Identification of Differentially Expressed Proteins of Normal and Cancerous Human Colorectal Tissues by Liquid Chromatograph-Mass Spectrometer Based on iTRAQ Approach

Lv, Jingjing; Fan, Ni; Wang, Yangkun; Wang, Xiuli; Gao, Chunfang

doi:10.3109/07357907.2015.1055757

Cited by 3 publications

(3 citation statements)

References 22 publications

(22 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Recent studies have shown that EHD2 could function as a tumor suppresser protein. 39 – 42 EHD2 overexpression was inversely associated with overall survival and EHD2 knockdown significantly enhanced breast cancer and esophageal squamous cell carcinoma (ESCC) cell migration, cell invasion and enhanced epithelial to mesenchymal transition (EMT). 39 , 40 In this study, we observed that dissociation of EHD2 from myoferlin in activated tumor cells (treated with IL-6) led to enhanced tumor cell motility and cancer stem cell phenotype.…”

Section: Discussionmentioning

confidence: 99%

A muscle-specific protein ‘myoferlin’ modulates IL-6/STAT3 signaling by chaperoning activated STAT3 to nucleus

et al. 2017

View full text Add to dashboard Cite

Myoferlin, a member of ferlin family of proteins, was first discovered as a candidate gene for muscular dystrophy and cardiomyopathy. Recently myoferlin was shown to be also expressed in endothelial and cancer cells where it was shown to modulate VEGFR-2 and EGFR signaling by enhancing their stability and recycling. Based on these reports, we hypothesized that myoferlin might be regulating IL-6 signaling by modulating IL-6R stabilization and recycling. However, in our immunoprecipitation (IP) experiments, we did not observe myoferlin binding with IL-6R. Instead, we made a novel discovery that in resting cells myoferlin was bound to EHD2 protein and when cells were treated with IL-6, myoferlin dissociated from EHD2 and binds to activated STAT3. Interestingly, myoferlin depletion did not affect STAT3 phosphorylation, but completely blocked STAT3 translocation to nucleus. In addition, inhibition of STAT3 phosphorylation by phosphorylation defective STAT3 mutants or JAK inhibitor blocked STAT3 binding to myoferlin and nuclear translocation. Myoferlin knockdown significantly decreased IL-6-mediated tumor cell migration, tumorsphere formation and ALDH positive cancer stem cell population, in vitro. Furthermore, myoferlin knockdown significantly decreased IL-6-meditated tumor growth and tumor metastasis. Based on these results, we have proposed a novel model for the role of myoferlin in chaperoning phosphorylated STAT3 to the nucleus.

show abstract

Section: Discussionmentioning

confidence: 99%

A muscle-specific protein ‘myoferlin’ modulates IL-6/STAT3 signaling by chaperoning activated STAT3 to nucleus

et al. 2017

View full text Add to dashboard Cite

show abstract

“…| 7 of 12 colorectal cancer through liquid chromatograph-mass spectrometer (LC/MS) based labeled with isobaric mass tags for relative and absolute quantitation (iTRAQ) analysis, including EHD2. 102 Studies have shown that EHD2 expression is decreased in CC tissues, which is associated with poor prognosis. 103 And the knockdown of EHD2…”

Section: Type Of Cancer Expression Actionsmentioning

confidence: 99%

“…Thus, there is a need to further investigate the molecular mechanisms of CC and identify new therapeutic targets to improve the survival rate for CC patients. Lv et al identified differentially expressed genes in colorectal cancer through liquid chromatograph‐mass spectrometer (LC/MS) based labeled with isobaric mass tags for relative and absolute quantitation (iTRAQ) analysis, including EHD2 102 . Studies have shown that EHD2 expression is decreased in CC tissues, which is associated with poor prognosis 103 .…”

Section: The Potential Clinical Applications Of Ehd2mentioning

confidence: 99%

EH domain‐containing protein 2 (EHD2): Overview, biological function, and therapeutic potential

Zhu,

Zhang,

Xia

et al. 2024

Cell Biochemistry & Function

View full text Add to dashboard Cite

EH domain‐containing protein 2 (EHD2) is a member of the EHD protein family and is mainly located in the plasma membrane, but can also be found in the cytoplasm and endosomes. EHD2 is also a nuclear‐cytoplasmic shuttle protein. After entering the cell nuclear, EHD2 acts as a corepressor of transcription to inhibit gene transcription. EHD2 regulates a series of biological processes. As a key regulator of endocytic transport, EHD2 is involved in the formation and maintenance of endosomal tubules and vesicles, which are critical for the intracellular transport of proteins and other substances. The N‐terminal of EHD2 is attached to the cell membrane, while its C‐terminal binds to the actin‐binding protein. After binding, EHD2 connects with the actin cytoskeleton, forming the curvature of the membrane and promoting cell endocytosis. EHD2 is also associated with membrane protein trafficking and receptor signaling, as well as in glucose metabolism and lipid metabolism. In this review, we highlight the recent advances in the function of EHD2 in various cellular processes and its potential implications in human diseases such as cancer and metabolic disease. We also discussed the prospects for the future of EHD2. EHD2 has a broad prospect as a therapeutic target for a variety of diseases. Further research is needed to explore its mechanism, which could pave the way for the development of targeted treatments.

show abstract

EHD2 Overexpression Suppresses the Proliferation, Migration, and Invasion in Human Colon Cancer

Guan

Xiao

et al. 2021

Cancer Investigation

View full text Add to dashboard Cite

Identification of Differentially Expressed Proteins of Normal and Cancerous Human Colorectal Tissues by Liquid Chromatograph-Mass Spectrometer Based on iTRAQ Approach

Cited by 3 publications

References 22 publications

A muscle-specific protein ‘myoferlin’ modulates IL-6/STAT3 signaling by chaperoning activated STAT3 to nucleus

A muscle-specific protein ‘myoferlin’ modulates IL-6/STAT3 signaling by chaperoning activated STAT3 to nucleus

EH domain‐containing protein 2 (EHD2): Overview, biological function, and therapeutic potential

EHD2 Overexpression Suppresses the Proliferation, Migration, and Invasion in Human Colon Cancer

Contact Info

Product

Resources

About