Golgi phosphoprotein 2 (GOLPH2/GP73/GOLM1) interacts with secretory clusterin

Zhou, Yan; Li, Leike; Hu, Longbo; Peng, Tao

doi:10.1007/s11033-010-0251-7

Cited by 39 publications

(40 citation statements)

References 17 publications

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“…We, and others, have now reported that GP73 protein is upregulated in patients with HCC[3, 5, 4, 2, 7]. Taken together with the results of the study reported here, it seems likely that the “source” cells for the elevated secreted levels of GP73 observed in HCC patients is the cancer, itself.…”

supporting

confidence: 85%

Analysis of GP73 in patients with HCC as a function of anti-cancer treatment

Hann

Wang

Hafner

et al. 2011

CBM

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In this study, we examined the level of Golgi protein 73 (GP73) in the serum of 9 patients as a function of anti-liver cancer treatment. Although the numbers are small, a clear trend was observed. Patients who remained tumor free (up to 6 years post-treatment) showed reductions in GP73 at the first time point available post-treatment. In contrast, patients who had high levels GP73 post treatment all had re-occurrence within a 5 year period. These data are preliminary but dramatically imply that this marker may have value in the monitoring of HCC patients and may be elevated even when small, undetectable tumors are present.

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supporting

confidence: 85%

Analysis of GP73 in patients with HCC as a function of anti-cancer treatment

Hann

Wang

Hafner

et al. 2011

CBM

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“…The coiled-coil domain of GP73 and its Golgi localization are necessary for the enhancement of HCV production (Figure 4). Our previous study showed that the coiled-coil domain of GP73 is highly conserved, and serves as the interaction domain for the homodimerization of GP73 and its interaction with other proteins such as clusterin [25], [27]. These results suggest that GP73 possibly recruits other proteins in HCV secretion through the coiled-coil domain.…”

Section: Discussionmentioning

confidence: 93%

“…Based on protein sequence analysis, GP73 is conserved among different species, and shares a short cytoplasmic N-terminus, a transmembrane domain (TMD), and a coiled-coil domain [25], [26]. Previous studies showed the following findings: GP73 exists as a dimer that is mainly mediated by the conserved coiled-coil domain, and the dimer is stabilized by two inter-protein disulfide bonds formed by two conserved cysteines in the coiled-coil domain; the Golgi localization of GP73 is determined by the TMD and a single positively charged residue flanking the TMD on the cytoplasmic site; GP73 interacts with other cellular proteins, including clusterin, mainly through the coiled-coil domain [25], [27]. However, the exact function and biological function of GP73 in HCV infection have not been investigated at the cellular level.…”

Section: Introductionmentioning

confidence: 99%

GP73 Is Upregulated by Hepatitis C Virus (HCV) Infection and Enhances HCV Secretion

Yao

Wang

et al. 2014

PLoS ONE

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Hepatitis C virus (HCV) is a major cause of chronic liver disease. However, little is known about the details of its assembly and secretion. Golgi-related proteins have been recently proven to have a key function in HCV secretion. Golgi protein 73 (GP73), a resident Golgi membrane protein, is a potential serum biomarker for the diagnosis of liver diseases and hepatocellular carcinoma. Previous studies have demonstrated the upregulation of GP73 in the liver samples and sera of HCV-infected patients. However, the function and regulatory mechanism of GP73 in HCV infection at the cellular level remain unknown. In this study, we examined the expression level of GP73 in HCV infected cells and its effect on HCV life cycle in cell culture systems. Both the protein expression and mRNA levels of GP73 significantly increased in HCV subgenomic replicon-harboring cells and HCV-infected cells, which imply that GP73 was upregulated by HCV infection. HCV production was significantly enhanced when GP73 was overexpressed, but dramatically inhibited when GP73 was silenced. However, the overexpression and knockdown of GP73 showed no evident effect on the entry, protein translation, RNA replication, and assembly of HCV, which indicates that GP73 enhanced the secretion process. Moreover, the coiled-coil domain of GP73 was required to increase HCV secretion. GP73 increased and interacted with apolipoprotein E, an identified host factor that assists in HCV secretion. These results demonstrate the critical function of GP73 in HCV secretion and provide new insights into the therapeutic design of antiviral strategies.

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“…Furthermore, GOLM1 is a cis-Golgi membrane protein with unknown function (19). This protein is a known noninvasive biomarker for prostate cancer (20), which is predominantly expressed by the cells of the epithelial lineage, especially in the liver and kidney (21). Defects in GOLM1 gene leads to the development of renal disease, most notably focal segmental glomerulosclerosis and hyaline thrombi (22).…”

Section: Discussionmentioning

confidence: 99%

Penalized Regression Versus Random Forest Model in Analyzing High Dimensional Proteomic Data: Diagnosis of IgA Nephropathy

et al. 2017

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Background: Immunoglobulin A nephropathy (IgAN) is considered a chronic renal disease and the most prevalent glomerulonephritis throughout the world. In order to model a large number of extracted biomarkers and identify the most effective biomarkers on IgAN disease, the researchers implemented 2 methods of penalized regression, known as LASSO and MCP logistic regression versus random forest method, which are appropriate for high dimensional and low sample size problems.

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Golgi phosphoprotein 2 (GOLPH2/GP73/GOLM1) interacts with secretory clusterin

Cited by 39 publications

References 17 publications

Analysis of GP73 in patients with HCC as a function of anti-cancer treatment

Analysis of GP73 in patients with HCC as a function of anti-cancer treatment

GP73 Is Upregulated by Hepatitis C Virus (HCV) Infection and Enhances HCV Secretion

Penalized Regression Versus Random Forest Model in Analyzing High Dimensional Proteomic Data: Diagnosis of IgA Nephropathy

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