Lectin-Carbohydrate Interactions in Model and Biological Membrane Systems

Hoekstra, Dick; Düzgüneş, Nejat

doi:10.1007/978-1-4613-9362-7_6

Cited by 11 publications

(3 citation statements)

References 198 publications

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“…It can be readily envisaged that the bulky and strongly hydrated carbohydrate head group forming a protrusion on a membrane surface can act as a steric barrier which might be acting as a protective shield against peroxidant damage. Lateral phase separation or local clustering of glycolipids induced by glycolipid-lectin interaction can result in a substantial reorganization of the membrane component [21]. Such lectin induced reorganization may produce a perturbation or destabilization of the membrane making it more susceptible to free radical damage as is evident from experimental results.…”

Section: -Tmentioning

confidence: 99%

Carbohydrate induced modulation of cell membrane. VI. Binding of exogenous lectin induces susceptibility of erythrocytes to free radical damage: a spin label study

1997

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The oxidation of erythrocyte membrane has been widely used as a model to study the damage of biomembranes by free radicals. Whether binding of lectin to erythrocytes has any effect on peroxidant injury has never been studied. This study reports for the first time that crosslinking of erythrocyte surface glycoprotein by an exogenous lectin significantly enhances the susceptibility to membrane damage by free radicals, as evidenced by the increase in membrane fluidity measured by EPR using spin label and the increase in the amount of oxyhemoglobin liberated due to cell lysis.

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Section: -Tmentioning

confidence: 99%

Carbohydrate induced modulation of cell membrane. VI. Binding of exogenous lectin induces susceptibility of erythrocytes to free radical damage: a spin label study

1997

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“…Several sphingolipids have been shown to reappear at the plasma membrane by a recycling mechanism, after exogenous membrane insertion and subsequent internalization by endocytosis (Kok et al 1989;Pagano, 1989, 1990). In this respect glycolipids may be of special interest, since most species belonging to this class of lipids are thought to reside mainly in the outer leaflet of the plasma membrane, in accordance with their functions in cell surface recognition phenomena (Curatalo, 1987;Hakomori, 1981;Hoekstra and Düzgünes, 1989). Recently we have presented direct evidence that the neutral glycolipid glucosylceramide is sorted during inbound cellular trafficking, thus avoiding degradation in the lysosomal compartment (Kok et al 1991).…”

Section: Introductionmentioning

confidence: 99%

Recycling pathways of glucosylceramide in BHK cells: distinct involvement of early and late endosomes

Kok

Hoekstra

Eskelinen

et al. 1992

Journal of Cell Science

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Recycling pathways of the sphingolipid glucosylceramide were studied by employing a fluorescent analog of glucosylceramide, 6(-)[N-(7-nitro-2,1,3-benzoxadiazol-4-yl)amino]hexanoylglucosyl sphingosine (C6-NBD-glucosylceramide). Direct recycling of the glycolipid from early endosomes to the plasma membrane occurs, as could be shown after treating the cells with the microtubule-disrupting agent nocodazole, which causes inhibition of the glycolipid's trafficking from peripheral early endosomes to centrally located late endosomes. When the microtubuli are intact, at least part of the glucosylceramide is transported from early to late endosomes together with ricin. Interestingly, also N-(lissamine rhodamine B sulfonyl)phosphatidylethanolamine (N-Rh-PE), a membrane marker of the fluid-phase endocytic pathway, is transported to this endosomal compartment. However, in contrast to both ricin and N-Rh-PE, the glucosylceramide can escape from this organelle and recycle to the plasma membrane. Monensin and brefeldin A have little effect on this recycling pathway, which would exclude extensive involvement of early Golgi compartments in recycling. Hence, the small fraction of the glycolipid that colocalizes with transferrin (Tf) in the Golgi area might directly recycle via the trans-Golgi network. When the intracellular pH was lowered to 5.5, recycling was drastically reduced, in accordance with the impeding effect of low intracellular pH on vesicular transport during endocytosis and in the biosynthetic pathway. Our results thus demonstrate the existence of at least two recycling pathways for glucosylceramide and indicate the relevance of early endosomes in recycling of both proteins and lipids.

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“…Both animal and plant cell surfaces have exposed glycosyl moieties bound to either proteins or lipids (17). Internal membrane systems such as ER, Golgi apparatus, glyoxysomes, and mitochondria have been found to contain surfaceexposed sugar residues (19,28).…”

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confidence: 99%

Flow Cytometry of Spinach Chloroplasts

Schröder¹,

Petit²

1992

Plant Physiol.

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Intact spinach (Spinacia oleracea) chloroplasts, thylakoid membranes, and inside-out or right-side-out thylakoid vesicles have been characterized by flow cytometry with respect to forward angle light scatter, right angle light scatter, and chlorophyll fluorescence. Analysis of intact chloroplasts with respect to forward light scatter and the chlorophyll fluorescence parameter revealed the presence of truly "intact" and "disrupted" chloroplasts. The forward light scatter parameter, normally considered to reflect object size, was instead found to reflect the particle density. One essential advantage of flow cytometry is that additional parameters such as Ricinus communis agglutinin (linked to fluorescein isothiocyanate) fluorescence can be determined through logical conditions placed on bit-maps, amounting to an analytical purification procedure. In the present case, chloroplast subpopulations with fully preserved envelopes, thylakoid membrane, and inside-out or right-side-out thylakoid membranes vesicles can be distinguished. Flow cytometry is also a useful tool to address the question of availability of glycosyl moities on the membrane surfaces if one keeps in mind that organelle-to-organelle interactions could be partially mediated through a recognition process. A high specific binding of R. communis agglutinin and peanut lectin to the chloroplast envelope was detected. This showed that galactose residues were exposed and accessible to specific lectins on the chloroplast surface. No exposed glucose, fucose, or mannose residues could be detected by the appropriate lectins. Ricin binding to the intact chloroplasts caused a strong aggregation. Disruption of these aggregates by resuspension or during passage in the flow cytometer induced partial breakage of the chloroplasts. Only minor binding of R. communis agglutinin and peanut lectin to the purified thylakoid membranes was detected; the binding was found to be low for both inside-out and right-side-out vesicles of the thylakoid membranes.Among the tools available to characterize cellular compartments by morphological and functional criteria, flow cytometry occupies an important place. Advantages of this 1 W.P.S. was supported by the Federation of European Biochemical Societies and the Swedish Institute.

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Lectin-Carbohydrate Interactions in Model and Biological Membrane Systems

Cited by 11 publications

References 198 publications

Carbohydrate induced modulation of cell membrane. VI. Binding of exogenous lectin induces susceptibility of erythrocytes to free radical damage: a spin label study

Carbohydrate induced modulation of cell membrane. VI. Binding of exogenous lectin induces susceptibility of erythrocytes to free radical damage: a spin label study

Recycling pathways of glucosylceramide in BHK cells: distinct involvement of early and late endosomes

Flow Cytometry of Spinach Chloroplasts

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