The binding of polyvalent galactosides to the lectin Ricinus communis agglutinin 120 (RCA120): an ITC and SPR study

2011 ◽  
Vol 2 (7) ◽  
pp. 1552 ◽  
Author(s):  
Sebastian G. Spain ◽  
Neil R. Cameron
Keyword(s):  
Ricinus Communis ◽  
Ricinus Communis Agglutinin

Glycoprotein Ib Has a Partial Role in Platelet-von Willebrand Factor Collagen Interaction

1988 ◽  
Vol 60 (02) ◽  
pp. 182-187 ◽  
Author(s):  
Morio Aihara ◽  
Ken Tamura ◽  
Ryuko Kawarada ◽  
Keizou Okawa ◽  
Yutaka Yoshida
Keyword(s):  
Platelet Aggregation ◽  
Von Willebrand Factor ◽  
Ricinus Communis ◽  
Protein S ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Normal Plasma ◽  
Ricinus Communis Agglutinin ◽  
Von Willebrand ◽  
Willebrand Factor

SummaryThe adhesion of human fixed washed platelets (FWP) to collagen was decreased after treatment with Serratia marcescens protease (SP), which removed 95% of the glycocalicin from platelet membrane glycoprotein (GP) lb. However, the diminished adhesion of SP treated FWP to collagen could still be increased in the presence of purified von Willebrand factor (vWF). This ability of vWF to increase FWP adhesion to collagen is defined as collagen cofactor (CCo). The adhesion of FWP to collagen was not affected by a monoclonal antibody (MAb) to GP Ilb/IIIa (10E5), that inhibits ADP and collagen induced platelet aggregation. On the other hand, it was decreased by 50% by a MAb to GP lb (6D1), that inhibits ristocetin induced platelet aggregation. Adhesion of FWP in buffer to collagen was completely inhibited by Ricinus communis agglutinin I or concanavalin A, while Lens culinalis agglutinin and wheat germ agglutinin showed 50% inhibition. The FWP adhesion to collagen in the presence of vWF (normal plasma) was unaffected by MAbs to GP Ilb/IIIa (10E5, P2, HPL1) but was decreased to 32-38% by MAbs to GP lb (6D1, AN51, HPL11). A MAb to vWF (CLB-RAg 35), that inhibits ristocetin induced binding of vWF to platelets, decreased the CCo of normal plasma by 70%. The MAb, CLB-RAg 201, that inhibits the binding of vWF to collagen, completely inhibited the CCo of normal plasma. In conclusion, our data suggest that (1) GP lb has a partial role in FWP adhesion to collagen; (2) the binding of vWF to collagen is required for the expression of CCo; (3) CCo is partly mediated through GP lb; but (4) other platelet membrane protein(s) besides GP lb or GP Ilb/IIIa must also be involved in FWP-vWF-collagen interactions.

Further Studies on Aggregation of Platelet-Type von Willebrand’s Disease Platelets by Human von Willebrand Factor

1986 ◽  
Vol 55 (03) ◽  
pp. 338-341 ◽  
Author(s):  
H Takahashi ◽  
W Tatewaki ◽  
M Hanano ◽  
R Nagayama ◽  
A Shibata
Keyword(s):  
Von Willebrand Factor ◽  
Ricinus Communis ◽  
Divalent Cations ◽  
Peanut Agglutinin ◽  
Von Willebrand's Disease ◽  
Von Willebrand’S Disease ◽  
Ricinus Communis Agglutinin ◽  
Von Willebrand ◽  
Induced Aggregation ◽  
Willebrand Factor

SummaryPlatelet-type von Willebrand’s disease (vWD) is a bleeding disorder characterized by a heightened interaction between platelets and von Willebrand factor (vWF) as the result of an intrinsic platelet abnormality (probably in GPIb). Platelet aggregability was nearly normal in response to thrombin, wheat germ agglutinin and Ricinus communis agglutinin in this disorder. Unmodified platelets showed no aggregation upon the addition of peanut agglutinin. Partially purified human vWF induced little aggregation of washed patient platelets, but the aggregation was greatly enhanced in the presence of plasma devoid of vWF. Monoclonal antibodies directed against GPIb and GPIIb/IIIa as well as EDTA completely inhibited vWF-induced aggregation. These results indicate that human vWF induces aggregation of platelet-type vWD platelets in the presence of divalent cations and some plasma cofactor(s), and that both GPIb and GPIIb/IIIa are involved in this aggregation.

scholarly journals Relationship Between Ricinus Communis Agglutinin-1 Binding and Nucleolar Organizer Regions in Human Gliomas

1993 ◽  
Vol 33 (6) ◽  
pp. 345-349
Author(s):  
Shuji NIIKAWA ◽  
Akira HARA ◽  
Shinichi SHIRAKAMI ◽  
Wei ZHANG ◽  
Noboru SAKAI ◽  
...  
Keyword(s):  
Ricinus Communis ◽  
Nucleolar Organizer ◽  
Nucleolar Organizer Regions ◽  
Human Gliomas ◽  
Ricinus Communis Agglutinin

Characterization of a cDNA encoding ricin E, a hybrid ricin-Ricinus communis agglutinin gene from the castor plant Ricinus communis

1987 ◽  
Vol 9 (3) ◽  
pp. 287-295 ◽  
Author(s):  
Beth F. Ladin ◽  
Elizabeth E. Murray ◽  
Amy C. Halling ◽  
Kevin C. Halling ◽  
Nanda Tilakaratne ◽  
...  
Keyword(s):  
Ricinus Communis ◽  
Ricinus Communis Agglutinin ◽  
Castor Plant

The Specific Binding between Galactose Group and Ricinus Communis Agglutinin (RCA) Investigated with Microcantilever

2012 ◽  
Vol 531-532 ◽  
pp. 600-604
Author(s):  
Hui Yong Zhang ◽  
Ji Hu ◽  
Hui Min Liu
Keyword(s):  
Atomic Force Microscopy ◽  
Self Assembly ◽  
Control Experiment ◽  
Ricinus Communis ◽  
Specific Binding ◽  
Specific Interaction ◽  
Protein Layer ◽  
Force Microscopy ◽  
Atomic Force ◽  
Ricinus Communis Agglutinin

The specific recognization between galactose group and Ricinus Communis Agglutinin (RCA) was investigated by microcantilever. The gold side of the microcantilever was covalently bound with N-galactose, RCA and asialofetuin (ASF) via mixed self assembly monolayer of 11-mercaptoundecanoic acid and 6-mercaptohexanol, respectively. After adding RCA into the flowing cell, the deflection could be observed on the N-galactose or ASF modified microcantilever. Meanwhile, the deflection could also be observed after ASF bound to the RCA modified microcantilever. In order to prove that the deflection is caused by the specific interaction between the galactose group and RCA, bovine serum albumin (BSA) was introduced into the flowing cell as control experiment and no obvious deflection was observed. The specific interaction was also confirmed by the evidence that the bound protein layer can be mechanically removed with atomic force microscopy nanolithography technology.

Albumin and Ricinus communis agglutinin decrease endothelial permeability via interactions with matrix

1993 ◽  
Vol 265 (2) ◽  
pp. C439-C446 ◽  
Author(s):  
R. Qiao ◽  
A. Siflinger-Birnboim ◽  
H. Lum ◽  
C. Tiruppathi ◽  
A. B. Malik
Keyword(s):  
Endothelial Cell ◽  
Ricinus Communis ◽  
Endothelial Permeability ◽  
Microvascular Endothelial Cell ◽  
Unit Surface Area ◽  
Ulex Europaeus ◽  
Liquid Flux ◽  
Ricinus Communis Agglutinin ◽  
Pulmonary Microvascular Endothelial Cell ◽  
Relationship Of

We studied the effects of albumin and the lectin Ricinus communis agglutinin (RCA) on hydraulic conductivity (Lp) of bovine pulmonary microvascular endothelial cell monolayers (BPMVEC) because of the evidence that albumin and RCA can interfere with transendothelial albumin permeability (Siflinger-Birnboim, A., J. Schnitzer, H. Lum, F. Blumenstock, C. Shen, P. Del Vecchio, and A. Malik. J. Cell. Physiol. 149: 575-584, 1991). BPMVEC were seeded on microporous polycarbonate filters, and the liquid flux was measured by collecting effluent into a tubing of known inner diameter at transendothelial hydrostatic pressures (P) ranging from 5 to 20 cmH2O. Lp was calculated as the slope of the relationship of liquid flux per unit surface area (Jv) vs. P. Addition of RCA (50 micrograms/ml) or albumin (5 mg/ml) to the endothelial cell medium containing albumin-free Hanks' balanced saline solution (HBSS) decreased total Lp (expressed x 10(-6) cm.s-1 x cmH2O-1) from 17.2 +/- 3.6 during HBSS to 4.7 +/- 0.9 during albumin and 5.7 +/- 1.6 during RCA (P < 0.01 for both). The RCA effect, but not that of albumin, was prevented by the addition of D-galactose (0.1 M) (the cognate hapten monosaccharide of RCA). We determined the contribution of the extracellular matrix (ECM) in decreasing the Lp by obtaining ECM after treatment of the monolayers with 0.025 M NH4OH to detach endothelial cells from the ECM. Basal ECM Lp (expressed x 10(-6) cm.s-1 x cmH2O-1) was 57.0 +/- 15.3, and it decreased to 19.7 +/- 4.3 and 17.5 +/- 2.9 during RCA and albumin, respectively (P < 0.01 for both). In contrast, RCA and albumin did not alter the filter Lp values. Another lectin, Ulex europaeus agglutinin, and the protein immunoglobulin G had no effect on Lp values.(ABSTRACT TRUNCATED AT 250 WORDS)

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