A 56-kDa Selenium-binding Protein Participates in Intra-Golgi Protein Transport

Porat, Amir; Sagiv, Yuval; Elazar, Zvulun

doi:10.1074/jbc.275.19.14457

Cited by 121 publications

(113 citation statements)

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“…The transport reactions were incubated for 2 h at 30°C. The incorporation of N-[ 3 H]acetylglucosamine into the VSV-G protein was determined as described previously (32).…”

Section: Methodsmentioning

confidence: 99%

Intra-Golgi Protein Transport Depends on a Cholesterol Balance in the Lipid Membrane

Stüven

Porat

Shimron

et al. 2003

Journal of Biological Chemistry

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Transport of proteins between intracellular membrane compartments is mediated by a protein machinery that regulates the budding and fusion processes of individual transport steps. Although the core proteins of both processes are defined at great detail, much less is known about the involvement of lipids. Here we report that changing the cellular balance of cholesterol resulted in changes of the morphology of the Golgi apparatus, accompanied by an inhibition of protein transport. By using a well characterized cell-free intra-Golgi transport assay, these observations were further investigated, and it was found that the transport reaction is sensitive to small changes in the cholesterol content of Golgi membranes. Addition as well as removal of cholesterol (10 ؎ 6%) to Golgi membranes by use of methyl-␤-cyclodextrin specifically inhibited the intra-Golgi transport assay. Transport inhibition occurred at the fusion step. Modulation of the cholesterol content changed the lipid raft partitioning of phosphatidylcholine and heterotrimeric G proteins, but not of other (non) lipid raft proteins and lipids. We suggest that the cholesterol balance in Golgi membranes plays an essential role in intra-Golgi protein transport and needs to be carefully regulated to maintain the structural and functional organization of the Golgi apparatus.

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“…The transport reactions were incubated for 2 h at 30°C. The incorporation of N-[ 3 H]acetylglucosamine into the VSV-G protein was determined as described previously (32).…”

Section: Methodsmentioning

confidence: 99%

Intra-Golgi Protein Transport Depends on a Cholesterol Balance in the Lipid Membrane

Stüven

Porat

Shimron

et al. 2003

Journal of Biological Chemistry

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“…SELENBP1 is a cytoplasmic protein, but a significant amount of SELENBP1 was also membrane associated, predominantly on the Golgi membrane. 18 To validate our findings, SELENBP1 protein levels in the membrane fraction of HOSE and cancer cells were assayed with the SELENBP1-specific antibody. As expected, SELENBP1 was detected in the HOSE cells (Fig.…”

Section: Selenbp1 Protein Identification and Verificationmentioning

confidence: 99%

Selenium binding protein 1 in ovarian cancer

Huang

Park

et al. 2006

Intl Journal of Cancer

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Selenium binding protein 1 (SELENBP1) was identified to be the most significantly down-regulated protein in ovarian cancer cells by a membrane proteome profiling analysis. SELENBP1 expression levels in 4 normal ovaries, 8 benign ovarian tumors, 12 borderline ovarian tumors and 141 invasive ovarian cancers were analyzed with immunohistochemical assay. SELENBP1 expression was reduced in 87% cases of invasive ovarian cancer (122/141) and was significantly reduced in borderline tumors and invasive cancers (p < 0.001). Cox multivariate analysis within the 141 invasive cancer tissues showed that SELENBP1 expression score was a potential prognostic indicator for unfavorable prognosis of ovarian cancer (hazard ratio [HR], 2.18; 95% CI 5 1.22-3.90; p 5 0.009). Selenium can disrupt the androgen pathway, which has been implicated in modulating SELENBP1 expression. We investigated the effects of selenium and androgen on normal human ovarian surface epithelial (HOSE) cells and cancer cells. Interestingly, SELENBP1 mRNA and protein levels were reduced by androgen and elevated by selenium treatment in the normal HOSE cells, whereas reversed responses were observed in the ovarian cancer cell lines. These results suggest that changes of SELENBP1 expression in malignant ovarian cancer are an indicator of aberration of selenium/androgen pathways and may reveal prognostic information of ovarian cancer. ' 2005 Wiley-Liss, Inc.Key words: ovarian cancer; membrane proteome profiling; 2-D PAGE; selenium binding protein 1; prognostic marker; androgen; methylselenocysteine Despite advances in cancer therapeutic agents in recent years, approximately 14,000 women still die of ovarian cancer each year in the United States, making it the most lethal of the gynecological malignancies. 1 Currently, surgical debulking followed by chemotherapy is the major treatment approach for ovarian cancer. Most cases of ovarian cancer are diagnosed at advanced stages when the prognosis for 5-year survival is poor. 2 Developing new diagnostic technique and improving current therapeutic strategy are the main directions to fight this morbid disease.Multiple genomic and proteomic approaches have been applied to identify disease-associated biomarkers for diagnosis and disease management. Applying cDNA and oligo microarray technology have enabled scientists to look into the global differences in gene expression between normal and cancer cells. 3 For proteomic approaches, two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) followed by protein identification using mass spectrometry has been the primary technique for biomarker discovery. 4,5 Membrane-associated proteins have been suggested to be a potential resource for biomarker screening. 6 In our pilot study of the use of 2-D PAGE to profile membrane-associated proteins of normal ovarian surface epithelial cells and ovarian cancer cell lines, selenium binding protein 1 (SELENBP1) was identified as the most significantly down-regulated protein in the cancer cells.The human selenium binding protein gene (...

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“…SELENBP1 is implicated to play a role in toxification/ detoxification processes (257), cell-growth regulation (21,119), intra-Golgi protein transport (255), aging (71), and lipid metabolism (251). Interestingly, several studies have reported decreased expression levels of both SELENBP1 and SELENBP2 in tumors compared with normal tissue.…”

Section: G Selenium-binding Proteinsmentioning

confidence: 99%

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2007

Antioxidants & Redox Signaling

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A 56-kDa Selenium-binding Protein Participates in Intra-Golgi Protein Transport

Cited by 121 publications

References 58 publications

Intra-Golgi Protein Transport Depends on a Cholesterol Balance in the Lipid Membrane

Intra-Golgi Protein Transport Depends on a Cholesterol Balance in the Lipid Membrane

Selenium binding protein 1 in ovarian cancer

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