Interaction of glycophorin A with lectins as measured by surface plasmon resonance (SPR).

Krotkiewska, Bożena; Pasek, Marta; Krotkiewski, Hubert

doi:10.18388/abp.2002_3807

Cited by 19 publications

(6 citation statements)

References 26 publications

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“…Another physiological function of glycophorins involves the lectin receptors. Glycophorins are linked to several sialo-oligosaccharides, so several lectins, such as Psathyrella velutina lectin (PVL), wheat germ agglutinin (WGA), and others, interact with the oligosaccharide moiety of glycophorin [ 117 , 118 , 119 ].…”

Section: Physiological Function Of Human Glycophorinsmentioning

confidence: 99%

A Comprehensive Review of Our Current Understanding of Red Blood Cell (RBC) Glycoproteins

Aoki

2017

Membranes

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Human red blood cells (RBC), which are the cells most commonly used in the study of biological membranes, have some glycoproteins in their cell membrane. These membrane proteins are band 3 and glycophorins A–D, and some substoichiometric glycoproteins (e.g., CD44, CD47, Lu, Kell, Duffy). The oligosaccharide that band 3 contains has one N-linked oligosaccharide, and glycophorins possess mostly O-linked oligosaccharides. The end of the O-linked oligosaccharide is linked to sialic acid. In humans, this sialic acid is N-acetylneuraminic acid (NeuAc). Another sialic acid, N-glycolylneuraminic acid (NeuGc) is present in red blood cells of non-human origin. While the biological function of band 3 is well known as an anion exchanger, it has been suggested that the oligosaccharide of band 3 does not affect the anion transport function. Although band 3 has been studied in detail, the physiological functions of glycophorins remain unclear. This review mainly describes the sialo-oligosaccharide structures of band 3 and glycophorins, followed by a discussion of the physiological functions that have been reported in the literature to date. Moreover, other glycoproteins in red blood cell membranes of non-human origin are described, and the physiological function of glycophorin in carp red blood cell membranes is discussed with respect to its bacteriostatic activity.

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Section: Physiological Function Of Human Glycophorinsmentioning

confidence: 99%

A Comprehensive Review of Our Current Understanding of Red Blood Cell (RBC) Glycoproteins

Aoki

2017

Membranes

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“…SPR arises from coupling of the surface plasmon wave on a metal surface when irradiated with total internal reflection (TIR) evanescent waves under certain conditions [2,6]. SPR has emerged to be a promising sensing technique in the fields of chemistry, biomedicine, and environmental monitoring because surface plasmons are extremely sensitive to variations in the refractive index of the surrounding medium [6][7][8][9][10]. There are many operating platforms to excite SPR on the basis of the TIR mechanism using prisms, optical fibers, and photonic crystal fibers (PCF).…”

Section: Introductionmentioning

confidence: 99%

Symmetrical dual D-shape photonic crystal fibers for surface plasmon resonance sensing

Liu

et al. 2018

Opt. Express

233

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Symmetrical dual D-shape photonic crystal fibers (PCFs) for surface plasmon resonance (SPR) sensing are designed and analyzed by the finite element method (FEM). The performance of the sensor is remarkably enhanced by the directional power coupling between the two fibers. We study the influence of the structural parameters on the performance of the sensor as well as the relationship between the resonance wavelengths and analyze refractive indexes between 1.36 and 1.41. An average spectral sensitivity of 14660 nm/RIU can be achieved in this sensing range and the corresponding refractive index resolution is 6.82 × 10 RIU. The characteristics of a single D-shape PCF-SPR sensor with the same structural parameters are compared with those of the dual PCFs sensor and the latter has distinct advantages concerning the spectral sensitivity, resolution, amplitude sensitivity, and figure of merits (FOM).

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“…The modeling and computational methods are described in the Result section, with the theoretical predictions derived from the model calculation Similarly, from the results in Figs. 2C, 2D, 2G, and 2H, we concluded that most of the FITC-WGA presumably bound to glycophorin-A [Krotkiewska et al, 2002] was washed away together with phospholipid membrane whereas FITC-Con A was retained bound to Band 3 of the delipidated spectrin network.…”

Section: Computer Simulationmentioning

confidence: 87%

Forced extension of delipidated red blood cell cytoskeleton with little indication of spectrin unfolding

et al. 2012

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Force-extension curves obtained on intact human red blood cells (RBC) were compared with those of delipidated RBCs to assess the contribution of cytoskeletal flexibility to the extensibility of the intact membrane skeleton. The RBCs were first delipidated by treatment with phospholipase A₂; tensile properties of the exposed cytoskeletal structures were measured using an atomic force microscope (AFM). The AFM probes were modified either with the Band 3 specific lectin, concanavalin A, (Con A) or anti-F-actin antibody, to localize the point of interaction between the probe and the cytoskeleton. Extension of the spectrin-based cytoskeleton reached up to 2-3 μm with a force less than 70 pN without showing any force peaks before the final rupture of the adhesive bonds. Our interpretation of the result is that the spectrin-based network was slack enough to allow the observed degree of extension without unfolding the tetrameric spectrin molecules. The force-extension curves obtained either on Band 3-ankyrin loci or on junction nodes of the cytoskeleton were not significantly different. Experimental results were verified by computer simulation of pulling mechanics of a network model of the RBC cytoskeleton. Our experimental results are also in agreement with the theoretical prediction of Mirijanian and Voth [2008; Proc Natl Acad Sci USA 105:1204-1208].

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Interaction of glycophorin A with lectins as measured by surface plasmon resonance (SPR).

Cited by 19 publications

References 26 publications

A Comprehensive Review of Our Current Understanding of Red Blood Cell (RBC) Glycoproteins

A Comprehensive Review of Our Current Understanding of Red Blood Cell (RBC) Glycoproteins

Symmetrical dual D-shape photonic crystal fibers for surface plasmon resonance sensing

Forced extension of delipidated red blood cell cytoskeleton with little indication of spectrin unfolding

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