GPI–Anchors: Structure and Functions

Eckert, Volker; Gerold, Peter; Schwarz, Ralph Τ.

doi:10.1002/9783527614738.ch12

Cited by 15 publications

(14 citation statements)

References 109 publications

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“…In these structures the membrane anchor is formed by two fatty acids from a phospholipid often with defined chain lengths for the individual species, for example C14:0 for the variable surface glycoprotein (VSG) of Trypanosoma brucei. Diacylglycerol, 1-alkyl-2-acylglycerol and monoacylglycerol have been identified as hydrophobic membrane-entering domains [107,108]. Moreover, diacylglycerol ceramide can serve as lipid part.…”

Section: Review Articlementioning

confidence: 99%

“…Actually, the occurrence of galactofuranose has been demonstrated in glycosyl inositolphosphoceramide and -phospholipids of T. cruzi and Leishmania species [111]. Since the anchor structures expose specific cleavage sites for (glycosyl) phosphatidylinositol phospholipases C [(G)PI-PLC] and glycosyl phosphatidylinositol phospholipases D (GPI-PLD), it is possible to convert the (glyco)protein part from membrane-bound to soluble form [108,112,113]. This selective release of certain membrane-associated proteins by a phospholipase was substantial evidence to describe this linkage type and to guide structural analysis [114,115].…”

Section: Review Articlementioning

confidence: 99%

See 1 more Smart Citation

Eukaryotic glycosylation: whim of nature or multipurpose tool?

Reuter¹,

Gabius²

1999

Cellular and Molecular Life Sciences (CMLS)

214

141

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Protein and lipid glycosylation is a ubiquitous phenomenon. The task of cataloguing the great structural variety of the glycan part has demanded considerable efforts over decades. This patient endeavor was imperative to discern the inherent rules of glycosylation which cannot affirm assumptions on a purely coincidental nature of this type of protein and lipid modification. These results together with theoretical considerations uncover a salient property of oligosaccharides. In comparison with amino acids and nucleotides, monosaccharides excel in their potential to serve as units of hardware for storing biological information. Thus, the view that glycan chains exclusively affect physiochemical properties of the conjugates is indubitably flawed. This original concept has been decisively jolted by the discovery of endogenous receptors (lectins) for distinct glycan epitopes which are as characteristic as a fingerprint or a signature for a certain protein (class) or cell type. Recent evidence documents that these binding proteins are even endowed with the capacity to select distinct low-energy conformers of the often rather flexible oligosaccharides, granting entry to a new level of regulation of ligand affinity by shifting conformer equilibria. The assessment of the details of this recognition by X-ray crystallography, nuclear magnetic resonance spectroscopy, microcalorimetry and custom-made derivatives is supposed to justify a guarded optimism in satisfying the need for innovative drug design in antiadhesion therapy, for example against viral or bacterial infections and unwanted inflammation. This review presents a survey of the structural aspects of glycosylation and of evidence to poignantly endorse the notion that carrier-attached glycan chains can partake in biological information transfer at the level of cell compartments, cells and organs.

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Section: Review Articlementioning

confidence: 99%

Section: Review Articlementioning

confidence: 99%

Eukaryotic glycosylation: whim of nature or multipurpose tool?

Reuter¹,

Gabius²

1999

Cellular and Molecular Life Sciences (CMLS)

214

141

View full text Add to dashboard Cite

show abstract

“…Differences in the susceptibility of protozoan, yeast and mammalian cells to the inhibitors of the GPI biosynthesis offers a new target for the development of new therapeutic agents against malaria [84][85][86][87]. Comprenhensive studies on GPI biosynthesis in Plasmodium might lead to the identification of parasite specific reaction of this pathway; particularly the inositol myristoylation is a unique feature of plasmodial GPIs to develop potent drugs [88].…”

Section: Glycophospatidyl Inositol (Gpi)mentioning

confidence: 99%

Current Status of Malaria Control

Tripathi¹,

Mishra²,

Dwivedi³

et al. 2005

CMC

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Malaria caused by Plasmodium parasites kills approximately 1-3 million people and causes disease in 300-500 million people annually throughout the world. The current approaches to curtail this disease include vector control, vaccination, immunotherapy and chemotherapy. The vector control is achieved by reducing vector density, interrupting their life cycle, and creating a barrier between the human host and mosquitoes. A number of vaccine candidates are being clinically tried and R&D effort in this direction is coming in a big way. Currently there are only limited safe drugs for the treatment of this disease, however, reports of emerging resistance against existing drugs warrant the introduction of new drugs, which are unlikely to come from pharmaceutical industries because of limited commercial opportunities. One of the most important current approaches to develop new drugs involves the synthesis of chemical libraries and evaluate them against most validated biochemical targets of malarial parasite. Although a number of such targets in antimalarial drug development are known today, yet only validated and selective biochemical targets including mitochondrial transport, glycolic pathway, folate pathway, proteases and heme metabolism, apicoplast metabolism, glycophospatidyl inositol, lipid metabolism (glycerophospholipids), peptidyl deformylase and oxidative stress in parasite-infected erythrocytes have been discussed here. The well known antimalarial drugs and different drug combinations for the treatment of malaria are also briefly reviewed. A survey of the recently discovered new molecules active against malaria has also been narrated. Lastly, the future of malaria chemotherapy and new directions emerging from literature has been elucidated.

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“…In 1985 these and other results were combined to establish a common mode of membrane attachment via a GPI anchor covalently bound to the C-terminus through ethanolamine [47]. Today, we know well over 100 proteins which are GPI-anchored (reviewed in [48,49,50,51,52,53,54]) and the structures of several GPI anchors have been elucidated, the first being that on the Trypanosoma brucei variant surface glycoprotein (VSG) [55,56]. All characterized GPI anchors share a common core of ethanolamine-PO 4 -6Man( α 1-2)Man( α1-6)Man(α1-4)GlcN(α1-6)myo-Ino-1-PO 4 -lipid.…”

Section: Scheme 3 Carbohydrate-peptide Linkages Found In O-glycoprotmentioning

confidence: 99%

Occurrence and Significance

Wittmann

2001

Glycoscience: Chemistry and Chemical Biology I–III

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GPI–Anchors: Structure and Functions

Cited by 15 publications

References 109 publications

Eukaryotic glycosylation: whim of nature or multipurpose tool?

Eukaryotic glycosylation: whim of nature or multipurpose tool?

Current Status of Malaria Control

Occurrence and Significance

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