Platelet Membrane Glycoprotein 1b Beta Chain

2020 ◽  
Author(s):  
Keyword(s):  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Beta Chain ◽  
Platelet Membrane Glycoprotein

Molecular Basis and Clinical Aspects of Hereditary Megakaryocyte and Platelet Membrane Glycoprotein Disorders

1996 ◽  
Vol 16 (02) ◽  
pp. 114-138 ◽  
Author(s):  
R. E. Scharf
Keyword(s):  
Genetic Basis ◽  
Molecular Mechanisms ◽  
Molecular Genetic ◽  
Platelet Membrane ◽  
Clinical Aspects ◽  
Membrane Glycoprotein ◽  
Membrane Glycoproteins ◽  
Membrane Expression ◽  
Receptor Complexes ◽  
Platelet Membrane Glycoprotein

SummarySpecific membrane glycoproteins (GP) expressed by the megakaryocyte-platelet system, including GPIa-lla, GPIb-V-IX, GPIIb-llla, and GPIV are involved in mediat-ing platelet adhesion to the subendothelial matrix. Among these glycoproteins, GPIIb-llla plays a pivotal role since platelet aggregation is exclusively mediated by this receptor and its interaction with soluble macromolecular proteins. Inherited defects of the GPIIb-llla or GPIb-V-IX receptor complexes are associated with bleeding disorders, known as Glanzmann's thrombasthenia, Bernard-Soulier syndrome, or platelet-type von Willebrand's disease, respectively. Using immuno-chemical and molecular biology techniques, rapid advances in our understanding of the molecular genetic basis of these disorders have been made during the last few years. Moreover, analyses of patients with congenital platelet membrane glycoprotein abnormalities have provided valuable insights into molecular mechanisms that are required for structural and functional integrity, normal biosynthesis of the glycoprotein complexes and coordinated membrane expression of their constituents. The present article reviews the current state of knowledge of the major membrane glycoproteins in health and disease. The spectrum of clinical bleeding manifestations and established diagnostic criteria for each of these dis-orders are summarized. In particular, the variety of molecular defects that have been identified so far and their genetic basis will be discussed.

scholarly journals Structure of the platelet membrane glycoprotein IIb. Homology to the alpha subunits of the vitronectin and fibronectin membrane receptors.

1987 ◽  
Vol 262 (18) ◽  
pp. 8476-8482 ◽  
Author(s):  
M Poncz ◽  
R Eisman ◽  
R Heidenreich ◽  
S M Silver ◽  
G Vilaire ◽  
...  
Keyword(s):  
Platelet Membrane ◽  
Membrane Receptors ◽  
Membrane Glycoprotein ◽  
Alpha Subunits ◽  
Platelet Membrane Glycoprotein

scholarly journals Alternative proteolytic processing of platelet membrane glycoprotein IIb.

1988 ◽  
Vol 263 (23) ◽  
pp. 11025-11028 ◽  
Author(s):  
J C Loftus ◽  
E F Plow ◽  
L K Jennings ◽  
M H Ginsberg
Keyword(s):  
Proteolytic Processing ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Platelet Membrane Glycoprotein

Divalent cation-dependent structure in the platelet membrane glycoprotein Ia–IIa (VLA-2) complex

1990 ◽  
Vol 168 (1) ◽  
pp. 107-113 ◽  
Author(s):  
William D. Staatz ◽  
Karen J. Peters ◽  
Samuel A. Santoro
Keyword(s):  
Divalent Cation ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Platelet Membrane Glycoprotein

Thrombin interaction with platelet membrane glycoprotein Ibα

2003 ◽  
Vol 9 (11) ◽  
pp. 461-464 ◽  
Author(s):  
Frédéric Adam ◽  
Marie-Christine Bouton ◽  
Marie-Geneviève Huisse ◽  
Martine Jandrot-Perrus
Keyword(s):  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Platelet Membrane Glycoprotein

scholarly journals Residual amounts of glycoprotein Ib concomitant with near-absence of glycoprotein IX in platelets of Bernard-Soulier patients

Blood ◽  
1988 ◽  
Vol 72 (3) ◽  
pp. 1086-1088 ◽  
Author(s):  
J Drouin ◽  
JL McGregor ◽  
S Parmentier ◽  
CA Izaguirre ◽  
KJ Clemetson
Keyword(s):  
Normal Level ◽  
Polyclonal Antibodies ◽  
Band Pattern ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Glycoprotein Ib ◽  
Gene Deletions ◽  
Immunoblot Assay ◽  
Platelet Membrane Glycoprotein ◽  
Bernard Soulier Syndrome

A study of the Bernard-Soulier syndrome in two unrelated families using different polyclonal antibodies in a sensitive immunoblot assay showed residual amounts of platelet membrane glycoprotein (GP) lb in the eight homozygotes, as well as the near-absence of GPlb beta and GPIX. The eight heterozygotes studied showed a double band pattern for GPlb and about half the normal level of GPlb beta and GPIX. Therefore, we conclude that the Bernard-Soulier syndrome is heterogeneous and is probably not due to gene deletions.

scholarly journals Expression and Functional Characterization of an Abnormal Platelet Membrane Glycoprotein Ibα (Met239 → Val) Reported in Patients With Platelet-Type von Willebrand Disease

Blood ◽  
1997 ◽  
Vol 90 (2) ◽  
pp. 698-705 ◽  
Author(s):  
Takanori Moriki ◽  
Mitsuru Murata ◽  
Tetsuya Kitaguchi ◽  
Hironobu Anbo ◽  
Makoto Handa ◽  
...  
Keyword(s):  
Platelet Aggregation ◽  
Platelet Rich Plasma ◽  
Functional Characterization ◽  
Point Mutations ◽  
Von Willebrand Disease ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Functional Abnormality ◽  
Platelet Membrane Glycoprotein ◽  
Von Willebrand

Abstract Platelet-type von Willebrand disease (vWD) is a congenital bleeding disorder characterized by heightened ristocetin-induced platelet aggregation caused by abnormally high affinity between the platelet membrane glycoprotein (GP) Ib/IX complex and von Willebrand factor (vWF ). Two distinct point mutations, Gly233 to Val and Met239 to Val, have been reported in GPIbα. We have constructed a recombinant GPIbα fragment containing the latter mutation, Met239 to Val (M239V) and characterized the mutant molecule using two methods, ie, interaction between soluble vWF and immobilized M239V and inhibition of platelet aggregation by purified soluble M239V. Spontaneous binding (ie, binding without any inducers) was observed between 125I-vWF and immobilized M239V but not between 125I-vWF and immobilized wild-type (WT) GPIbα. The addition of low concentrations of ristocetin (0.2 mg/mL) induced specific 125I-vWF binding to immobilized M239V, but not to WT GPIbα. At high concentrations of ristocetin (1.2 mg/mL), both WT GPIbα and M239V specifically bound to 125I-vWF. Thus, M239V reproduced the unique functional abnormality of the GPIb/IX complex in platelet-type vWD. Moreover, the purified soluble M239V inhibited platelet aggregation induced by low concentration of ristocetin (0.3 mg/mL) in platelet-rich plasma from a patient having Met239 to Val mutation, whereas purified WT did not. These results provide direct evidences that the reported point mutation is the responsible molecular basis of this disorder.

scholarly journals Characteristics of quinine- and quinidine-induced antibodies specific for platelet glycoproteins IIb and IIIa

Blood ◽  
1991 ◽  
Vol 77 (12) ◽  
pp. 2668-2676 ◽  
Author(s):  
GP Visentin ◽  
PJ Newman ◽  
RH Aster
Keyword(s):  
Immune Response ◽  
Platelet Membrane ◽  
The Other ◽  
Membrane Glycoprotein ◽  
Igg Antibodies ◽  
Drug Induced ◽  
Disulfide Bonding ◽  
Platelet Membrane Glycoprotein ◽  
Drug Dependent

Abstract Recent studies have shown that antibodies characteristic of quinine- and quinidine-induced thrombocytopenia sometimes recognize the platelet membrane glycoprotein (GP) complex IIb/IIIa in addition to their well known target, GPIb/IX. We have investigated the frequency with which drug-induced antibodies bind to GPIIb/IIIa and the nature of their target epitopes. In studies of sera from 13 patients sensitive to quinidine or quinine, we found that 10 contained IgG antibodies specific for both GPIb/IX and GPIIb/IIIa, two reacted with GPIb/IX alone, and one reacted with GPIIb/IIIa alone. In all cases, the presence of drug was required for binding of IgG to target GPs. By immunoabsorption, we found that each of five polyspecific sera contained at least two different antibodies, one reactive with GPb/IX and the other with GPIIb/IIIa. Further studies with eight drug- dependent antibodies (DDAb) specific for GPIIb/IIIa showed that three recognized the GPIIb/IIIa complex only, one recognized GPIIb alone, and three recognized GPIIIa alone. The eighth serum appeared to bind to both GPIIIa alone and to an epitope determined by the GPIIb/IIIa complex. The three antibodies specific for GPIIIa alone also reacted with GPIIIa deglycosylated with endo-H, and with the major (61 Kd) fragment obtained by chymotryptic digestion of GPIIIa but failed to react with reduced GPIIIa. These findings demonstrate that, in drug- induced, immunologic thrombocytopenia, the anti-platelet immune response is typically directed against epitopes on both GPIb/IX and GPIIb/IIIa. The three DDAb we studied that were specific for GPIIIa alone recognize epitopes resistant to chymotrypsin and endo-H treatment that are dependent on intrachain disulfide bonding.

scholarly journals Immunologic relationship between platelet membrane glycoprotein GPIIb/IIIa and cell surface molecules expressed by a variety of cells.

1986 ◽  
Vol 83 (16) ◽  
pp. 6002-6006 ◽  
Author(s):  
E. F. Plow ◽  
J. C. Loftus ◽  
E. G. Levin ◽  
D. S. Fair ◽  
D. Dixon ◽  
...  
Keyword(s):  
Cell Surface ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Cell Surface Molecules ◽  
Surface Molecules ◽  
Platelet Membrane Glycoprotein
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