Altered Expression Patterns of the Sumoylation Enzymes E1, E2 and E3 Are Associated with Glucose Oxidase- and UVA-Induced Cataractogenesis

Nie, Qian; Gong, Xiang; Xiang, Jia-Wen; Xiao, Yuan; Xie, Jianhui; Yang, Lan; Chen, Huimin; Gan, Yuwen; Chen, Zhigang; Li, David Wan‐Cheng

doi:10.2174/1566524019666190111152324

Cited by 3 publications

(1 citation statement)

References 71 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Small ubiquitin-like modifier (SUMO) modification is a reversible ATP-dependent post-translational modification process similar to ubiquitination [11,12]. SUMO protein is a typical representative of ubiquitin-like modified protein subfamily, and SUMO modification is one of the conservative post-translational modifications in eukaryotes [13]. By now, four SUMO isomers have been found in mammalian cells, namely SUMO1, SUMO2, SUMO3 and SUMO4 [14,15].…”

Section: Introductionmentioning

confidence: 99%

SUMO2/3 participates in regulating the protective effect of propofol on human umbilical vein endothelial cells

Liu

Wang

Chen

2019

Biotechnology & Biotechnological Equipment

View full text Add to dashboard Cite

The present study investigated the role and mechanism of SUMO2/3 in the protection of vascular endothelial cells by propofol. An ischemia-reperfusion (I/R) injury model of human umbilical vein endothelial cells (HUVECs) was constructed. After treatment with propofol, we determined the expression of SUMO2/3 proteins by Western blotting, cell proliferation by CCK-8 assay, cell migration by Transwell assay and apoptosis by flow cytometry. After interference of SUMO2/3, the biological functions of HUVECs were observed. Using Western blotting and laser scanning confocal microscopy, the autophagy of HUVECs was examined. Using immunoprecipitation, the SUMO modification site of Beclin1 was examined. The results showed that I/R injury decreased the proliferation and migration and promoted the apoptosis of HUVECs, and propofol restored the normal biological functions to HUVECs. I/R injury inhibited the expression of SUMO2/3 in HUVECs, and propofol increased the expression of SUMO2/3 in HUVECs. Interference of SUMO2/ 3 expression suppressed the proliferation and migration, and promoted the apoptosis of HUVECs. Propofol exerted its protective effect on HUVECs via autophagy mediated by SUMO2/3 proteins. Beclin1 was modified by SUMO2/3 at the K26 site. SUMO modification of the K26 site in Beclin1 was involved in the regulation of autophagy of HUVECs, and K26R Beclin1 had reduced effect in activating autophagy of HUVECs compared with wild-type Beclin1. These results demonstrate that SUMO2/3 participates in regulating the protective effect of propofol on HUVECs. SUMO2/3 activates the autophagy activity of cells by modifying the K26 site of Beclin1, thus inhibiting I/R injury to vascular endothelial cells.

show abstract

Section: Introductionmentioning

confidence: 99%

SUMO2/3 participates in regulating the protective effect of propofol on human umbilical vein endothelial cells

Liu

Wang

Chen

2019

Biotechnology & Biotechnological Equipment

View full text Add to dashboard Cite

show abstract

The biomedical application of inorganic metal nanoparticles in aging and aging-associated diseases

Meng,

Zhang,

Liu

et al. 2024

Journal of Advanced Research

View full text Add to dashboard Cite

Glucose Oxidase- and UVA-Induced Changes in the Expression Patterns of Seven De-sumoylation Enzymes (SENPs) Are Associated with Cataract Development

Xiang

Xiao

Gan

et al. 2019

CMM

View full text Add to dashboard Cite

Objective: It has been well established that sumoylation acts as an important regulatory mechanism that controls many different cellular processes. We and others have shown that sumoylation plays an indispensable role during mouse eye development. Whether sumoylation is implicated in ocular pathogenesis remains to be further studied. In the present study, we have examined the expression patterns of the de-sumoylation enzymes (SENPs) in the in vitro cataract models induced by glucose oxidase and UVA irradiation. Methods: Four-week-old C57BL/6J mice were used in our experiments. Lenses were carefully dissected out from mouse eyes and cultured in M199 medium for 12 hours. Transparent lenses (without surgical damage) were selected for experimentation. The lenses were exposed to UVA for 60 min or treated with 20 mU/mL glucose oxidase (GO) to induce cataract formation. The mRNA levels were analyzed with qRT-PCR. The protein levels were determined with western blot analysis and quantitated with Image J. Results: GO treatment and UVA irradiation can induce cataract formation in lens cultured in vitro. GO treatment significantly down-regulated the mRNA levels for SENPs from 50% to 85%; on the other hand, expression of seven SENP proteins under GO treatment appeared in 3 situations: upregulation for SENP1, 2 and 6; downregulation for SENP 5 and 8; and unchanged for SENP3 and 7. UVA irradiation upregulates the mRNAs for all seven SENPs; In contrast to the mRNA levels for 7 SENPs, the expression levels for 6 SENPs (SENP1-3, 5-6 and 8) appeared down-regulated from 10% to 50%, and only SENP7 was slightly upregulated. Conclusion: Our results for the first time established the differentiation expression patterns of 7 de-sumoylation enzymes (SENPs) under treatment by GO or UVA, which provide preliminary data to link sumoylation to stress-induced cataractogenesis.

show abstract

Altered Expression Patterns of the Sumoylation Enzymes E1, E2 and E3 Are Associated with Glucose Oxidase- and UVA-Induced Cataractogenesis

Cited by 3 publications

References 71 publications

SUMO2/3 participates in regulating the protective effect of propofol on human umbilical vein endothelial cells

SUMO2/3 participates in regulating the protective effect of propofol on human umbilical vein endothelial cells

The biomedical application of inorganic metal nanoparticles in aging and aging-associated diseases

Glucose Oxidase- and UVA-Induced Changes in the Expression Patterns of Seven De-sumoylation Enzymes (SENPs) Are Associated with Cataract Development

Contact Info

Product

Resources

About