRSp53 inhibited the activation of NF-κB in HUVECs and strengthened HUVEC migration. Knockdown of IRSp53 facilitated the activation of NF-κB in HUVECs and decreased HUVEC migration. However, neither overexpression nor knockdown of IRSp53 altered the effects of insulin on HG-induced detrimental changes in HUVECs. HG and hyperglycemia resulted in downregulation of IRSp53 in vitro and in vivo. IRSp53 is concluded to inhibit the activation of NF-κB in HUVECs and to strengthen HUVEC migration.
      pubtype: Academic Journal
      doctype:
        pictorial
        research
        tables/charts
        Journal Article
      ougenre: Article
    language: English
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