Genomes and Genes
Affiliation: Texas Medical Center
- C1qTNF-related protein-1 (CTRP-1): a vascular wall protein that inhibits collagen-induced platelet aggregation by blocking VWF binding to collagenGerald Lasser
ZymoGenetics, Cardiovascular Biology, Seattle, WA 98102, USA
Blood 107:423-30. 2006....
- The platelet glycoprotein Ib-von Willebrand factor interaction activates the collagen receptor alpha2beta1 to bind collagen: activation-dependent conformational change of the alpha2-I domainMiguel A Cruz
Thrombosis Research Section, Department of Medicine, Baylor College of Medicine, One Baylor Plaza, N1319, Houston, TX 77030, USA
Blood 105:1986-91. 2005..These results strongly suggest that the interaction of platelet GP Ib with VWF mediates the activation of alpha2beta1, increasing its affinity for collagen...
- Evaluation of ADAMTS-13 activity in plasma using recombinant von Willebrand Factor A2 domain polypeptide as substrateMiguel A Cruz
Thrombosis Research Section, Department of Medicine, Baylor College of Medicine, One Baylor Plaza, N1319, Houston, Texas 77030, USA
Thromb Haemost 90:1204-9. 2003..This novel recombinant VWF-A2 protein has potential utility as matrix for a rapid clinical measurement of plasma ADAMTS-13 activity...
- Ultralarge multimers of von Willebrand factor form spontaneous high-strength bonds with the platelet glycoprotein Ib-IX complex: studies using optical tweezersManeesh Arya
Department of Bioengineering, Rice University, Houston, TX, USA
Blood 99:3971-7. 2002..Therefore, we suggest that the conformational state of ULVWF multimers is more critical than their size for interaction with platelets...
- Dynamic force spectroscopy of glycoprotein Ib-IX and von Willebrand factorManeesh Arya
Department of Bioengineering, Rice University, Houston, TX 77251, USA
Biophys J 88:4391-401. 2005..Our data illustrate the importance of the bond kinetics associated with the VWF/GP Ib-IX interaction in hemostasis and also demonstrate the drastic changes in binding that can occur when only a single amino acid of GP Ibalpha is altered...
- Kinetics of GPIbalpha-vWF-A1 tether bond under flow: effect of GPIbalpha mutations on the association and dissociation ratesR Anand Kumar
Department of Bioengineering, Rice University, Houston, Texas, USA
Biophys J 85:4099-109. 2003..These findings are in contrast to the functionally similar selectin bonds where some of the mutations have been reported to affect only the dissociation rate...
- The mechanism of VWF-mediated platelet GPIbalpha bindingMatthew Auton
Cardiovascular Research, Baylor College of Medicine, Houston, Texas, USA
Biophys J 99:1192-201. 2010..Our analysis unites thermodynamics of protein unfolding and conformation-specific binding with the force dependence of biological catch bonds and it encompasses the effects of two subtypes of mutations that cause Von Willebrand Disease...
- Destabilization of the A1 domain in von Willebrand factor dissociates the A1A2A3 tri-domain and provokes spontaneous binding to glycoprotein Ibalpha and platelet activation under shear stressMatthew Auton
Section of Cardiovascular Research, Department of Medicine, Baylor College of Medicine, Houston, Texas 77030, USA
J Biol Chem 285:22831-9. 2010..Therefore, the termination of A domain association within VWF in solution results in binding to GPIba and platelet activation under high shear stress...
- Changes in thermodynamic stability of von Willebrand factor differentially affect the force-dependent binding to platelet GPIbalphaMatthew Auton
Department of Bioengineering, Rice University, Houston, Texas, USA
Biophys J 97:618-27. 2009....
- Magnesium maintains endothelial integrity, up-regulates proteolysis of ultra-large von Willebrand factor, and reduces platelet aggregation under flow conditionsJing Fei Dong
Section of Thrombosis Research, Department of Medicine, Baylor College of Medicine, Houston, Texas 77030, USA
Thromb Haemost 99:586-93. 2008..MgSO(4) is critical for maintaining endothelial integrity and regulates ULVWF proteolysis and aggregation under flow conditions. These results provide a new insight into additional mechanisms involved with magnesium therapy...
- ADAMTS-13 metalloprotease interacts with the endothelial cell-derived ultra-large von Willebrand factorJing Fei Dong
Thrombosis Research Section, Department of Medicine, Baylor College of Medicine, Houston, Texas 77030, USA
J Biol Chem 278:29633-9. 2003..Once released, these cleaved VWF fragments become inaccessible for the metalloprotease to prevent further cleavage...
- The alpha1 helix-beta13 strand spanning Leu214 to Val229 of platelet glycoprotein Ibalpha facilitates the interaction with von Willebrand factor: evidence from characterization of the epitope of monoclonal antibody AP1Yuandong Peng
Thrombosis Research Section, Baylor College of Medicine, BCM 286, N1319, 1 Baylor Plaza, Houston, TX 77030, USA
Blood 104:3971-8. 2004..This region thus appears to be more important for maintaining the regional conformation of GP Ibalpha, thereby facilitating the interaction with VWF...
- Haemoglobin blocks von Willebrand factor proteolysis by ADAMTS-13: a mechanism associated with sickle cell diseaseZhou Zhou
Thrombosis Research Section, Dept of Medicine, One Baylor Plaza, BCM286, N1319, Houston, Texas 77030, USA
Thromb Haemost 101:1070-7. 2009..Therefore, the Hb-VWF interaction may be considered as a therapeutic target for treating thrombotic and vaso-occlusive complications in patients with severe intravascular haemolysis such as those with SCD...
- Conformational stability and domain unfolding of the Von Willebrand factor A domainsMatthew Auton
Department of Bioengineering, Rice University, Houston, TX 77005, USA
J Mol Biol 366:986-1000. 2007..The low stability of the A2 domain is likely to be important in regulating the exposure of the A2 domain cleavage site in response to shear stress, ULVWF platelet adherence, and the attachment of ADAMTS-13 to ULVWF...
- The catalytic subunit of protein phosphatase 1 gamma regulates thrombin-induced murine platelet alpha(IIb)beta(3) functionFrancisca C Gushiken
Department of Medicine, Baylor College of Medicine, Houston, Texas, USA
PLoS ONE 4:e8304. 2009..Although the catalytic subunit of protein phosphatase 1 (PP1c) interacts with alpha(IIb)beta(3), the role of PP1c in platelet reactivity is unclear...
- Localization of the adhesion receptor glycoprotein Ib-IX-V complex to lipid rafts is required for platelet adhesion and activationCorie N Shrimpton
Thrombosis Research Section, Department of Medicine, Baylor College of Medicine, Houston, TX 77030, USA
J Exp Med 196:1057-66. 2002..Thus, localization of the GP Ib-IX-V complex within rafts is crucial for both platelet adhesion and postadhesion signaling...
- Platelet glycoprotein Ibalpha forms catch bonds with human WT vWF but not with type 2B von Willebrand disease vWFTadayuki Yago
Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, Oklahoma 73104, USA
J Clin Invest 118:3195-207. 2008..We conclude that in type 2B vWD, prolonged lifetimes of vWF bonds with GPIbalpha on circulating platelets may allow ADAMTS-13 to deplete large vWF multimers, causing bleeding...
- Platelet aggregation by membrane-expressed A1 domains of von Willebrand Factor is dependent on residues Asp 560 and Gly 561Jan Schulte Am Esch
Department of Hepatobiliary and Transplantation Surgery, University Hospital, University of Hamburg, Hamburg, Germany
Biochem Biophys Res Commun 302:873-7. 2003..The experimental system tested here provides a rapid and reproducible approach for the functional analysis of isolated A1-domain interactions with platelet-GPIb...
- Structural basis of von Willebrand factor activation by the snake toxin botrocetinKoichi Fukuda
The Burnham Institute, 10901 North Torrey Pines Road, La Jolla, California 92037, USA
Structure 10:943-50. 2002..Functional studies of platelet adhesion under flow further suggest that the activation mechanism is distinct from that of the gain-of-function mutation...