OTUB1 Recruits Tumor Infiltrating Lymphocytes and Is a Prognostic Marker in Digestive Cancers

Zhang, Wenhao; Qiu, Wenlong

doi:10.3389/fmolb.2020.00212

Cited by 11 publications

(9 citation statements)

References 55 publications

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“…OTUB1, known as a deubiquitinases, can protect the protein from degradation and belongs to the ovarian cancer proteases family. Zhang W et al found that OTUB1 performed as a molecular indicator of poor prognosis in digestive cancers, regulated the in ltration of tumor immunocytes, and exerted a signi cant in uence on apoptosis and autophagy [15]. Our study found that LPS reduced the expression of OTUB1, which may act directly with Na, K-ATPase α1.…”

Section: Discussionsupporting

confidence: 56%

Identification of Different Proteins Binding to Na, K-ATPase α1 in LPS-Induced ARDS Cell Model by Proteomic Analysis

Wen

Long

Zhang

et al. 2022

Preprint

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Background: Acute respiratory distress syndrome (ARDS) is characterized by refractory hypoxemia caused by accumulation of pulmonary fluid, which is related to inflammatory cell infiltration, impaired tight junction of pulmonary epithelium and impaired Na, K-ATPase function, especially Na, K-ATPase α1 subunit. Up until now, the pathogenic mechanism at the level of protein during lipopolysaccharide- (LPS-) induced ARDS remains unclear.Methods: Using an unbiased, discovery and quantitative proteomic approach, we discovered the differentially expressed proteins binding to Na, K-ATPase α1 between LPS-A549 cells and Control-A549 cells. These Na, K-ATPase α1 interacting proteins were screened by co-immunoprecipitation (Co-IP) technology. Among them, some of the differentially expressed proteins with significant performance were identified and quantified by liquid chromatography-tandem mass spectrometry (LC-MS/MS). The protein interaction network was constructed by the related Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis. Several differentially expressed proteins were validated by Western blot.Results: Of identified 1598 proteins, 89 were differentially expressed proteins between LPS-A549 cells and Control-A549 cells. Intriguingly, protein-protein interaction network showed that there were 244 significantly enriched co-expression among 60 proteins in the group control-A549. while the group LPS-A549 showed 43 significant enriched interactions among 29 proteins. The related GO and KEGG analysis found evident phenomena of ubiquitination and deubiquitination, as well as the pathways related to autophagy. Among proteins with rich abundance, there were several intriguing ones, including the deubiquitinase (OTUB1), the tight junction protein zonula occludens-1 (ZO-1), the scaffold protein in CUL4B-RING ubiquitin ligase (CRL4B) complexes (CUL4B) and the autophagy-related protein sequestosome-1 (SQSTM1).Conclusions: In conclusion, our proteomic approach revealed targets related to the occurrence and development of ARDS, being the first study to investigate significant differences in Na, K-ATPase α1 interacting proteins between LPS-induced ARDS cell model and control-A549 cell. These proteins may help the clinical diagnosis and facilitate the personalized treatment of ARDS.

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Section: Discussionsupporting

confidence: 56%

Identification of Different Proteins Binding to Na, K-ATPase α1 in LPS-Induced ARDS Cell Model by Proteomic Analysis

Wen

Long

Zhang

et al. 2022

Preprint

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“…48 Zhang W et al found that OTUB1 performed as a molecular indicator of poor prognosis in digestive cancers, regulated the in ltration of tumor immunocytes, and exerted a signi cant in uence on apoptosis and autophagy. 49 Our study found that LPS reduced the expression of OTUB1, which may act directly with Na, K-ATPase α1. Therefore, LPS may decrease the level of Na, K-ATPase α1 to lessen its protection by decreasing OTUB1.…”

Section: Discussionmentioning

confidence: 46%

Identification of Different Proteins Binding to Na, K-ATPase α1 in Lipopolysaccharide-Induced Acute Respiratory Distress Syndrome Cell Model by Proteomic Analysis

Wen

Zhang

Huang

et al. 2021

Preprint

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Acute respiratory distress syndrome (ARDS) is characterized by refractory hypoxemia caused by accumulation of pulmonary fluid, which is related to inflammatory cell infiltration, impaired tight junction of pulmonary epithelium and impaired Na, K-ATPase function, especially Na, K-ATPase α1 subunit. Up until now, the pathogenic mechanism at the level of protein during lipopolysaccharide- (LPS-) induced ARDS remains unclear. Using an unbiased, discovery and quantitative proteomic approach, the discovery of differentially expressed proteins binding to Na, K-ATPase α1 between LPS-induced A549 cell and control-A549 group is of particular interest for the current study. These proteins may help the clinical diagnosis and facilitate the personalized treatment of ARDS. We screened these Na, K-ATPase α1 interacting proteins, carried out the related Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis, and found evident phenomena of ubiquitination and deubiquitination, as well as the pathways related to autophagy. We also chose some of the differentiated expressing proteins with significant performance for further verification by liquid chromatography-tandem mass spectrometry (LC-MS/MS). Among proteins with rich abundance, there were several intriguing ones, including the deubiquitinase (OTUB1), the tight junction protein zonula occludens-1 (ZO-1), the scaffold protein in CUL4B-RING ubiquitin ligase (CRL4B) complexes (CUL4B) and the autophagy-related protein sequestosome-1 (SQSTM1). Protein-protein interaction network showed that there were 244 significantly enriched co-expression among 60 proteins in the group control-A549. while the group LPS-A549 showed 43 significant enriched interactions among 29 proteins. In conclusion, our quantitative discovery-based proteomic approach identified commonalities, and revealed targets related to the occurrence and development of ARDS, being the first study to investigate significant differences in Na, K-ATPase α1 interacting proteins between LPS-induced ARDS cell model and control-A549 cell.

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“…OTUB1, known as a deubiquitinases, can protect the protein from degradation and belongs to the ovarian cancer proteases family. Zhang W et al found that OTUB1 performed as a molecular indicator of poor prognosis in digestive cancers, regulated the infiltration of tumor immunocytes, and exerted a significant influence on apoptosis and autophagy [ 15 ]. Our study found that LPS reduced the expression of OTUB1, which may act directly with Na, K-ATPase α1.…”

Section: Discussionmentioning

confidence: 99%

Identification of different proteins binding to Na, K-ATPase α1 in LPS-induced ARDS cell model by proteomic analysis

et al. 2022

View full text Add to dashboard Cite

Background Acute respiratory distress syndrome (ARDS) is characterized by refractory hypoxemia caused by accumulation of pulmonary fluid, which is related to inflammatory cell infiltration, impaired tight junction of pulmonary epithelium and impaired Na, K-ATPase function, especially Na, K-ATPase α1 subunit. Up until now, the pathogenic mechanism at the level of protein during lipopolysaccharide- (LPS-) induced ARDS remains unclear. Methods Using an unbiased, discovery and quantitative proteomic approach, we discovered the differentially expressed proteins binding to Na, K-ATPase α1 between LPS-A549 cells and Control-A549 cells. These Na, K-ATPase α1 interacting proteins were screened by co-immunoprecipitation (Co-IP) technology. Among them, some of the differentially expressed proteins with significant performance were identified and quantified by liquid chromatography-tandem mass spectrometry (LC–MS/MS). Data are available via ProteomeXchange with identifier PXD032209. The protein interaction network was constructed by the related Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis. Several differentially expressed proteins were validated by Western blot. Results Of identified 1598 proteins, 89 were differentially expressed proteins between LPS-A549 cells and Control-A549 cells. Intriguingly, protein–protein interaction network showed that there were 244 significantly enriched co-expression among 60 proteins in the group control-A549. while the group LPS-A549 showed 43 significant enriched interactions among 29 proteins. The related GO and KEGG analysis found evident phenomena of ubiquitination and deubiquitination, as well as the pathways related to autophagy. Among proteins with rich abundance, there were several intriguing ones, including the deubiquitinase (OTUB1), the tight junction protein zonula occludens-1 (ZO-1), the scaffold protein in CUL4B-RING ubiquitin ligase (CRL4B) complexes (CUL4B) and the autophagy-related protein sequestosome-1 (SQSTM1). Conclusions In conclusion, our proteomic approach revealed targets related to the occurrence and development of ARDS, being the first study to investigate significant differences in Na, K-ATPase α1 interacting proteins between LPS-induced ARDS cell model and control-A549 cell. These proteins may help the clinical diagnosis and facilitate the personalized treatment of ARDS. Graphical Abstract

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OTUB1 Recruits Tumor Infiltrating Lymphocytes and Is a Prognostic Marker in Digestive Cancers

Cited by 11 publications

References 55 publications

Identification of Different Proteins Binding to Na, K-ATPase α1 in LPS-Induced ARDS Cell Model by Proteomic Analysis

Identification of Different Proteins Binding to Na, K-ATPase α1 in LPS-Induced ARDS Cell Model by Proteomic Analysis

Identification of Different Proteins Binding to Na, K-ATPase α1 in Lipopolysaccharide-Induced Acute Respiratory Distress Syndrome Cell Model by Proteomic Analysis

Identification of different proteins binding to Na, K-ATPase α1 in LPS-induced ARDS cell model by proteomic analysis

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