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(Patho)Physiology of glycosylphosphatidylinositol-anchored proteins I: localization at plasma membranes and extracellular compartments.
Biomolecules 13:41 (2023)
Glycosylphosphatidylinositol (GPI)-anchored proteins (APs) are anchored at the outer leaflet of plasma membranes (PMs) of all eukaryotic organisms studied so far by covalent linkage to a highly conserved glycolipid rather than a transmembrane domain. Since their first description, experimental data have been accumulating for the capability of GPI-APs to be released from PMs into the surrounding milieu. It became evident that this release results in distinct arrangements of GPI-APs which are compatible with the aqueous milieu upon loss of their GPI anchor by (proteolytic or lipolytic) cleavage or in the course of shielding of the full-length GPI anchor by incorporation into extracellular vesicles, lipoprotein-like particles and (lyso)phospholipid- and cholesterol-harboring micelle-like complexes or by association with GPI-binding proteins or/and other full-length GPI-APs. In mammalian organisms, the (patho)physiological roles of the released GPI-APs in the extracellular environment, such as blood and tissue cells, depend on the molecular mechanisms of their release as well as the cell types and tissues involved, and are controlled by their removal from circulation. This is accomplished by endocytic uptake by liver cells and/or degradation by GPI-specific phospholipase D in order to bypass potential unwanted effects of the released GPI-APs or their transfer from the releasing donor to acceptor cells (which will be reviewed in a forthcoming manuscript).
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Times Cited
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5.500
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Publication type
Article: Journal article
Document type
Review
Keywords
(g)pi-specific Phospholipase D (gpld1) ; Adipose Cells ; Extracellular Vesicles ; Glycosylphosphatidylinositol (gpi)-anchored Proteins (gpi-aps) ; Metabolic Diseases ; Protein Release ; Sulfonylurea Drugs; Phosphatidylinositol-specific Phospholipase; Intestinal Alkaline-phosphatase; Decay-accelerating Factor; Angiotensin-converting Enzyme; Variant Surface Glycoprotein; Human-erythrocyte Acetylcholinesterase; Inhibitor Protectin Cd59; Fibroblast-growth-factor; Rat Adipocytes Depends; Colon-cancer-cells
Language
english
Publication Year
2023
HGF-reported in Year
2023
ISSN (print) / ISBN
2218-273X
e-ISSN
2218-273X
Journal
Biomolecules
Quellenangaben
Volume: 13,
Issue: 5,
Article Number: 41
Publisher
MDPI
Publishing Place
Basel
Reviewing status
Peer reviewed
Institute(s)
Institute of Diabetes and Obesity (IDO)
POF-Topic(s)
90000 - German Center for Diabetes Research
Research field(s)
Helmholtz Diabetes Center
PSP Element(s)
G-501900-221
Grants
European Research Council ERC-CoG Trusted
German Center for Diabetes Research (DZD e.V.)
German Research Foundation (DFG)
European Research Council ERC-CoG Trusted
German Center for Diabetes Research (DZD e.V.)
German Research Foundation (DFG)
WOS ID
000995593900001
Scopus ID
85160380452
PubMed ID
37238725
Erfassungsdatum
2023-10-06