Binding of Purified 14-3-3 ζ Signaling Protein to Discrete Amino Acid Sequences within the Cytoplasmic Domain of the Platelet Membrane Glycoprotein Ib-IX-V Complex†

Biochemistry ◽  
1998 ◽  
Vol 37 (2) ◽  
pp. 638-647 ◽  
Author(s):  
Robert K. Andrews ◽  
Simon J. Harris ◽  
Tracy McNally ◽  
Michael C. Berndt
Keyword(s):  
Amino Acid ◽  
Cytoplasmic Domain ◽  
Amino Acid Sequences ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Glycoprotein Ib ◽  
Signaling Protein ◽  
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.

Interaction of calmodulin with the cytoplasmic domain of the platelet membrane glycoprotein Ib-IX-V complex

Blood ◽  
2001 ◽  
Vol 98 (3) ◽  
pp. 681-687 ◽  
Author(s):  
Robert K. Andrews ◽  
Adam D. Munday ◽  
Christina A. Mitchell ◽  
Michael C. Berndt
Keyword(s):  
Synthetic Peptide ◽  
Leukocyte Adhesion ◽  
Thrombus Formation ◽  
Sodium Dodecyl ◽  
Cytoplasmic Domain ◽  
Platelet Membrane ◽  
Membrane Glycoprotein ◽  
Iq Motif ◽  
Calmodulin Binding ◽  
Platelet Membrane Glycoprotein

Abstract Engagement of platelet membrane glycoprotein (GP) Ib-IX-V by von Willebrand factor triggers Ca++-dependent activation of αIIbβ3, resulting in (patho)physiological thrombus formation. It is demonstrated here that the cytoplasmic domain of GPIb-IX-V associates with cytosolic calmodulin. First, an anti-GPIbα antibody coimmunoprecipitated GPIb-IX and calmodulin from platelet lysates. Following platelet stimulation, calmodulin dissociated from GPIb-IX and, like the GPIb-IX–associated proteins 14-3-3ζ and p85, redistributed to the activated cytoskeleton. Second, a synthetic peptide based on the cytoplasmic sequence of GPIbβ, R149–L167 (single-letter amino acid codes), affinity-isolated calmodulin from platelet cytosol in the presence of Ca++ as confirmed by comigration with bovine calmodulin on sodium dodecyl sulfate–polyacrylamide gels, by sequence analysis, and by immunoreactivity with the use of an anticalmodulin antibody. The membrane-proximal GPIbβ sequence was analogous to a previously reported calmodulin-binding sequence in the leukocyte adhesion receptor, L-selectin. In addition, the cytoplasmic sequence of GPV, K529–G544, was analogous to a calmodulin-binding IQ motif within the α1c subunit of L-type Ca++ channels. Calmodulin coimmunoprecipitated with GPV from resting platelet lysates, but was dissociated in stimulated platelets. A GPV-related synthetic peptide also bound calmodulin and induced a Ca++-dependent shift on nondenaturing gels. Together, these results suggest separate regions of GPIb-IX-V can directly bind calmodulin, and this novel interaction potentially regulates aspects of GPIb-IX-V–dependent platelet activation.

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
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