PMID- 9668212
OWN - NLM
STAT- MEDLINE
DCOM- 19981117
LR  - 20131121
IS  - 0006-2979 (Print)
IS  - 0006-2979 (Linking)
VI  - 63
IP  - 6
DP  - 1998 Jun
TI  - Interaction of wheat germ agglutinin and concanavalin A with platelets. 
      Stimulation of platelet functional reactions and binding with membrane 
      glycoproteins.
PG  - 710-8
AB  - Effects of two lectins, wheat germ agglutinin (WGA) and concanavalin A (Con A), 
      on platelet functional reactions and interaction of lectins with the platelet 
      membrane glycoproteins (GPs) have been studied. Both lectins stimulated platelet 
      aggregation and secretion of serotonin from platelet dense granules. The effects 
      of WGA and Con A were blocked by specific sugars, N-acetyl-D-glucosamine and 
      alpha-methyl-D-mannopyranoside, respectively, by adenylate cyclase activator 
      prostaglandin E1, and by anti-GP IIb-IIIa monoclonal antibody (monAB), CRC64, 
      that inhibits platelet interaction with fibrinogen. The data indicate that both 
      lectins interacting with the carbohydrate moiety on the platelet surface 
      stimulated not passive agglutination but fibrinogen--GP IIb-IIIa-dependent 
      platelet aggregation which is coupled with the secretion from granules and 
      activation of the intracellular systems of signal transduction. However, there 
      were significant differences between the stimulatory effects of WGA and Con A. 
      WGA induced more pronounced and quick platelet aggregation and stimulated several 
      times higher serotonin secretion than Con A. In addition, adhesion studies showed 
      that plastic-adsorbed WGA appeared to be a nonadhesive substrate, whereas Con A 
      effectively stimulated platelet adhesion. Unlike Con A-induced platelet 
      aggregation, adhesion to Con A substrate was not inhibited by monAB CRC64, i.e., 
      was not dependent on GP IIb-IIIa--fibrinogen interaction. Binding of lectins with 
      major platelet GPs was studied using immobilized WGA and Con A and platelet 
      lysate as a source of GPs. Platelet lysate was incubated with immobilized lectins 
      and then binding of individual GPs was evaluated using specific mono- and 
      polyclonal antibodies. WGA binds with GP Ib and P-selectin but not with other GPs 
      tested. Interaction of Con A with platelet GPs was less specific. This lectin 
      binds with GP IIb-IIIa, GP Ib, GP IV, and P-selectin. Although GP Ib appeared to 
      be the main protein which bound WGA on platelet surface, anti-GP Ib antibodies 
      failed to affect WGA-induced platelet aggregation, but inhibited WGA-induced 
      agglutination of fixed platelets. Thus, interaction of the WGA with GP Ib could 
      not be considered as a major stimulus initiating WGA-dependent platelet 
      activation and aggregation.
FAU - Smirnova, I V
AU  - Smirnova IV
AD  - Institute of Biochemistry and Physiology of Plants and Microorganisms, Russian 
      Academy of Sciences, Saratov, 410015, Russia.
FAU - Khaspekova, S G
AU  - Khaspekova SG
FAU - Ignatov, V V
AU  - Ignatov VV
FAU - Mazurov, A V
AU  - Mazurov AV
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochemistry (Mosc)
JT  - Biochemistry. Biokhimiia
JID - 0376536
RN  - 0 (Platelet Membrane Glycoproteins)
RN  - 0 (Wheat Germ Agglutinins)
RN  - 11028-71-0 (Concanavalin A)
RN  - 333DO1RDJY (Serotonin)
SB  - IM
MH  - Blood Platelets/cytology/*drug effects/metabolism
MH  - Cell Adhesion/drug effects
MH  - Cell Membrane/drug effects/metabolism
MH  - Concanavalin A/*pharmacology
MH  - Humans
MH  - Platelet Activation/*drug effects
MH  - Platelet Aggregation/*drug effects
MH  - Platelet Membrane Glycoproteins/immunology/*metabolism
MH  - Protein Binding
MH  - Serotonin/metabolism
MH  - Wheat Germ Agglutinins/*pharmacology
EDAT- 1998/07/21 00:00
MHDA- 1998/07/21 00:01
CRDT- 1998/07/21 00:00
PHST- 1998/07/21 00:00 [pubmed]
PHST- 1998/07/21 00:01 [medline]
PHST- 1998/07/21 00:00 [entrez]
PST - ppublish
SO  - Biochemistry (Mosc). 1998 Jun;63(6):710-8.