Inherited abnormalities of platelet glycoproteins

1981 ◽  
Vol 294 (1072) ◽  
pp. 281-290 ◽  
Keyword(s):  
Platelet Aggregation ◽  
Platelet Function ◽  
Membrane Glycoproteins ◽  
Blood Disorders ◽  
Glanzmann’S Thrombasthenia ◽  
Glanzmann's Thrombasthenia ◽  
Bernard Soulier Syndrome

Glanzmann’s thrombasthenia and the Bernard-Soulier syndrome are inherited blood disorders characterized by abnormalities in different aspects of platelet function during haemostasis. Platelets from patients with thrombasthenia do not aggregate in response to the normal physiological platelet aggregation inducing stimuli, while Bernard-Soulier platelets have a reduced capacity to adhere to exposed subendothelium. Deficiencies of different membrane glycoproteins have been located in the platelets of both disorders and suggest specific roles for membrane glycoproteins in different aspects of platelet function.

Platelet Membrane Glycoproteins and their Possible Relationship to the ADP Mechanism of Platelet Aggregation

1975 ◽  
Author(s):  
D. R. Phillips ◽  
C. S. P. Jenkins ◽  
D. Meyer ◽  
M.-J. Larrieu ◽  
E. F. Luscher
Keyword(s):  
Platelet Aggregation ◽  
Surface Structure ◽  
Marked Reduction ◽  
Membrane Surface ◽  
Platelet Membrane ◽  
Membrane Glycoproteins ◽  
Altered Expression ◽  
Glanzmann’S Thrombasthenia ◽  
Glanzmann's Thrombasthenia ◽  
Induced Aggregation

Platelets isolated from patients with Glanzmann’s Thrombasthenia release in the presence of thrombin and other stimuli but fail to respond to ADP. Since the iutia.l interaction, between the platelet and ADP is at the membrane surface, it would appear that this surface lacks the necessary receptor for ADP. The surface structure of normal and thrombasthenia platelets was compared using the lactoperoxidase iodination technique. Iodination of normal platelets results in the labelling of four glycoproteins, I, IIa IIb and III, with relative ratios of 1 : 1 : 1 : 3 plus other non-characterised polypeptides. Thrombasthenic platelets similarly treated revealed a drastically altered expression of the glycoproteins on the membrane. The relative ratios (1.5: 1:0.4:0.5) revealed the decrease of glycoprotein IIb and the marked reduction of glycoprotein III. Arguments and data will be presented which point to the possibility that glycoprotein IIb is involved in ADP-induced aggregation.

Antigenic Properties And Structure Of Membrane Glycoprotein Receptors

1981 ◽  
Author(s):  
T J Kunicki
Keyword(s):  
Platelet Aggregation ◽  
Platelet Adhesion ◽  
Membrane Glycoproteins ◽  
Glanzmann’S Thrombasthenia ◽  
Normal Platelet ◽  
Glanzmann's Thrombasthenia ◽  
Antigenic Properties ◽  
Normal Hemostasis ◽  
Triton X

Membrane glycoproteins (GP) IIb and IIIa are not detectable on the platelets of a majority (Type 1) of patients with Glanzmann’s thrombasthenia, a hereditary disorder of platelet function characterized by an absence of platelet-platelet adhesion. These platelets also do not express the human platelet alloantigen, PlA1, a finding which led to the demonstration that the PlA1 alloantigen is associated with GPIIIa, but not with GPIIb. Alloantibodies directed against the PlA1 determinant or certain other determinants associated with GPIIb and/or GPIIIa appear to be capable of inhibiting normal platelet- platelet adhesion, suggesting that these glycoproteins function as key mediators of this process, an obligate step in normal hemostasis. Subsequent studies have supported this hypothesis by demonstrating that fibrinogen, which is known to be a key cofactor in normal platelet aggregation, does not bind to thrombasthenic platelets.We have used crossed immunoelectrophoresis of Triton X-100 soluble membrane glycoproteins against a multispecific rabbit antibody to quantitate levels of GPIIb and GPIIIa on normal and thrombasthenic platelets and to study the interaction of these two glycoproteins in a soluble nondenatured state. These studies have provided information on 1) the inheritance of PlA1 and the glycoprotein IIb/IIIa defect in Glanzmann’s thrombasthenia, and 2) reversible Ca++-dependent changes in the orientation of GPIIb and GPIIIa, which may contribute to understanding of the function of these glycoproteins in normal platelet aggregation. In the presence of sufficient Ca++, glycoproteins IIb and IIIa were found to exist only in heterogenous complexes, whether within isolated membranes, or in solution. Chelation of Ca++ by EDTA or EGTA resulted in the dissociation of these glycoproteins; reassociation could be induced by readdition of excess Ca++.

ANTIBODIES AGAINST MEMBRANE GLYCOPROTEINS: AGGREGATION, CROSS IMMUNOELECTROPHORESIS STUDIES, AND RELEVANCE TO GLANZMANN’S THROMBASTHENIA

1981 ◽  
Author(s):  
C S P Jenkins ◽  
E F Ali-Briggs ◽  
K J Clemetson
Keyword(s):  
Platelet Aggregation ◽  
Marked Reduction ◽  
Membrane Glycoproteins ◽  
Clot Retraction ◽  
Glanzmann’S Thrombasthenia ◽  
Crossed Immunoelectrophoresis ◽  
Glanzmann's Thrombasthenia ◽  
Triton X ◽  
Induced Aggregation ◽  
Second Wave

In Glanzmann’s thrombasthenia, glycoproteins (GPs) IIb and IIIa are missing or strongly reduced in concentration and aggregation to ADP, collagen and thrombin is impaired. Antibodies against GPs IIb and IIIa did not entirely induce a thrombasthenia-like state in normal platelets; however they did strongly inhibit collagen-induced aggregation, inhibited the second wave of aggregation induced by ADP, inhibited to some extent thrombin-induced aggregation and clot retraction, and were totally without effect on ristocetin-human VIIIR:WF.Crossed immunoelectrophoresis studies using Triton X-100 extracts of whole platelets and platelet membranes with these antibodies gave a single immunoprecipitate. This immunoprecipitate was absent when similar studies were carried out with thrombasthenie platelets. Anti-whole platelets antibodies gave a number of immunoprecipitates with normal platelets and differences were observed with thrombasthenie platelets, the most notable of which was a marked reduction in one of the major immunoprecipitates.These results provide further evidence that GPs IIb and IIIa are involved in the later stages of platelet aggregation.

A Case Report on Glanzmann’s Thrombasthenia: A Rare Platelet Function Disorder

2018 ◽  
Vol 2 (02) ◽  
pp. 59-60
Author(s):  
Farida Yasmin ◽  
Md. Anwarul Karim ◽  
Chowdhury Yakub Jamal ◽  
Mamtaz Begum ◽  
Ferdousi Begum
Keyword(s):  
Case Report ◽  
Platelet Function ◽  
The Body ◽  
Presenting Symptoms ◽  
Glanzmann’S Thrombasthenia ◽  
Glanzmann's Thrombasthenia ◽  
Platelet Function Disorders ◽  
Recurrent Epistaxis ◽  
Severe Epistaxis ◽  
History Of

Epistaxis in children is one of the important presenting symptoms for attending emergency department in paediatric patients. Recurrent epistaxis is common in children. Although epistaxis in children usually occurred due to different benign conditions, it may be one of the important presenting symptoms of some inherited bleeding disorder. Whereas most bleeding disorders can be diagnosed through different standard hematologic assessments, diagnosing rare platelet function disorders may be challenging. In this article we describe one case report of platelet function disorders on Glanzmann’s thrombasthenia (GT). Our patient was a 10-year old girl who presented to us with history of recurrent severe epistaxis. She had a bruise on her abdomen and many scattered petechiae in different parts of the body. Her previous investigations revealed no demonstrable haemostatic anomalies. After performing platelet aggregation test, she was diagnosed as GT.

Acquired Glanzmann's thrombasthenia: Diagnosis aided by platelet aggregation mixing study

Haemophilia ◽  
2020 ◽  
Vol 26 (2) ◽  
Author(s):  
Frances Compton ◽  
Ravi Sarode ◽  
Cynthia Rutherford ◽  
Brian Curtis ◽  
Nicole De Simone
Keyword(s):  
Platelet Aggregation ◽  
Glanzmann’S Thrombasthenia ◽  
Glanzmann's Thrombasthenia

Absence of the Complete Platelet-Specific Alloantigens Zw (PlA) On Platelets in Glanzmann’S Thrombasthenia and the Effect of Anti-Zwa Antibody on Platelet-Function

1979 ◽  
Author(s):  
E.F. von Leeuwen ◽  
G.T.E. Zonneveld ◽  
L.E. von Riesz ◽  
C.S.P Jenkins ◽  
J.A. van Mourik ◽  
...  
Keyword(s):  
Platelet Function ◽  
Gel Electrophoresis ◽  
Family Members ◽  
Glanzmann’S Thrombasthenia ◽  
Platelet Membranes ◽  
Glanzmann's Thrombasthenia ◽  
The Family ◽  
Induced Aggregation ◽  
Aggregation Of Platelets ◽  
Slight Inhibition

The expression of the platelet-speciftc alloantigens on the platelets from 6 patients with Glanzmann’s Thrombasthenia (G.T.) and their nearest relatives was studied. The alloantigens Zwa (PIAl) and Zwb(PIA2) were found to be completely absent from thrombasthenic platelets while the alloantigens of the Ko-system were found to be normally expressed. The alloantigen Baka(phenotypefrequency 90.2%) was absent on the platelets from 4 studied G.T. patients. The platelets of all the family members reacted positively with anti-Zwa, negatively with antt-Zwb serum. SDS-PA gel electrophoresis of G.T. platelet membranes demonstrated a marked deficiency of the glycoproteins IIb and IIIa. Glycoprotein analysis of the platelet membranes from the family members of 3 of the 6 patients reveoled no apparent abnormalities.Pre-incubation with anti-Zwa containing plasma strongly inhibits ADP-and collagen induced aggregation of platelets from normal Zwa homozygous individuols with a slight inhibition of the aggregation induced by ristocetin. Zwa antibodies did not affect the functions of platelets from ZWb homozygous individuals. Thus binding of Zwa antibodies induces a thrombosthenis-like state.

scholarly journals Monocytes and platelets share the glycoproteins IIb and IIIa that are absent from both cells in Glanzmann's thrombasthenia type I

1983 ◽  
Vol 214 (2) ◽  
pp. 331-337 ◽  
Author(s):  
G Gogstad ◽  
Ø Hetland ◽  
N O Solum ◽  
H Prydz
Keyword(s):  
Platelet Membrane ◽  
Type I ◽  
Membrane Glycoproteins ◽  
Edta Treatment ◽  
Glanzmann’S Thrombasthenia ◽  
Glanzmann's Thrombasthenia

By means of an antiserum specific to the complex of the platelet membrane glycoproteins IIb and IIIa we demonstrate here that monocytes and purified monocyte membranes share these glycoproteins with platelets. The monocyte glycoprotein IIb-IIIa complex showed complete immunological identity with the platelet counterpart and, furthermore, dissociated after EDTA treatment exactly as did the platelet complex. In Glanzmann's thrombasthenia type I, monocytes as well as platelets lack this antigen completely.

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