The Experts below are selected from a list of 9 Experts worldwide ranked by ideXlab platform
Robert I. Lechler - One of the best experts on this subject based on the ideXlab platform.
-
Expression of α-1,3-Galactose and Other Type 2 Oligosaccharide Structures in a Porcine Endothelial Cell Line Transfected with Human α-1,2-Fucosyltransferase cDNA
The Journal of biological chemistry, 1997Co-Authors: Armin Sepp, Patricia Skacel, Ragnar Lindstedt, Robert I. LechlerAbstract:Abstract The binding of xenoreactive natural antibodies to the Galα1–3Galβ1–4GlcNAc (α-Galactose) Oligosaccharide epitope on pig cells activates the recipient’s complement system in pig to primate xenotransplantation. Expression of human α-1,2-fucosyltransferase in pigs has been proposed as a strategy for reducing the expression level of the α-Galactose epitope, thereby rendering the pig organs more suitable for transplantation into humans. The aim of this study was to examine how the cell surface expression of α-Galactose, H, and related fucosylated and sialylated structures on a pig liver endothelial cell line is affected by transfection of human α-1,2-fucosyltransferase cDNA. Nontransfected and mock-transfected cells expressed α-Galactose, α-2,3-sialylated, and α-2,6-sialylated epitopes strongly, with low level expression of type 2 H and LewisX. By contrast, expression of the H epitope was increased 5–8-fold in transfected cells with a 40% reduction in the expression of α-Galactose epitope and a 50% decrease in sialylation, as measured by binding of Maackia amurensis and Sambuccus nigra agglutinins. LewisX expression was reduced to background levels, while the LewisY neoepitope was induced in human α-1,2-fucosyltransferase-expressing pig cells. The activities of endogenous α-1,3-galactosyltransferase, α-1,3-fucosyltransferases, and α-2,3- and α-2,6-sialyltransferases acting on lactosamine were unaffected. Our results show that a reduction in α-Galactose epitope expression in porcine endothelial cells transfected with human α-1,2-fucosyltransferase cDNA may be achieved but at the expense of considerable distortion of the overall cell surface glycosylation profile, including the appearance of carbohydrate epitopes that are absent from the parent cells.
Armin Sepp - One of the best experts on this subject based on the ideXlab platform.
-
Expression of α-1,3-Galactose and Other Type 2 Oligosaccharide Structures in a Porcine Endothelial Cell Line Transfected with Human α-1,2-Fucosyltransferase cDNA
The Journal of biological chemistry, 1997Co-Authors: Armin Sepp, Patricia Skacel, Ragnar Lindstedt, Robert I. LechlerAbstract:Abstract The binding of xenoreactive natural antibodies to the Galα1–3Galβ1–4GlcNAc (α-Galactose) Oligosaccharide epitope on pig cells activates the recipient’s complement system in pig to primate xenotransplantation. Expression of human α-1,2-fucosyltransferase in pigs has been proposed as a strategy for reducing the expression level of the α-Galactose epitope, thereby rendering the pig organs more suitable for transplantation into humans. The aim of this study was to examine how the cell surface expression of α-Galactose, H, and related fucosylated and sialylated structures on a pig liver endothelial cell line is affected by transfection of human α-1,2-fucosyltransferase cDNA. Nontransfected and mock-transfected cells expressed α-Galactose, α-2,3-sialylated, and α-2,6-sialylated epitopes strongly, with low level expression of type 2 H and LewisX. By contrast, expression of the H epitope was increased 5–8-fold in transfected cells with a 40% reduction in the expression of α-Galactose epitope and a 50% decrease in sialylation, as measured by binding of Maackia amurensis and Sambuccus nigra agglutinins. LewisX expression was reduced to background levels, while the LewisY neoepitope was induced in human α-1,2-fucosyltransferase-expressing pig cells. The activities of endogenous α-1,3-galactosyltransferase, α-1,3-fucosyltransferases, and α-2,3- and α-2,6-sialyltransferases acting on lactosamine were unaffected. Our results show that a reduction in α-Galactose epitope expression in porcine endothelial cells transfected with human α-1,2-fucosyltransferase cDNA may be achieved but at the expense of considerable distortion of the overall cell surface glycosylation profile, including the appearance of carbohydrate epitopes that are absent from the parent cells.
Patricia Skacel - One of the best experts on this subject based on the ideXlab platform.
-
Expression of α-1,3-Galactose and Other Type 2 Oligosaccharide Structures in a Porcine Endothelial Cell Line Transfected with Human α-1,2-Fucosyltransferase cDNA
The Journal of biological chemistry, 1997Co-Authors: Armin Sepp, Patricia Skacel, Ragnar Lindstedt, Robert I. LechlerAbstract:Abstract The binding of xenoreactive natural antibodies to the Galα1–3Galβ1–4GlcNAc (α-Galactose) Oligosaccharide epitope on pig cells activates the recipient’s complement system in pig to primate xenotransplantation. Expression of human α-1,2-fucosyltransferase in pigs has been proposed as a strategy for reducing the expression level of the α-Galactose epitope, thereby rendering the pig organs more suitable for transplantation into humans. The aim of this study was to examine how the cell surface expression of α-Galactose, H, and related fucosylated and sialylated structures on a pig liver endothelial cell line is affected by transfection of human α-1,2-fucosyltransferase cDNA. Nontransfected and mock-transfected cells expressed α-Galactose, α-2,3-sialylated, and α-2,6-sialylated epitopes strongly, with low level expression of type 2 H and LewisX. By contrast, expression of the H epitope was increased 5–8-fold in transfected cells with a 40% reduction in the expression of α-Galactose epitope and a 50% decrease in sialylation, as measured by binding of Maackia amurensis and Sambuccus nigra agglutinins. LewisX expression was reduced to background levels, while the LewisY neoepitope was induced in human α-1,2-fucosyltransferase-expressing pig cells. The activities of endogenous α-1,3-galactosyltransferase, α-1,3-fucosyltransferases, and α-2,3- and α-2,6-sialyltransferases acting on lactosamine were unaffected. Our results show that a reduction in α-Galactose epitope expression in porcine endothelial cells transfected with human α-1,2-fucosyltransferase cDNA may be achieved but at the expense of considerable distortion of the overall cell surface glycosylation profile, including the appearance of carbohydrate epitopes that are absent from the parent cells.
Ragnar Lindstedt - One of the best experts on this subject based on the ideXlab platform.
-
Expression of α-1,3-Galactose and Other Type 2 Oligosaccharide Structures in a Porcine Endothelial Cell Line Transfected with Human α-1,2-Fucosyltransferase cDNA
The Journal of biological chemistry, 1997Co-Authors: Armin Sepp, Patricia Skacel, Ragnar Lindstedt, Robert I. LechlerAbstract:Abstract The binding of xenoreactive natural antibodies to the Galα1–3Galβ1–4GlcNAc (α-Galactose) Oligosaccharide epitope on pig cells activates the recipient’s complement system in pig to primate xenotransplantation. Expression of human α-1,2-fucosyltransferase in pigs has been proposed as a strategy for reducing the expression level of the α-Galactose epitope, thereby rendering the pig organs more suitable for transplantation into humans. The aim of this study was to examine how the cell surface expression of α-Galactose, H, and related fucosylated and sialylated structures on a pig liver endothelial cell line is affected by transfection of human α-1,2-fucosyltransferase cDNA. Nontransfected and mock-transfected cells expressed α-Galactose, α-2,3-sialylated, and α-2,6-sialylated epitopes strongly, with low level expression of type 2 H and LewisX. By contrast, expression of the H epitope was increased 5–8-fold in transfected cells with a 40% reduction in the expression of α-Galactose epitope and a 50% decrease in sialylation, as measured by binding of Maackia amurensis and Sambuccus nigra agglutinins. LewisX expression was reduced to background levels, while the LewisY neoepitope was induced in human α-1,2-fucosyltransferase-expressing pig cells. The activities of endogenous α-1,3-galactosyltransferase, α-1,3-fucosyltransferases, and α-2,3- and α-2,6-sialyltransferases acting on lactosamine were unaffected. Our results show that a reduction in α-Galactose epitope expression in porcine endothelial cells transfected with human α-1,2-fucosyltransferase cDNA may be achieved but at the expense of considerable distortion of the overall cell surface glycosylation profile, including the appearance of carbohydrate epitopes that are absent from the parent cells.
Wen-hua Wang - One of the best experts on this subject based on the ideXlab platform.
-
Separation of galacto-Oligosaccharides mixture by nanofiltration
Journal of the Taiwan Institute of Chemical Engineers, 2009Co-Authors: Y.m. Feng, Chang Xiulian, Wen-hua WangAbstract:Abstract Four commercial 1812 spiral wound nanofiltration membranes were firstly applied to examine the separation performance of sugar solutions in total recycle mode of operation. Membrane NF-3 (supplied by Sepro Co. (USA)) with molecular weight cut-off of 800–1000 Da was selected for separation of a commercial Galactose-Oligosaccharide (GOS) mixture with low content of Oligosaccharides in constant volume diafiltration (CVD) process at 50 °C and 6 bar pressure. The choosing of membrane and operation conditions for CVD process was based on a compromise between the permeate fluxes and apparent rejections of the sugar solution. In CVD course, the concentration of various sugars and the relationship between the yield and purity of Oligosaccharides predicted well with mathematical models for the following situation: when the volume of every removing batch of permeate is equal to the volume of tank, the increased rate of sugar rejections is less than 8% and the decreased rate of tank concentrations is less than 15%. 90.5% monosaccharide and 52.5% lactose in the mixture were removed with NF-3 membrane in this study, and the Oligosaccharides purity of 54.5% was achieved (1.5 times of the raw material), obtaining Oligosaccharides yield of 70.0%.
