Studies on a patient with thrombocytopenia, giant platelets and a platelet membrane glycoprotein Ib with reduced amount of sialic acid

1990 ◽  
Vol 74 (3) ◽  
pp. 320-329 ◽  
Author(s):  
A. M. Aakhus ◽  
P. Stavem ◽  
T. Hovig ◽  
T. M. Pedersen ◽  
N. O. Solum
Keyword(s):  
Sialic Acid ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Glycoprotein Ib ◽  
Giant Platelets ◽  
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.

Binding of Heparin to Platelet Membrane Glycoprotein Ib: Functional Effects

1999 ◽  
Vol 81 (02) ◽  
pp. 316-317 ◽  
Author(s):  
K. J. Clemetson ◽  
M.-C. Guillin ◽  
M.-C. Bouton ◽  
M. Jandrot-Perrus
Keyword(s):  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Glycoprotein Ib ◽  
Platelet Membrane Glycoprotein

Polymorphisms of Platelet Membrane Glycoprotein Ib Associated With Arterial Thrombotic Disease

Blood ◽  
1998 ◽  
Vol 92 (8) ◽  
pp. 2771-2776 ◽  
Author(s):  
Rocio Gonzalez-Conejero ◽  
Maria L. Lozano ◽  
Jose Rivera ◽  
Javier Corral ◽  
Juan A. Iniesta ◽  
...  
Keyword(s):  
Coronary Heart Disease ◽  
Heart Disease ◽  
Venous Thrombosis ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Glycoprotein Ib ◽  
Initial Development ◽  
Thrombotic Disease ◽  
Platelet Membrane Glycoprotein ◽  
Increased Risk

Abstract Platelet membrane glycoprotein Ib (GPIb) is a major receptor for von Willebrand factor and thrombin, which plays a key role in the initial development of thrombi. Two polymorphisms (HPA-2 and VNTR) that affect phenotype have been described in GPIb. The relevance of these polymorphisms to thrombotic disease was investigated by genotypic identification in three case-control studies: 104 case patients with acute cerebrovascular disease (CVD), 101 case patients with acute coronary heart disease (CHD), 95 patients with deep venous thrombosis (DVT), and one control age-, sex-, and race-matched for each case patient. Results show that the C/B genotype of the VNTR and the HPA-2b polymorphisms of GPIb are strongly associated with increased risk of coronary heart disease and cerebral vascular disease but not with deep vein thrombosis. These two polymorphisms of GPIb may represent newly identified risk factors for arterial thrombotic disease, but not for venous thrombosis. © 1998 by The American Society of Hematology.

scholarly journals Unravelling the mechanism and significance of thrombin binding to platelet glycoprotein Ib

2010 ◽  
Vol 104 (11) ◽  
pp. 894-902 ◽  
Author(s):  
Alessandro Zarpellon ◽  
James Roberts ◽  
Richard Mc Clintock ◽  
Hua Jing ◽  
G. Loredana Mendolicchio ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Vascular Injury ◽  
Platelet Membrane ◽  
Active Enzyme ◽  
Platelet Glycoprotein ◽  
Membrane Glycoprotein ◽  
Main Question ◽  
Glycoprotein Ib ◽  
Platelet Membrane Glycoprotein

SummaryThe main question concerning the mechanism of α-thrombin binding to platelet membrane glycoprotein (GP)Ib is whether it involves both thrombin exosite I and exosite II. The solution of two independent crystal structures suggests alternative explanations that may actually reflect different modes of binding with distinct pathophysiological significance. With respect to function, it is still unclear whether thrombin binding to GPIb promotes procoagulant and prothrombotic pathways of re-sponse to vascular injury or limits such responses by sequestering, at least temporarily, the active enzyme. We review here published information on these topics and touch upon ongoing studies aimed at finding definitive answers to outstanding questions relevant for a better understanding of thrombosis and haemostasis.

Absence of the 145,000 Molecular Weight, Soluble Platelet Membrane Glycoprotein - Lack of Platelet Agglutination

1979 ◽  
Vol 42 (05) ◽  
pp. 1626-1629 ◽  
Author(s):  
Nils Olav Solum ◽  
Inger Hagen ◽  
Miroslav Peterka ◽  
Torbjørn Gjemdal
Keyword(s):  
Molecular Weight ◽  
Factor Viii ◽  
Human Platelets ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Related Protein ◽  
Giant Platelets ◽  
Platelet Membrane Glycoprotein ◽  
Human Factor Viii ◽  
Bovine Factor

SummaryOne step in the function of platelets in hemostasis is their adhesion to subendothelial tissue. The human factor VIII related protein (von Willebrand factor) is considered to be involved in the adhesion phenomenon (Baumgartner et al. 1977). One manifestation of the protein-cell interaction can be observed as a platelet agglutination after addition to the human platelets of a combination of the human protein and the glycopeptide ristocetin, or after addition of the bovine protein alone. The bovine factor VIII related protein as such directly binds to the platelet membrane (Kirby and Sha May Tang 1977) and thus represents a simpler system than ristocetin plus the human cofactor which may have to interact with each other before excerting their effect on the platelet membrane. The present paper concerns the se.One of the characteristics of the agglutination of human platelets brought about by the bovine factor VIII related protein (as well as by ristocetin plus the human cofactor) is that it is independent of the energy metabolism and the internal organization of the platelet. One would therefore expect that modified platelets and platelet “ghosts” would agglutinate as long as certain structures on the outer cell surface are chemically and sterically intact. Because of the hydrophilic character of the carbohydrate side chains, the membrane glycoproteins are considered of special importance for cell contact phenomena. Thus it has already been known for some years that giant platelets of the Bernard-Soulier type which do not agglutinate with the bovine protein (Bithell et al. 1972), contain a reduced amount of sialic acid related to protein content and surface area (Grottum and Solum 1969), and show a reduced glycoprotein stain in the GP I region on SDS polyacrylamide gel electrophoresis (Nurden and Caen 1975).This paper presents five observations which support a working hypothesis stating that the presence on the platelet membrane of the 145,000 molecular weight, soluble platelet membrane glycoprotein called GPS or glycocalicin is a prerequisite to the agglutination of human platelets by bovine factor VIII related protein.

Thrombin Binding to Platelet Membrane Glycoprotein Ib

1992 ◽  
Vol 18 (02) ◽  
pp. 261-266 ◽  
Author(s):  
Martine Jandrot-Perrus ◽  
Marie-Geneviève Huisse ◽  
Catherine Ternisien ◽  
Annie Bezeaud ◽  
Marie-Claude Guillin
Keyword(s):  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Glycoprotein Ib ◽  
Platelet Membrane Glycoprotein
Sign in / Sign up

Export Citation Format

Share Document