Trans-golgi network and subapical compartment of HepG2 cells display different properties in sorting and exiting of sphingolipids
| العنوان: | Trans-golgi network and subapical compartment of HepG2 cells display different properties in sorting and exiting of sphingolipids |
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| المؤلفون: | Dick Hoekstra, Olaf Maier |
| المساهمون: | Nanotechnology and Biophysics in Medicine (NANOBIOMED) |
| المصدر: | The Journal of Biological Chemistry, 278(1), 164-173. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| بيانات النشر: | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 2003. |
| سنة النشر: | 2003 |
| مصطلحات موضوعية: | Carcinoma, Hepatocellular, Biology, Cell Fractionation, Ceramides, PLASMA-MEMBRANE PROTEINS, Biochemistry, Models, Biological, GPI-ANCHORED PROTEINS, symbols.namesake, HT29 Cells, MDCK CELLS, MAMMALIAN-CELLS, Cell polarity, Tumor Cells, Cultured, Compartment (development), Humans, Transport Vesicles, Molecular Biology, Fluorescent Dyes, ENDOCYTIC PATHWAY, Sphingolipids, Vesicle, Cell Membrane, Liver Neoplasms, Temperature, Cell Polarity, Biological Transport, Cell Biology, Golgi apparatus, Apical membrane, HT29 CELLS, Endocytosis, Trifluoperazine, Cell biology, MULTIDRUG-RESISTANCE PROTEIN, HEPATOMA-CELLS, 4-Chloro-7-nitrobenzofurazan, CANINE KIDNEY-CELLS, symbols, CACO-2 CELLS, lipids (amino acids, peptides, and proteins), Cell fractionation, Biogenesis, trans-Golgi Network |
| الوصف: | In HepG2 cells, the subapical compartment (SAC) is involved in the biogenesis of membrane polarity. By contrast, direct apical transport originating from the trans-Golgi network (TGN), which may contribute to polarity establishment, has been poorly defined in these cells. Thus, although newly synthesized sphingolipids can be directly transported from the TGN to the apical membrane, numerous apical resident proteins are traveling via the transcytotic route. Here, we developed an in vitro transport assay and compared the molecular sorting of 6-[N-(7-nitrobenz-2-oxa-1,3 diazol-4-yl)amino] hexanoyl-sphingomyelin (C6NBD-SM) and C6NBD-glucosylceramide (C6NBD-GlcCer) in TGN and SAC. SM is released from both TGN and SAC in the lumenal leaflet of transport vesicles. This holds also for GlcCer released from the SAC but not for a substantial fraction that departed from the Golgi. Distinct transport vesicles, enriched in either SM or GlcCer are released from SAC, consistent with their rigid sorting in this compartment. Different vesicle populations could not be recovered from TGN, although in situ experiments reveal that GlcCer is preferentially transported to the apical membrane, reflecting different transport mechanisms. The results indicate that in HepG2 cells sphingolipids are mainly sorted in the SAC membrane and that the release of SM from SAC and TGN is differentially regulated. |
| اللغة: | English |
| تدمد: | 1083-351X 0021-9258 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dded5dc6e3aa4898b37d1567cbe2da8cTest https://research.rug.nl/en/publications/d29e2607-bfa9-4b6f-9189-e391055d1382Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....dded5dc6e3aa4898b37d1567cbe2da8c |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 1083351X 00219258 |
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