Correction to: TPTEP1 suppresses high glucose‑induced dysfunction in retinal vascular endothelial cells by interacting with STAT3 and targeting VEGFA

Sun, Xiaoping; Lu, Yuebing; Lei, Tao

doi:10.1007/s00592-022-01979-9

Cited by 1 publication

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“…Activated T cells release many inflammatory cytokines into the blood, and these cytokines participate in the pathogenesis of KD ( 11 ). The activation of STAT3 can promote the activation and transcription of VEGF ( 41 , 42 ). The upregulation of STAT3 can increase the expression of Th17/Tregs.…”

Section: Discussionmentioning

confidence: 99%

Ubiquitin ligase MDM2 mediates endothelial inflammation in Kawasaki disease vasculitis development

Xu,

Qian,

Zhu

et al. 2024

Transl Pediatr

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Background Kawasaki disease (KD) often complicates coronary artery lesions (CALs). Despite the established significance of STAT3 signaling during the acute phase of KD and signal transducer and activator of transcription 3 (STAT3) signaling being closely related to CALs, it remains unknown whether and how STAT3 was regulated by ubiquitination during KD pathogenesis. Methods Bioinformatics and immunoprecipitation assays were conducted, and an E3 ligase, murine double minute 2 (MDM2) was identified as the ubiquitin ligase of STAT3. The blood samples from KD patients before and after intravenous immunoglobulin (IVIG) treatment were utilized to analyze the expression level of MDM2. Human coronary artery endothelial cells (HCAECs) and a mouse model were used to study the mechanisms of MDM2-STAT3 signaling during KD pathogenesis. Results The MDM2 expression level decreased while the STAT3 level and vascular endothelial growth factor A (VEGFA) level increased in KD patients with CALs and the KD mouse model. Mechanistically, MDM2 colocalized with STAT3 in HCAECs and the coronary vessels of the KD mouse model. Knocking down MDM2 caused an increased level of STAT3 protein in HCAECs, whereas MDM2 overexpression upregulated the ubiquitination level of STAT3 protein, hence leading to significantly decreased turnover of STAT3 and VEGFA. Conclusions MDM2 functions as a negative regulator of STAT3 signaling by promoting its ubiquitination during KD pathogenesis, thus providing a potential intervention target for KD therapy.

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Section: Discussionmentioning

confidence: 99%