| http://purl.uniprot.org/citations/28782625 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/28782625 | http://www.w3.org/2000/01/rdf-schema#comment | "BackgroundThere is a pressing need for biomarkers that can distinguish indolent from aggressive prostate cancer to prevent over-treatment of patients with indolent tumor.MethodsGolgi targeting of glycosyltransferases was characterized by confocal microscopy after knockdown of GM130, giantin, or both. N-glycans on a trans-Golgi enzyme β4galactosyltransferase-1 isolated by immunoprecipitation from androgen-sensitive and independent prostate cancer cells were determined by matrix-assisted laser desorption-time of flight-mass spectrometry. In situ proximity ligation assay was employed to determine co-localization of (a) α-mannosidase IA, an enzyme required for processing Man8GlcNAc2 down to Man5GlcNAc2 to enable synthesis of complex-type N-glycans, with giantin, GM130, and GRASP65, and (b) trans-Golgi glycosyltransferases with high mannose N-glycans terminated with α3-mannose.ResultsDefective giantin in androgen-independent prostate cancer cells results in a shift of Golgi targeting of glycosyltransferases and α-mannosidase IA from giantin to GM130-GRASP65. Consequently, trans-Golgi enzymes and cell surface glycoproteins acquire high mannose N-glycans, which are absent in cells with functional giantin. In situ proximity ligation assays of co-localization of α-mannosidase IA with GM130 and GRASP65, and trans-Golgi glycosyltransferases with high mannose N-glycans are negative in androgen-sensitive LNCaP C-33 cells but positive in androgen-independent LNCaP C-81 and DU145 cells, and LNCaP C-33 cells devoid of giantin.ConclusionIn situ proximity ligation assays of Golgi localization of α-mannosidase IA at giantin versus GM130-GRASP65 site, and absence or presence of N-glycans terminated with α3-mannose on trans-Golgi glycosyltransferases may be useful for distinguishing indolent from aggressive prostate cancer cells."xsd:string |
| http://purl.uniprot.org/citations/28782625 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbagen.2017.08.006"xsd:string |
| http://purl.uniprot.org/citations/28782625 | http://purl.uniprot.org/core/author | "Bhat G."xsd:string |
| http://purl.uniprot.org/citations/28782625 | http://purl.uniprot.org/core/author | "Lin M.F."xsd:string |
| http://purl.uniprot.org/citations/28782625 | http://purl.uniprot.org/core/author | "Cheng P.W."xsd:string |
| http://purl.uniprot.org/citations/28782625 | http://purl.uniprot.org/core/author | "Hothpet V.R."xsd:string |
| http://purl.uniprot.org/citations/28782625 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
| http://purl.uniprot.org/citations/28782625 | http://purl.uniprot.org/core/name | "Biochim Biophys Acta Gen Subj"xsd:string |
| http://purl.uniprot.org/citations/28782625 | http://purl.uniprot.org/core/pages | "2891-2901"xsd:string |
| http://purl.uniprot.org/citations/28782625 | http://purl.uniprot.org/core/title | "Shifted Golgi targeting of glycosyltransferases and alpha-mannosidase IA from giantin to GM130-GRASP65 results in formation of high mannose N-glycans in aggressive prostate cancer cells."xsd:string |
| http://purl.uniprot.org/citations/28782625 | http://purl.uniprot.org/core/volume | "1861"xsd:string |
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