Results 171 to 180 of about 56,362 (206)
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Lipid Rafts, Caveolae and GPI-Linked Proteins

2012
Lipid rafts and caveolae are specialized membrane microdomains enriched in sphingolipids and cholesterol. They function in a variety of cellular processes including but not limited to endocytosis, transcytosis, signal transduction and receptor recycling.
Reeves, V.L.   +2 more
openaire   +3 more sources

Phase partitioning detects differences between phospholipase-released forms of alkaline phosphatase — a GPI-linked protein

Biochimica et Biophysica Acta (BBA) - General Subjects, 1993
A number of enzymes are known to release alkaline phosphatase and other glycan phosphatidylinositol-anchored proteins from membrane surfaces. We describe a novel approach to detect and measure these activities by partitioning in aqueous phase systems. The procedures avoid the complications of micelle-formation involving hydrophobic molecules that may ...
F D, Raymond, D W, Moss, D, Fisher
openaire   +2 more sources

The presence of GPI-linked protein(s) in an archaeobacterium, Sulfolobus acidocaldarius, closely related to eukaryotes

Biochimica et Biophysica Acta (BBA) - General Subjects, 1997
GPI-anchored proteins are distributed ubiquitously in eukaryotes, but not in procaryotes. By metabolic-labeling of Sulfolobus acidocaldarius cells, 14C-radiolabeled precursors of GPI and caldarchaetidylinositol were incorporated into 120, 143 and 185 kDa proteins.
T, Kobayashi, R, Nishizaki, H, Ikezawa
openaire   +2 more sources

GPI-Linked Proteins Do Not Transfer Spontaneously from Erythrocytes to Liposomes. New Aspects of Reorganization of the Cell Membrane

Biochemistry, 2000
Exposure of cells to liposomes results in the release of integral membrane proteins. However, it is still controversial whether the release is due to spontaneous protein transfer from cells to liposomes or shed vesicles released from cells. We investigated this issue in an erythrocyte-liposome system by examining the location of acetylcholinesterase ...
K, Suzuki, Y, Okumura
openaire   +2 more sources

Two distinct patterns of glycosylphosphatidylinositol (GPI) linked protein deficiency in the red cells of patients with paroxysmal nocturnal haemoglobinuria

British Journal of Haematology, 1992
Summary.We have studied three glycosylphosphatidylinositol (GPI) linked proteins on the erythrocytes of 14 patients with paroxysmal nocturnal haemoglobinuria (PNH). The pattern observed was bimodal in 12 of the patients and trimodal in two. Ten patients had a red cell population with normal CD59 antigen (membrane inhibitor of reactive lysis, MIRL ...
P, Hillmen, J M, Hows, L, Luzzatto
openaire   +2 more sources

Investigating the role of murine epididymosomes and uterosomes in GPI‐linked protein transfer to sperm using SPAM1 as a model

Molecular Reproduction and Development, 2008
AbstractSperm uptake of glycosyl phosphatidylinositol (GPI)‐linked proteins from luminal fluids has been shown to occur in male and estrous female reproductive tracts. In males, this is attributed to membranous vesicles secreted into the epididymis and prostate. While epididymosomes have been characterized, there have been no reports of the presence of
Genevieve S, Griffiths   +3 more
openaire   +2 more sources

Mutations in the PIG‐A gene causing partial deficiency of GPI‐linked surface proteins (PNH II) in patients with paroxysmal nocturnal haemoglobinuria

British Journal of Haematology, 1994
SummaryParoxysmal nocturnal haemoglobinuria (PNH) is due to the absence or marked reduction of glycan phosphatidylinositol (GPI)‐anchored proteins on the surface of blood cells. Affected patients may have a population of red blood cells that are completely deficient (PNH III) or partially deficient (PNH II) in these proteins, or they may have both. PNH
M, Bessler   +3 more
openaire   +2 more sources

Deletion of the GPI pre-anchor sequence in human p97—a general approach for generating the soluble form of GPI-linked proteins

Protein Expression and Purification, 2004
Melanotransferrin, also named p97, belongs to the transferrin-like group of iron-binding proteins. Unlike the other members of this family, p97 exists in two forms-one soluble form and one attached to the cell membrane by a glycosylphosphatidylinositol (GPI) anchor.
Joseph, Yang   +3 more
openaire   +2 more sources

Mice with Blood Cells Deficient in GPI-linked Proteins — The Generation of a Murine Model to Investigate the Pathogenesis and Pathophysiology of Paroxysmal Nocturnal Hemoglobinuria (PNH)

2003
Clinical characteristics of PNH include anemia due to intravascular hemolysis and hemoglobinuria, complications caused by bone marrow failure, and recurrent thrombosis. Despite the cloning of the Piga gene and the recent insights into the molecular lesion that causes the loss of glycosyl phosphatidylinositol-(GPI) linked proteins, much of the ...
Monica Bessler   +5 more
openaire   +1 more source

Expression of GPI-linked Green Fluorescent Protein on the surface of CHO cells

Biochemical Society Transactions, 2000
S. Hiscox   +2 more
openaire   +1 more source

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