A thermodynamic study of GPI-anchored and soluble form of alkaline phosphatase films at the air–water interface

Ronzon, Frédéric; Rieu, Jean-Paul; Chauvet, Jean-Paul; Roux, B.

doi:10.1016/j.jcis.2006.05.055

Cited by 13 publications

(6 citation statements)

References 51 publications

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“…By comparison, the GPI membrane anchor of human PLAP is made of 1- O -alkyl-2- O -acylglycerol, essentially 1- O -(C 18:0 )-alkyl-2- O -(C 18:1 ) acylglycero-3-phosphoinositol and 1- O -(C 16:0 )-alkyl-2- O -(C 18:0 ) acylglycero-3-phosphoinositol, and the existence of an anchor with three fatty acid residues has not been reported. Assuming that BIAP occupies an area of ∼45 nm 2 , at the surface of the bilayer and that each DPPC molecule in the gel phase occupies ∼47 Å 2 , − each BIAP dimer would cover ∼95 DPPC molecules. Considering the acyl composition, it seems also reasonable to assume that the area occupied by each glycosylphosphatidylinositol anchor in the bilayer is comparable to that of DPPC.…”

Section: Discussionmentioning

confidence: 99%

Remodeling of Ordered Membrane Domains by GPI-Anchored Intestinal Alkaline Phosphatase

et al. 2007

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Glycosylphosphatidyl-inositol (GPI)-anchored proteins preferentially localize in the most ordered regions of the cell plasma membrane. Acyl and alkyl chain composition of GPI anchors influence the association with the ordered domains. This suggests that, conversely, changes in the fluid and in the ordered domains lipid composition affect the interaction of GPI-anchored proteins with membrane microdomains. Validity of this hypothesis was examined by investigating the spontaneous insertion of the GPI-anchored intestinal alkaline phophatase (BIAP) into the solid (gel) phase domains of preformed supported membranes made of dioleoylphosphatidylcholine/dipalmitoylphosphatidylcholine (DOPC/DPPC), DOPC/sphingomyelin (DOPC/SM), and palmitoyloleoylphosphatidylcholine/SM (POPC/SM). Atomic force microscopy (AFM) showed that BIAP inserted in the gel phases of the three mixtures. However, changes in the lipid composition of membranes had a marked effect on the protein containing bilayer topography. Moreover, BIAP insertion was associated with a net transfer of phospholipids from the fluid to the gel (DOPC/DPPC) or from the gel to the fluid (POPC/SM) phases. For DOPC/SM bilayers, transfer of lipids was dependent on the homogeneity of the gel SM phase. The data strongly suggest that BIAP interacts with the most ordered lipid species present in the gel phases of phase-separated membranes. They also suggest that GPI-anchored proteins might contribute to the selection of their own microdomain environment.

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Section: Discussionmentioning

confidence: 99%

Remodeling of Ordered Membrane Domains by GPI-Anchored Intestinal Alkaline Phosphatase

et al. 2007

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“…Shortly after the first description of membrane anchorage of cell surface proteins by glycolipidic anchors and elucidation of their detailed structure [5,6,97,98], the possibility of their spontaneous release from and insertion into PM of donor and acceptor cells, respectively, has been raised [99][100][101]. Subsequently, both the release [102][103][104][105][106][107] and insertion [108][109][110][111][112][113][114][115] of GPI-APs were substantiated by cell biological findings that, however, did not address putative (patho)physiological implications for the cells and tissues involved.…”

Section: (Patho)physiological Role Of Intercellular Transfer Of Gpi-apsmentioning

confidence: 99%

Biological Role of the Intercellular Transfer of Glycosylphosphatidylinositol-Anchored Proteins: Stimulation of Lipid and Glycogen Synthesis

Müller

2022

IJMS

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Glycosylphosphatidylinositol-anchored proteins (GPI-APs), which are anchored at the outer leaflet of plasma membranes (PM) only by a carboxy-terminal GPI glycolipid, are known to fulfill multiple enzymic and receptor functions at the cell surface. Previous studies revealed that full-length GPI-APs with the complete GPI anchor attached can be released from and inserted into PMs in vitro. Moreover, full-length GPI-APs were recovered from serum, dependent on the age and metabolic state of rats and humans. Here, the possibility of intercellular control of metabolism by the intercellular transfer of GPI-APs was studied. Mutant K562 erythroleukemia (EL) cells, mannosamine-treated human adipocytes and methyl-ß-cyclodextrin-treated rat adipocytes as acceptor cells for GPI-APs, based on their impaired PM expression of GPI-APs, were incubated with full-length GPI-APs, prepared from rat adipocytes and embedded in micelle-like complexes, or with EL cells and human adipocytes with normal expression of GPI-APs as donor cells in transwell co-cultures. Increases in the amounts of full-length GPI-APs at the PM of acceptor cells as a measure of their transfer was assayed by chip-based sensing. Both experimental setups supported both the transfer and upregulation of glycogen (EL cells) and lipid (adipocytes) synthesis. These were all diminished by serum, serum GPI-specific phospholipase D, albumin, active bacterial PI-specific phospholipase C or depletion of total GPI-APs from the culture medium. Serum inhibition of both transfer and glycogen/lipid synthesis was counteracted by synthetic phosphoinositolglycans (PIGs), which closely resemble the structure of the GPI glycan core and caused dissociation of GPI-APs from serum proteins. Finally, large, heavily lipid-loaded donor and small, slightly lipid-loaded acceptor adipocytes were most effective in stimulating transfer and lipid synthesis. In conclusion, full-length GPI-APs can be transferred between adipocytes or between blood cells as well as between these cell types. Transfer and the resulting stimulation of lipid and glycogen synthesis, respectively, are downregulated by serum proteins and upregulated by PIGs. These findings argue for the (patho)physiological relevance of the intercellular transfer of GPI-APs in general and its role in the paracrine vs. endocrine (dys)regulation of metabolism, in particular. Moreover, they raise the possibility of the use of full-length GPI-APs as therapeutics for metabolic diseases.

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“…The presence of a hydrophobic moiety in the GPI-anchor gives an amphiphilic character to the enzyme, providing an interesting parameter to investigate the behavior of the enzyme at the air-water interface. Moreover, model membranes such as lipid Langmuir monolayers [3][4][5][6][7][8][9], lipid Langmuir-Blodgett films [10][11][12][13][14] and liposomes [15][16][17][18][19][20] have been applied to catalytic studies, and molecular organization of GPI-enzymes. In this context, it is worthwhile to investigate the role of the anchor in the enzyme stability in terms of its secondary structure when the enzyme is spread and compressed at the air-water interface.…”

Section: Introductionmentioning

confidence: 99%

Rat osseous plate alkaline phosphatase as Langmuir monolayer—An infrared study at the air–water interface

Caseli

Masui

Furriel

et al. 2008

Journal of Colloid and Interface Science

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A thermodynamic study of GPI-anchored and soluble form of alkaline phosphatase films at the air–water interface

Cited by 13 publications

References 51 publications

Remodeling of Ordered Membrane Domains by GPI-Anchored Intestinal Alkaline Phosphatase

Remodeling of Ordered Membrane Domains by GPI-Anchored Intestinal Alkaline Phosphatase

Biological Role of the Intercellular Transfer of Glycosylphosphatidylinositol-Anchored Proteins: Stimulation of Lipid and Glycogen Synthesis

Rat osseous plate alkaline phosphatase as Langmuir monolayer—An infrared study at the air–water interface

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