The glycosyl-phosphatidylinositol anchor of membrane proteins

Low, Martin G.

doi:10.1016/0304-4157(89)90014-2

Cited by 516 publications

(233 citation statements)

References 298 publications

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“…This technique was first developed by Brown and Rose [8] on the basis of reports that both glycosphingolipids [9] and multiple glycosyl-phosphatidylinositol (GPI)-anchored proteins [10][11][12][13] were essentially insoluble in certain non-ionic detergents such as Triton X-100. Because of their high lipid content, the resulting detergentinsoluble glycolipid-enriched fraction (DIG) floats to a low density during sucrose-density-gradient centrifugation.…”

Section: Introductionmentioning

confidence: 99%

Amyloid precursor protein, although partially detergent-insoluble in mouse cerebral cortex, behaves as an atypical lipid raft protein

Parkin

Turner

Hooper

1999

Biochemical Journal

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Lipid rafts are regions of the plasma membrane that are enriched in cholesterol, glycosphingolipids and acylated proteins, and which have been proposed as sites for the proteolytic processing of the Alzheimer's amyloid precursor protein (APP). Lipid rafts can be isolated on the basis of their insolubility in Triton X-100 at 4 mC, with the resulting low-density, detergent-insoluble glycolipid-enriched fraction (DIG) being isolated by flotation through a sucrose density gradient. The detergent-insolubility of APP in mouse cerebral cortex relative to a variety of DIG marker proteins (alkaline phosphatase, flotillin, F3 protein and prion protein) and non-DIG proteins (alkaline phosphodiesterase I, aminopeptidase A and clathrin) has been examined. Alkaline phosphatase, flotillin, F3 protein and the prion protein were present exclusively in the DIG region of the sucrose gradient over a range of protein\detergent ratios used to solubilize the membranes and displayed a characteristic enrichment in the lowdensity fraction as the protein\detergent ratio was decreased. In

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Section: Introductionmentioning

confidence: 99%

Amyloid precursor protein, although partially detergent-insoluble in mouse cerebral cortex, behaves as an atypical lipid raft protein

Parkin

Turner

Hooper

1999

Biochemical Journal

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“…They are expressed by different genes in intestine, in placenta and bones, and liver and kidneys [62]. They are highly polymorphic dimeric proteins made of homodimers, each monomer having a GPI anchor linked to the C-terminal group.…”

Section: Afm Detection Of Ap-gpi In Model Membranesmentioning

confidence: 99%

“…Analysis of the lipid anchor reveals large variations in the composition and linkages of the diacyl-or alkyl-acylglycerol moiety of GPI proteins [31,62,63]. For instance, the saturated acyl chains of variant surface glycoprotein VSG, Thy-1, renal membrane dipeptidase, and human folate binding protein contain 14, 16, 18, and 22 carbons, respectively [9,62,63].…”

Section: Predictable Consequences For Biomembranesmentioning

confidence: 99%

“…For instance, the saturated acyl chains of variant surface glycoprotein VSG, Thy-1, renal membrane dipeptidase, and human folate binding protein contain 14, 16, 18, and 22 carbons, respectively [9,62,63]. As pointed out in a recent review, we still know very little concerning the structures of side chains and lipid moieties on the large number of GPI proteins [66].…”

Section: Predictable Consequences For Biomembranesmentioning

confidence: 99%

“…Glycosylphosphatidylinositol-anchored proteins (GPI proteins) are eukaryotic exoplasmic membrane proteins that play very diverse biological functions including hydrolytic enzyme activity, transmembrane signaling, intracellular sorting and cell adhesion interaction [32,62,66]. Besides these biological functions, GPI proteins such as alkaline phosphatases (AP-GPI), 5′-nucleotidase, dipeptidase, aminopeptidase P, have been used primarily as markers of plasma membranes during their purification procedure [6,28,96].…”

Section: Introductionmentioning

confidence: 99%

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Characterizing the interactions between GPI-anchored alkaline phosphatases and membrane domains by AFM

Giocondi

Seantier

Dosset

et al. 2007

Pflugers Arch - Eur J Physiol

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In plasma membranes, most glycosylphosphatidylinositol-anchored proteins (GPI proteins) would be associated with ordered microdomains enriched in sphingolipids and cholesterol. Debates on the composition and the nano-or mesoscales organization of these membrane domains are still opened. This complexity of biomembranes explains the use, in the recent years, of both model systems and atomic force microscopy (AFM) approaches to better characterize GPI proteins/membranes interactions. So far, the studies have mainly been focused on alkaline phosphatases of intestinal (BIAP) or placental (PLAP) origins reconstituted in model systems. The data show that GPI-anchored alkaline phosphatases (AP-GPI) molecules inserted in supported membranes can be easily imaged by AFM, in physiological buffer. They are generally observed in the most ordered domains of model membranes under phase separation, i.e. presenting both fluid and ordered domains. This direct access to the membrane structure at a mesoscopic scale allows establishing the GPI protein induced changes in microdomains size. It provides direct evidence for the temperature-dependent distribution of a GPI protein between fluid and ordered membrane domains. Origins of reported differences in the behavior of BIAP and PLAP are discussed. Finally, advantages and limits of AFM in the study of GPI proteins/membrane domains interactions are presented in this review.

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Intestinal alkaline phosphatase of the fishCyprinus carpio: Regional distribution and membrane association

et al. 1997

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The distribution of alkaline phosphatase along the carp intestine and also its association to the enterocyte membrane have been studied in order to correlate them with the morphological features and functional specialization of the different intestine portions. The intestine was sectioned in seven segments and from each segment a butanol extract of intestinal alkaline phosphatase (IAP) was prepared. The enzyme activity, when expressed as a function of the mucosa or protein content of each segment showed a clear proximo-distal gradient. In addition, IAP was recovered in the precipitate after centrifugation of the homogenate, along the intestine, indicating that it is membrane associated protein. Also, when brush border membranes (BBM) were isolated, IAP was enriched 10-fold. Butanol extracted IAP from all segments exhibited three bands of activity when separated in PAGE-Triton X-100. The slowest migrating band showed a hydrophobic character as it was retained in a phenyl-Sepharose CL-4B column, whereas the other bands represent hydrophilic IAP found in the flow through of the column. Butanol extracted IAP from BBM rendered only one band with hydrophobic character in PAGE-Triton X-100, which could be converted to hydrophilic forms when incubated with phosphatidyl-inositol phospholipase C. These results clearly demonstrate, that in carp as well as in all other species studied, IAP is anchored to the membrane via a glycosyl-phosphatidylinositol. The high IAP content found in the first segment is consistent with the function of dephosphorylation of nutritional compounds proposed in higher vertebrates. The involvement of IAP in other physiological roles such as lipid absorption or protein internalization cannot be ruled out.

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The glycosyl-phosphatidylinositol anchor of membrane proteins

Cited by 516 publications

References 298 publications

Amyloid precursor protein, although partially detergent-insoluble in mouse cerebral cortex, behaves as an atypical lipid raft protein

Amyloid precursor protein, although partially detergent-insoluble in mouse cerebral cortex, behaves as an atypical lipid raft protein

Characterizing the interactions between GPI-anchored alkaline phosphatases and membrane domains by AFM

Intestinal alkaline phosphatase of the fishCyprinus carpio: Regional distribution and membrane association

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