Variations on Fibrinogen-Erythrocyte Interactions during Cell Aging

被引:41
作者
Carvalho, Filomena A. [1 ]
de Oliveira, Sofia [1 ]
Freitas, Teresa [1 ]
Goncalves, Sonia [1 ]
Santos, Nuno C. [1 ]
机构
[1] Univ Lisbon, Fac Med, Inst Mol Med, P-1699 Lisbon, Portugal
关键词
RED-BLOOD-CELLS; MOLECULAR RECOGNITION; GOLD NANOPARTICLES; FORCE SPECTROSCOPY; BINDING-SITES; SIALIC-ACID; MEMBRANE; CENTRIFUGATION; AGGREGATION; POPULATIONS;
D O I
10.1371/journal.pone.0018167
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
070301 [无机化学]; 070403 [天体物理学]; 070507 [自然资源与国土空间规划学]; 090105 [作物生产系统与生态工程];
摘要
Erythrocyte hyperaggregation, a cardiovascular risk factor, is considered to be caused by an increase in plasma adhesion proteins, particularly fibrinogen. We have recently reported a specific binding between fibrinogen and an erythrocyte integrin receptor with a beta(3) or beta(3)-like subunit. In this study we evaluate the influence of erythrocyte aging on the fibrinogen binding. By atomic force microscopy-based force spectroscopy measurements we found that increasing erythrocyte age, there is a decrease of the binding to fibrinogen by decreasing the frequency of its occurrence but not its force. This observation is reinforced by zeta-potential and fluorescence spectroscopy measurements. We conclude that upon erythrocyte aging the number of fibrinogen molecules bound to each cell decreases significantly, due to the progressive impairment of the specific fibrinogen-erythrocyte receptor interaction. Knowing that younger erythrocytes bind more to fibrinogen, we could presume that this population is the main contributor to the cardiovascular diseases associated with increased fibrinogen content in blood, which could disturb the blood flow. Our data also show that the sialic acids exposed on the erythrocyte membrane contribute for the interaction with fibrinogen, possibly by facilitating its binding to the erythrocyte membrane receptor.
引用
收藏
页数:8
相关论文
共 33 条
[1]
ALDERMAN EM, 1980, BLOOD, V55, P817
[2]
Chemical modifications of AFM tips for the study of molecular recognition events [J].
Barattin, Regis ;
Voyer, Normand .
CHEMICAL COMMUNICATIONS, 2008, (13) :1513-1532
[3]
BOSCH FH, 1992, BLOOD, V79, P254
[4]
Cellular and molecular mechanisms of senescent erythrocyte phagocytosis by macrophages. A review [J].
Bratosin, D ;
Mazurier, J ;
Tissier, JP ;
Estaquier, J ;
Huart, JJ ;
Ameisen, JC ;
Aminoff, D ;
Montreuil, J .
BIOCHIMIE, 1998, 80 (02) :173-195
[5]
Probing BSA binding to citrate-coated gold nanoparticles and surfaces [J].
Brewer, SH ;
Glomm, WR ;
Johnson, MC ;
Knag, MK ;
Franzen, S .
LANGMUIR, 2005, 21 (20) :9303-9307
[6]
Atomic Force Microscopy-Based Molecular Recognition of a Fibrinogen Receptor on Human Erythrocytes [J].
Carvalho, Filomena A. ;
Connell, Simon ;
Miltenberger-Miltenyi, Gabriel ;
Pereira, Sonia Vale ;
Tavares, Alice ;
Ariens, Robert A. S. ;
Santos, Nuno C. .
ACS NANO, 2010, 4 (08) :4609-4620
[7]
CHEN XY, 2007, CURRENT APPL PHYS, V7, pE94, DOI DOI 10.1016/J.CAP.2006.11.024
[8]
Force spectroscopy of the fibrin(ogen) - Fibrinogen interaction [J].
Chtcheglova, Lilia A. ;
Haeberli, Andre ;
Dietler, Giovanni .
BIOPOLYMERS, 2008, 89 (04) :292-301
[9]
SENESCENCE OF RED BLOOD-CELLS - PROGRESS AND PROBLEMS [J].
CLARK, MR .
PHYSIOLOGICAL REVIEWS, 1988, 68 (02) :503-554
[10]
Alteration of α-spectrin ubiquitination due to age-dependent changes in the erythrocyte membrane [J].
Corsi, D ;
Paiardini, M ;
Crinelli, R ;
Bucchini, A ;
Magnani, M .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1999, 261 (03) :775-783