Agglutination of like-charged red blood cells induced by binding of β2-glycoprotein I to outer cell surface

Lokar, Maruša; Urbanija, Jasna; Frank, Mojca; Hägerstrand, Henry; Rozman, B; Bobrowska-Hägerstrand, Malgorzata; Iglič, Aleš; Kralj‐Iglič, Veronika

doi:10.1016/j.bioelechem.2008.04.015

Cited by 12 publications

(13 citation statements)

References 45 publications

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“…9 One of the bridging proteins, which directly mediates attractive interactions between charged-charged, chargedneutral, and neutral-neutral phospholipid membranes, is β2GPI. 79,80 It was found that β2GPI binds to structures with negatively charged phospholipid molecules, thrombocytes, 81 erythrocytes, 80 and serum lipoproteins; 82,83 moreover, it binds to phospholipid layers with electrostatic and also hydrophobic interactions. 79,80,84 β2GPI has a positive ζ-potential of 17.80 mV.…”

Section: Discussionmentioning

confidence: 99%

“…79,80 It was found that β2GPI binds to structures with negatively charged phospholipid molecules, thrombocytes, 81 erythrocytes, 80 and serum lipoproteins; 82,83 moreover, it binds to phospholipid layers with electrostatic and also hydrophobic interactions. 79,80,84 β2GPI has a positive ζ-potential of 17.80 mV. Several domains of β2GPI are highly positively charged, 85,86 which probably contributes to binding to negatively charged TiO 2 surfaces.…”

Section: Discussionmentioning

confidence: 99%

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Binding of plasma proteins to titanium dioxide nanotubes with different diameters

Kulkarni

Flašker

Lokar

et al. 2015

IJN

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Titanium and titanium alloys are considered to be one of the most applicable materials in medical devices because of their suitable properties, most importantly high corrosion resistance and the specific combination of strength with biocompatibility. In order to improve the biocompatibility of titanium surfaces, the current report initially focuses on specifying the topography of titanium dioxide (TiO 2 ) nanotubes (NTs) by electrochemical anodization. The zeta potential (ζ-potential) of NTs showed a negative value and confirmed the agreement between the measured and theoretically predicted dependence of ζ-potential on salt concentration, whereby the absolute value of ζ-potential diminished with increasing salt concentrations. We investigated binding of various plasma proteins with different sizes and charges using the bicinchoninic acid assay and immunofluorescence microscopy. Results showed effective and comparatively higher protein binding to NTs with 100 nm diameters (compared to 50 or 15 nm). We also showed a dose-dependent effect of serum amyloid A protein binding to NTs. These results and theoretical calculations of total available surface area for binding of proteins indicate that the largest surface area (also considering the NT lengths) is available for 100 nm NTs, with decreasing surface area for 50 and 15 nm NTs. These current investigations will have an impact on increasing the binding ability of biomedical devices in the body leading to increased durability of biomedical devices.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Binding of plasma proteins to titanium dioxide nanotubes with different diameters

Kulkarni

Flašker

Lokar

et al. 2015

IJN

Self Cite

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“…In this case only the decrease of the deviatoric part of the bending energy of the attached rod-like proteins and their direct interaction energy may overcome the increase of the free energy due to decrease of the conﬁgurational (mixing) entropy, upon the lateral sorting of curved rod-like BAR domains, thereby stabilizing the nanotubular membrane protrusion [40,43-46]. An experimental evidence for membrane proteins that can stabilize and bend highly curved membrane regions is the appearance of a network of thin nanotubular connections [38,47-49]. These thin nanotubular connections can be seen using a phase contrast microscope upon the addition of β2-GPI molecules [47-49].…”

Section: Flexible or Semi-flexible Rod-like Proteinsmentioning

confidence: 99%

“…An experimental evidence for membrane proteins that can stabilize and bend highly curved membrane regions is the appearance of a network of thin nanotubular connections [38,47-49]. These thin nanotubular connections can be seen using a phase contrast microscope upon the addition of β2-GPI molecules [47-49]. One possible explanation to the observed increase in nanotube diameter (Fig.…”

Section: Flexible or Semi-flexible Rod-like Proteinsmentioning

confidence: 99%

Attachment of Rod-Like (BAR) Proteins and Membrane Shape

Kabaso¹,

Gongadze²,

Elter³

et al. 2011

MRMC

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Previous studies have shown that cellular function depends on rod-like membrane proteins, among them Bin/Amphiphysin/Rvs (BAR) proteins may curve the membrane leading to physiologically important membrane invaginations and membrane protrusions. The membrane shaping induced by BAR proteins has a major role in various biological processes such as cell motility and cell growth. Different models of binding of BAR domains to the lipid bilayer are described. The binding includes hydrophobic insertion loops and electrostatic interactions between basic amino acids at the concave region of the BAR domain and negatively charged lipids. To shed light on the elusive binding dynamics, a novel experiment is proposed to expand the technique of single-molecule AFM for the traction of binding energy of a single BAR domain.

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“…However, it is also possible that a change in the electrostatic attraction on the surface of the echinocyte membrane could potentially result in a blood clot in the circuit. 20) Consid- The results for blood pH, hold up (HU) ，the pressure gradient (PG) ，and red blood cell reduction rate (RRR) ．Increases in blood pH were similar under all the conditions tested (excluding the control condition) ，regardless of the volumes of NaHCO3 and albumin added. However, HU and PG increased, and RRR was greatest with NaHCO3 200.…”

Section: ⅳ．Discussionmentioning

confidence: 94%

Alkalemic conditions result in blood clotting in the circuit soon after initiating cardiopulmonary bypass

Soyama

Takahashi

Yoshida

et al. 2016

JJECT

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Purpose : This study investigated the relationship between blood clotting in the circuit soon after initiating cardiopulmonary bypass (CPB) and echinocytes that appear with alkalemia, using a recirculation circuit filled with heparinized bovine blood.Methods : Alkalemic conditions in the recirculation circuit were prepared by adding various concentrations of NaHCO 3 to the priming fluid. Albumin was also added to confirm its inhibitory effect on blood clotting. Blood pH, hold-up, the pressure gradient, and red blood cell (RBC) reduction rate were monitored. Blood clots were examined microscopically.Results : Although blood pH was elevated under all experimental conditions, clotting in the circuit increased with increased concentrations of HCO3 -. Albumin inhibited the clotting under the same alkalemic conditions. Microscopic findings revealed echinocytes in the blood clots.Conclusions : The shape of echinocytes was transformed by a reduction in the Donnan equilibrium ratio because of changes in pH inside and outside the RBC membrane. Blood clotting in the circuit soon after initiating CPB may be caused by echinocytes that appear under alkalemic conditions. This was inhibited by albumin, suggesting that the addition of albumin to the priming fluid may prevent such clotting in the circuit after initiating CPB.

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Agglutination of like-charged red blood cells induced by binding of β2-glycoprotein I to outer cell surface

Cited by 12 publications

References 45 publications

Binding of plasma proteins to titanium dioxide nanotubes with different diameters

Binding of plasma proteins to titanium dioxide nanotubes with different diameters

Attachment of Rod-Like (BAR) Proteins and Membrane Shape

Alkalemic conditions result in blood clotting in the circuit soon after initiating cardiopulmonary bypass

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