The effect of receptor protein tyrosine phosphatase kappa on the change of cell adhesion and proliferation induced by <i>N</i>‐acetylglucosaminyltransferase V

Wang, Can; Li, Zengxia; Yang, Zhaohua; Zhao, Hongbo; Yang, Yong; Chen, Kangli; Cai, Xiumei; Wang, Liying; Shi, Ying‐Hong; Qiu, Shuang–Jian; Fan, Jian‐Gao; Zha, Xiliang

doi:10.1002/jcb.22387

Cited by 5 publications

(5 citation statements)

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“…It was also reported that transcription levels of mgat4b , and mgat5 were increased in mice with HCC [9] . Recently, further analysis revealed that mgat5 could partially decrease cell adhesion and promote cell proliferation through RPTPκ [10] .…”

Section: Introductionmentioning

confidence: 99%

The Transcriptional Profiling of Glycogenes Associated with Hepatocellular Carcinoma Metastasis

et al. 2014

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Background and objectiveMetastasis is one of the important reasons for the poor prognosis of hepatocellular carcinoma (HCC), abnormal glycosylation plays a pivotal role in HCC metastasis. The goal of this study was to screen and validate the transcriptional profiling of glycogenes associated with HCC metastasis.MethodologyThe differentially transcribed glycogenes were screened out by the Human Glycosylation RT2 Profiler PCR Array, and were identified by qRT-PCR in human HCC cell lines and their orthotopic xenograft tumors. Further analyses were performed with K-mean clustering, Gene Ontology (GO) and ingenuity pathways analysis (IPA). Four differentially transcribed glycogenes were validated in clinical cancer specimens by qRT-PCR.ResultsA total of thirty-three differentially transcribed glycogenes were obtained by comparison the transcription in the metastatic human HCC cell lines (MHCC97L, MHCC97H and HCCLM3) with the transcription in the non-metastatic HCC cell line Hep3B. Seven differentially transcribed glycogenes were selected to further identification in human HCC cell lines and their orthotopic xenograft tumors. According to their trends by K-mean clustering, all of the differentially transcribed glycogenes were classified in six clusters. GO analysis of the differentially transcribed glycogenes described them in biological process, subcellular location and molecular function. Furthermore, the partial regulatory network of the differentially transcribed glycogenes was acquired through the IPA. The transcription levels of galnt3, gcnt3, man1a1, mgat5b in non-metastatic and metastatic HCC clinical cancer specimens showed the same changing trends with the results in human HCC cell lines and their orthotopic xenograft tumors, and the divergent transcription levels of gcnt3 and mgat5b were statistically significant.ConclusionsThe transcriptional profiling of glycogenes associated with HCC metastasis was obtained and validated in this study and it might provide novel drug targets and potential biological markers for HCC metastasis.

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Section: Introductionmentioning

confidence: 99%

The Transcriptional Profiling of Glycogenes Associated with Hepatocellular Carcinoma Metastasis

et al. 2014

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“…Alteration of glycosylation on RPTPs could affect their membrane retention level and change their phosphatase activity [20], [21]. We detected the in situ PTPRT expression in GnT-V cells and Mock cells.…”

Section: Resultsmentioning

confidence: 97%

“…The effect of aberrant N-glycosylation in PTPRT molecule on its function has not been well defined. PTPRK, an N-linked glycoprotein, has been reported as a novel substrate of GnT-V [19], [20]. In this study, we are interested in exploring whether GnT-V overexpression could affect PTPRT N-glycosylation and increase the amount of PTPRT at cell surface.…”

Section: Discussionmentioning

confidence: 99%

“…PTPRK (RPTPκ), another member of type IIB receptor-like PTPs subfamily, has been identified as a substrate of GnT-V [19]. Our previous work revealed that overexpression of GnT-V gene in human hepatoma cell line SMMC-7721 induced the addition of β1,6 GlcNAc branches to N-glycans of PTPRK and decreased the phosphatase activity of PTPRK, thus activating EGFR signaling [20]. In the present study, we report that PTPRT can be modified by GnT-V, leading to increased β1,6 GlcNAc branches on PTPRT.…”

Section: Introductionmentioning

confidence: 99%

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β1,6 GlcNAc Branches-Modified PTPRT Attenuates Its Activity and Promotes Cell Migration by STAT3 Pathway

Fan

et al. 2014

PLoS ONE

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Receptor-like protein tyrosine phosphatases (RPTPs) are type I transmembrane glycoproteins with N-glycans whose catalytic activities are regulated by dimerization. However, the intrinsic mechanism involved in dimerizing processes remains obscure. In this study, receptor protein tyrosine phosphatase rho (PTPRT) is identified as a novel substrate of N-Acetylglucosaminyltransferase V (GnT-V). We show that addition of β1,6 GlcNAc branches on PTPRT prolongs PTPRT's cell-surface retention time. GnT-V overexpression enhances galectin-3's cell-surface retention and promotes PTPRT's dimerization mediated by galectin-3. Increased dimerization subsequently reduces PTPRT's catalytic activity on the dephosphorylation of signal transducer and activator of transcription 3 (STAT3) at tyrosine residue 705 (pY705 STAT3), then the accumulated pY705 STAT3 translocates into the nucleus. Collectively, these findings provide an insight into the molecular mechanism by which GnT-V promotes cell migration, suggesting that accumulation of β1,6 GlcNAc branched N-glycans promotes PTPRT's dimerization and decreases its catalytic activity, resulting in enhanced cell migratory capacity.

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“…Indeed, PTPRF (LAR) is cleaved intracellularly into two subunits[ 11 ]. Proteolytic processing of other members of the PTPR family has been reported [ 12 – 15 ]. Among these, it is known that three isoforms of PTPRZ, the only other member of class V PTPRs beside PTPRG, are generated by alternative splicing from a single Ptprz gene in the rat [ 16 ].…”

Section: Introductionmentioning

confidence: 99%

Identification of Protein Tyrosine Phosphatase Receptor Gamma Extracellular Domain (sPTPRG) as a Natural Soluble Protein in Plasma

et al. 2015

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BackgroundPTPRG is a widely expressed protein tyrosine phosphatase present in various isoforms. Peptides from its extracellular domain have been detected in plasma by proteomic techniques. We aim at characterizing the plasmatic PTPRG (sPTPRG) form and to identify its source.Methodology/Principal FindingsThe expression of sPTPRG was evaluated in human plasma and murine plasma and tissues by immunoprecipitation and Western blotting. The polypeptides identified have an apparent Mr of about 120 kDa (major band) and 90 kDa (minor band) respectively. Full length PTPRG was identified in the 100.000×g pelleted plasma fraction, suggesting that it was present associated to cell-derived vesicles (exosomes). The release of sPTPRG by HepG2 human hepatocellular carcinoma cell line was induced by ethanol and sensitive to metalloproteinase and not to Furin inhibitors. Finally, increased levels of the plasmatic ∼120 kDa isoform were associated with the occurrence of liver damage.ConclusionsThese results demonstrate that sPTPRG represent a novel candidate protein biomarker in plasma whose increased expression is associated to hepatocyte damage. This observation could open a new avenue of investigation in this challenging field.

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The effect of receptor protein tyrosine phosphatase kappa on the change of cell adhesion and proliferation induced by N‐acetylglucosaminyltransferase V

Cited by 5 publications

References 45 publications

The Transcriptional Profiling of Glycogenes Associated with Hepatocellular Carcinoma Metastasis

The Transcriptional Profiling of Glycogenes Associated with Hepatocellular Carcinoma Metastasis

β1,6 GlcNAc Branches-Modified PTPRT Attenuates Its Activity and Promotes Cell Migration by STAT3 Pathway

Identification of Protein Tyrosine Phosphatase Receptor Gamma Extracellular Domain (sPTPRG) as a Natural Soluble Protein in Plasma

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