The Experts below are selected from a list of 9957 Experts worldwide ranked by ideXlab platform
D Westaway - One of the best experts on this subject based on the ideXlab platform.
-
doppel is an n glycosylated Glycosylphosphatidylinositol anchored protein expression in testis and ectopic production in the brains ofprnp 0 0 mice predisposed to purkinje cell loss
Journal of Biological Chemistry, 2000Co-Authors: Gregory L Silverman, Stanley B Prusiner, Richard C Moore, Peter Mastrangelo, Ying Yang, Patrick Tremblay, Fred E Cohen, D WestawayAbstract:Abstract The Prnd gene encodes a homolog of the cellular prion protein (PrPC) called doppel (Dpl). Up-regulation of Prnd mRNA in two distinct lines of PrP gene ablated (Prnp 0/0) mice, designatedRcm0 and Ngsk, is associated with death of Purkinje cells. Using recombinant Dpl expressed in Escherichia coli and mouse neuroblastoma cells we demonstrate that wild type (wt) Dpl, like PrPC, adopts a predominantly α-helical conformation, forms intramolecular disulfide bonds, has twoN-linked oligosaccharides, and is presented on the cell surface via a Glycosylphosphatidylinositol anchor. Dpl protein was detected in testis of wt mice. Using Triton X-114 phase partitioning to enrich for Glycosylphosphatidylinositol-anchored proteins, Dpl was detected in brain samples from Rcm0 Prnp 0/0mice but was absent in equivalent samples from wt mice and ZrchI Prnp 0/0 mice, indicating that ectopic expression of this protein may cause cerebellar pathology in Rcm0 mice. Biochemical and structural similarities between PrPC and Dpl documented here parallel the observation that ataxic Ngsk Prnp 0/0 mice can be rescued by overexpression of wild-type PrP transgenes, and suggest that cell surface PrPC can antagonize the toxic effect of Dpl expressed in the central nervous system.
-
doppel is an n glycosylated Glycosylphosphatidylinositol anchored protein expression in testis and ectopic production in the brains ofprnp 0 0 mice predisposed to purkinje cell loss
Journal of Biological Chemistry, 2000Co-Authors: Gregory L Silverman, Stanley B Prusiner, Richard C Moore, Peter Mastrangelo, Ying Yang, Patrick Tremblay, Kefeng Qin, Frederick Cohen, D WestawayAbstract:The Prnd gene encodes a homolog of the cellular prion protein (PrPC) called doppel (Dpl). Up-regulation of Prnd mRNA in two distinct lines of PrP gene ablated (Prnp 0/0) mice, designatedRcm0 and Ngsk, is associated with death of Purkinje cells. Using recombinant Dpl expressed in Escherichia coli and mouse neuroblastoma cells we demonstrate that wild type (wt) Dpl, like PrPC, adopts a predominantly α-helical conformation, forms intramolecular disulfide bonds, has twoN-linked oligosaccharides, and is presented on the cell surface via a Glycosylphosphatidylinositol anchor. Dpl protein was detected in testis of wt mice. Using Triton X-114 phase partitioning to enrich for Glycosylphosphatidylinositol-anchored proteins, Dpl was detected in brain samples from Rcm0 Prnp 0/0mice but was absent in equivalent samples from wt mice and ZrchI Prnp 0/0 mice, indicating that ectopic expression of this protein may cause cerebellar pathology in Rcm0 mice. Biochemical and structural similarities between PrPC and Dpl documented here parallel the observation that ataxic Ngsk Prnp 0/0 mice can be rescued by overexpression of wild-type PrP transgenes, and suggest that cell surface PrPC can antagonize the toxic effect of Dpl expressed in the central nervous system.
Peter Overath - One of the best experts on this subject based on the ideXlab platform.
-
endocytosis of a Glycosylphosphatidylinositol anchored protein via clathrin coated vesicles sorting by default in endosomes and exocytosis via rab11 positive carriers
Molecular Biology of the Cell, 2003Co-Authors: Christoph G Grunfelder, Markus Engstler, Frank Weise, Heinz Schwarz, Yorkdieter Stierhof, Gareth W Morgan, Mark C Field, Peter OverathAbstract:Recently, proteins linked to Glycosylphosphatidylinositol (GPI) residues have received considerable attention both for their association with lipid microdomains and for their specific transport bet...
-
expression of a Glycosylphosphatidylinositol anchored trypanosoma brucei transferrin binding protein complex in insect cells
Proceedings of the National Academy of Sciences of the United States of America, 1994Co-Authors: Maliha Chaudhri, Dietmar Steverding, Dorothee Kittelberger, Sian Tjia, Peter OverathAbstract:Abstract The expression site-associated gene ESAG 6 was previously implicated in transferrin binding in the protozoan parasite Trypanosoma brucei. ESAG 6 and the closely related ESAG 7 of T. brucei strain AnTat1.3 have now been expressed in insect cells using the baculovirus expression system. Expression of ESAG 6 alone in insect cells gives rise to a glycosylated protein of approximately 52 kDa, which is cell surface-associated through a Glycosylphosphatidylinositol anchor at its C terminus. The ESAG 7 product of about 42 kDa is also glycosylated, but lacks the Glycosylphosphatidylinositol modification, and is located intracellularly. No transferrin-binding activity is observed when either ESAG is expressed independently. However, their expression results in a cell surface complex of ESAG 6 and 7 products that specifically binds transferrin. This shows that both ESAG 6 and 7 products are necessary and sufficient for binding to transferrin.
-
expression of a Glycosylphosphatidylinositol anchored trypanosoma brucei transferrin binding protein complex in insect cells
Proceedings of the National Academy of Sciences of the United States of America, 1994Co-Authors: Maliha Chaudhri, Dietmar Steverding, Dorothee Kittelberger, Sian Tjia, Peter OverathAbstract:Abstract The expression site-associated gene ESAG 6 was previously implicated in transferrin binding in the protozoan parasite Trypanosoma brucei. ESAG 6 and the closely related ESAG 7 of T. brucei strain AnTat1.3 have now been expressed in insect cells using the baculovirus expression system. Expression of ESAG 6 alone in insect cells gives rise to a glycosylated protein of approximately 52 kDa, which is cell surface-associated through a Glycosylphosphatidylinositol anchor at its C terminus. The ESAG 7 product of about 42 kDa is also glycosylated, but lacks the Glycosylphosphatidylinositol modification, and is located intracellularly. No transferrin-binding activity is observed when either ESAG is expressed independently. However, their expression results in a cell surface complex of ESAG 6 and 7 products that specifically binds transferrin. This shows that both ESAG 6 and 7 products are necessary and sufficient for binding to transferrin.
Gregory L Silverman - One of the best experts on this subject based on the ideXlab platform.
-
doppel is an n glycosylated Glycosylphosphatidylinositol anchored protein expression in testis and ectopic production in the brains ofprnp 0 0 mice predisposed to purkinje cell loss
Journal of Biological Chemistry, 2000Co-Authors: Gregory L Silverman, Stanley B Prusiner, Richard C Moore, Peter Mastrangelo, Ying Yang, Patrick Tremblay, Fred E Cohen, D WestawayAbstract:Abstract The Prnd gene encodes a homolog of the cellular prion protein (PrPC) called doppel (Dpl). Up-regulation of Prnd mRNA in two distinct lines of PrP gene ablated (Prnp 0/0) mice, designatedRcm0 and Ngsk, is associated with death of Purkinje cells. Using recombinant Dpl expressed in Escherichia coli and mouse neuroblastoma cells we demonstrate that wild type (wt) Dpl, like PrPC, adopts a predominantly α-helical conformation, forms intramolecular disulfide bonds, has twoN-linked oligosaccharides, and is presented on the cell surface via a Glycosylphosphatidylinositol anchor. Dpl protein was detected in testis of wt mice. Using Triton X-114 phase partitioning to enrich for Glycosylphosphatidylinositol-anchored proteins, Dpl was detected in brain samples from Rcm0 Prnp 0/0mice but was absent in equivalent samples from wt mice and ZrchI Prnp 0/0 mice, indicating that ectopic expression of this protein may cause cerebellar pathology in Rcm0 mice. Biochemical and structural similarities between PrPC and Dpl documented here parallel the observation that ataxic Ngsk Prnp 0/0 mice can be rescued by overexpression of wild-type PrP transgenes, and suggest that cell surface PrPC can antagonize the toxic effect of Dpl expressed in the central nervous system.
-
doppel is an n glycosylated Glycosylphosphatidylinositol anchored protein expression in testis and ectopic production in the brains ofprnp 0 0 mice predisposed to purkinje cell loss
Journal of Biological Chemistry, 2000Co-Authors: Gregory L Silverman, Stanley B Prusiner, Richard C Moore, Peter Mastrangelo, Ying Yang, Patrick Tremblay, Kefeng Qin, Frederick Cohen, D WestawayAbstract:The Prnd gene encodes a homolog of the cellular prion protein (PrPC) called doppel (Dpl). Up-regulation of Prnd mRNA in two distinct lines of PrP gene ablated (Prnp 0/0) mice, designatedRcm0 and Ngsk, is associated with death of Purkinje cells. Using recombinant Dpl expressed in Escherichia coli and mouse neuroblastoma cells we demonstrate that wild type (wt) Dpl, like PrPC, adopts a predominantly α-helical conformation, forms intramolecular disulfide bonds, has twoN-linked oligosaccharides, and is presented on the cell surface via a Glycosylphosphatidylinositol anchor. Dpl protein was detected in testis of wt mice. Using Triton X-114 phase partitioning to enrich for Glycosylphosphatidylinositol-anchored proteins, Dpl was detected in brain samples from Rcm0 Prnp 0/0mice but was absent in equivalent samples from wt mice and ZrchI Prnp 0/0 mice, indicating that ectopic expression of this protein may cause cerebellar pathology in Rcm0 mice. Biochemical and structural similarities between PrPC and Dpl documented here parallel the observation that ataxic Ngsk Prnp 0/0 mice can be rescued by overexpression of wild-type PrP transgenes, and suggest that cell surface PrPC can antagonize the toxic effect of Dpl expressed in the central nervous system.
Robert A Hegele - One of the best experts on this subject based on the ideXlab platform.
-
a novel mutation in gpihbp1 causes familial chylomicronemia syndrome
Journal of Clinical Lipidology, 2018Co-Authors: Martine Paquette, Robert A Hegele, Guillaume Pare, Alexis BaassAbstract:Familial chylomicronemia syndrome is characterized by severe elevation in serum triglycerides and an increased risk of acute pancreatitis. Although familial chylomicronemia syndrome is mainly caused by mutations in the lipoprotein lipase (LPL) gene, few causal mutations in other genes (ie, APOC2, APOA5, LMF1, and GPIHBP1) have also been reported. In this case report, we present the discovery of a novel mutation in the Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1) gene and discuss its pathogenicity through a familial segregation study.
-
homozygous missense mutation g56r in Glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1 gpi hbp1 in two siblings with fasting chylomicronemia mim 144650
Lipids in Health and Disease, 2007Co-Authors: Jian Wang, Robert A HegeleAbstract:Background Mice with a deleted Gpihbp1 gene encoding Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPI-HBP1) develop severe chylomicronemia. We screened the coding regions of the human homologue – GPIHBP1 – from the genomic DNA of 160 unrelated adults with fasting chylomicronemia and plasma triglycerides >10 mmol/L, each of whom had normal sequence of the LPL and APOC2 genes.
Stanley B Prusiner - One of the best experts on this subject based on the ideXlab platform.
-
doppel is an n glycosylated Glycosylphosphatidylinositol anchored protein expression in testis and ectopic production in the brains ofprnp 0 0 mice predisposed to purkinje cell loss
Journal of Biological Chemistry, 2000Co-Authors: Gregory L Silverman, Stanley B Prusiner, Richard C Moore, Peter Mastrangelo, Ying Yang, Patrick Tremblay, Fred E Cohen, D WestawayAbstract:Abstract The Prnd gene encodes a homolog of the cellular prion protein (PrPC) called doppel (Dpl). Up-regulation of Prnd mRNA in two distinct lines of PrP gene ablated (Prnp 0/0) mice, designatedRcm0 and Ngsk, is associated with death of Purkinje cells. Using recombinant Dpl expressed in Escherichia coli and mouse neuroblastoma cells we demonstrate that wild type (wt) Dpl, like PrPC, adopts a predominantly α-helical conformation, forms intramolecular disulfide bonds, has twoN-linked oligosaccharides, and is presented on the cell surface via a Glycosylphosphatidylinositol anchor. Dpl protein was detected in testis of wt mice. Using Triton X-114 phase partitioning to enrich for Glycosylphosphatidylinositol-anchored proteins, Dpl was detected in brain samples from Rcm0 Prnp 0/0mice but was absent in equivalent samples from wt mice and ZrchI Prnp 0/0 mice, indicating that ectopic expression of this protein may cause cerebellar pathology in Rcm0 mice. Biochemical and structural similarities between PrPC and Dpl documented here parallel the observation that ataxic Ngsk Prnp 0/0 mice can be rescued by overexpression of wild-type PrP transgenes, and suggest that cell surface PrPC can antagonize the toxic effect of Dpl expressed in the central nervous system.
-
doppel is an n glycosylated Glycosylphosphatidylinositol anchored protein expression in testis and ectopic production in the brains ofprnp 0 0 mice predisposed to purkinje cell loss
Journal of Biological Chemistry, 2000Co-Authors: Gregory L Silverman, Stanley B Prusiner, Richard C Moore, Peter Mastrangelo, Ying Yang, Patrick Tremblay, Kefeng Qin, Frederick Cohen, D WestawayAbstract:The Prnd gene encodes a homolog of the cellular prion protein (PrPC) called doppel (Dpl). Up-regulation of Prnd mRNA in two distinct lines of PrP gene ablated (Prnp 0/0) mice, designatedRcm0 and Ngsk, is associated with death of Purkinje cells. Using recombinant Dpl expressed in Escherichia coli and mouse neuroblastoma cells we demonstrate that wild type (wt) Dpl, like PrPC, adopts a predominantly α-helical conformation, forms intramolecular disulfide bonds, has twoN-linked oligosaccharides, and is presented on the cell surface via a Glycosylphosphatidylinositol anchor. Dpl protein was detected in testis of wt mice. Using Triton X-114 phase partitioning to enrich for Glycosylphosphatidylinositol-anchored proteins, Dpl was detected in brain samples from Rcm0 Prnp 0/0mice but was absent in equivalent samples from wt mice and ZrchI Prnp 0/0 mice, indicating that ectopic expression of this protein may cause cerebellar pathology in Rcm0 mice. Biochemical and structural similarities between PrPC and Dpl documented here parallel the observation that ataxic Ngsk Prnp 0/0 mice can be rescued by overexpression of wild-type PrP transgenes, and suggest that cell surface PrPC can antagonize the toxic effect of Dpl expressed in the central nervous system.