Glycolipid transfer protein and intracellular traffic of glucosylceramide

Sasaki, Terukatsu

doi:10.1007/bf01939700

Cited by 53 publications

(39 citation statements)

References 60 publications

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“…The characteristics of GlcCer transport more closely resemble carrier-mediated transport ofphosphoglycerides such as phosphatidylcholine to the plasma membrane (16). The kinetics of GlcCer transport, while not as rapid as those of phosphatidylcholine (7), are significantly more rapid than that of GM3 or estimates of bulk flow through the Golgi compartment (Fig.…”

Section: Discussionmentioning

confidence: 71%

Transport of newly synthesized glucosylceramide to the plasma membrane by a non-Golgi pathway.

Warnock

Lutz

Blackburn

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

113

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High-gradient magnetic affinity chromatography (HDMAC) has been used to obtain highly enriched plasma membranes, free of intracellular membrane contaminmts, from cultured Chinese hamster ovary (CHO) cells in yields of .80%. Using this procedure we have characterized the transport of glucosYceramlde (GlcCer) and the gangoide GM3 to the plasma membrane. Newly synthesized GlcCer reaches the plasma membrane in 7.2 min, whereas GM3 requires 21.5 min to reach the plasma membrane. Brefeldin A prevents transport of newly synthesized GM3 and sWhinmyelmn to the plasma membrane but has no effect on the transport of GIcCer. Similarly, incubation of CHO cells at 15°C blocks transport of GM3 and sphingomyelin to the plasma membrane but has no effect on GicCer movement. We propose that carrier-mediated transport accounts for a major fraction of the plasma membrane GlcCer. Puls-chase studies with either [3Hglcose or [3pH] (2) and ganglioside GM3 (3) as well as short-chain derivatives of sphingomyelin and glucosylceramide (GlcCer) (4-6) to the plasma membrane. (ii) Soluble carriers such as lipid-transfer proteins account for a major portion of the movement of the phospholipids phosphatidylcholine (7) and phosphatidylethanolamine (8, 9) to the plasma membrane. (iii) A vesicular transport pathway which is distinct from the secretory pathway accounts for the transport of newly synthesized cholesterol (10) to the plasma membrane. Transfer ofglucose to ceramide by UDPglucoseceramide glucosyltransferase has been localized to the cytosolic surface of the Golgi apparatus (11)(12)(13)(14), indicating that GlcCer must be translocated to the luminal leaflet for higher glycosylation to occur. We have determined that 45% of GlcCer in Chinese hamster ovary (CHO) cells is located in the plasma membrane (15). Since GlcCer is synthesized on the cytosolic surface of the Golgi membrane and translocated to the luminal surface, GlcCer could be transported to the plasma membrane through the vesicular protein secretory pathway and/or by an alternative pathway through the cytosol, perhaps by lipid-transfer proteins as proposed by Sasaki (16 (vol/vol) heat-inactivated fetal bovine serum. CHO K1 cells were maintained in Dulbecco's modified Eagle's medium (DMEM) containing 10%6 iron-supplemented heat-inactivated fetal bovine serum, 2 mM glutamine, 1x nonessential amino acids, 1 mM proline, and lx penicillin/streptomycin. Cells were released by trypsin/EDTA treatment and plated on fresh culture dishes 48 hr prior to experimental manipulation.Metabolic Labeling. For pulse-chase experiments, cells were rinsed three times in Dulbecco's phosphate-buffered saline (PBS) and incubated for 1 hr at 370C in methionine-and cysteine-free medium. The medium was replaced with fresh methionine-and cysteine-free medium containing Tran35S-label at 150 pCi/ml. After 20 min of-incubation, incorporation was terminated by washing twice with PBS and the chase was initiated by addition of complete medium. For metabolic labeling of lipids [3H]palmitate [10 puCi/ml ...

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Section: Discussionmentioning

confidence: 71%

Transport of newly synthesized glucosylceramide to the plasma membrane by a non-Golgi pathway.

Warnock

Lutz

Blackburn

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

113

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“…Rapid transfer of GlcCer by GLTP was observed only when the donor and acceptor phosphatidylcholine vesicles were both in the liquid-crystalline state [4]. Additional insights into these early studies of the 1980s are provided in several excellent and comprehensive reviews [15][16][17][18].…”

Section: Historic Overview ---Early Insightsmentioning

confidence: 99%

Glycolipid transfer proteins

Brown

Mattjus

2007

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

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Glycolipid transfer proteins (GLTPs) are small (24 kD), soluble, ubiquitous proteins characterized by their ability to accelerate the intermembrane transfer of glycolipids in vitro. GLTP specificity encompasses both sphingoid-and glycerol-based glycolipids, but with a strict requirement that the initial sugar residue be beta-linked to the hydrophobic lipid backbone. The 3D protein structures of GLTP reveal liganded structures with unique lipid binding modes. The biochemical properties of GLTP action at the membrane surface have been studied rather comprehensively, but the biological role of GLTP remains enigmatic. What is clear is that GLTP differs distinctly from other known glycolipid-binding proteins, such as nonspecific lipid transfer proteins, lysosomal sphingolipid activator proteins, lectins, lung surfactant proteins as well as other lipid binding/transfer proteins. Based on the unique conformational architecture that targets GLTP to membranes and enables glycolipid binding, GLTP is now considered the prototypical and founding member of a new protein superfamily in eukaryotes.

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“…After the initial discovery in the membranefree cytosolic extract of bovine spleen [160], proteins with similar activities were found in a wide variety of tissues, including bovine and porcine brain, liver and kidney, as well as in plants [161]. Purified GLTPs from animal spleen and brain consist of single polypeptides of 23-24 kDa and have basic isoelectric points and absolute specificity for glycolipids [162][163][164].…”

Section: Glycolipid Transfer Protein May Also Be Involved In Gangliosmentioning

confidence: 99%

Shedding and uptake of gangliosides and glycosylphosphatidylinositol-anchored proteins

Lauc

Heffer-Lauc

2006

Biochimica et Biophysica Acta (BBA) - General Subjects

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Glycolipid transfer protein and intracellular traffic of glucosylceramide

Cited by 53 publications

References 60 publications

Transport of newly synthesized glucosylceramide to the plasma membrane by a non-Golgi pathway.

Transport of newly synthesized glucosylceramide to the plasma membrane by a non-Golgi pathway.

Glycolipid transfer proteins

Shedding and uptake of gangliosides and glycosylphosphatidylinositol-anchored proteins

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