<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Hauschner, Hagit</style></author><author><style face="normal" font="default" size="100%">Mor-Cohen, Ronit</style></author><author><style face="normal" font="default" size="100%">Messineo, Stefania</style></author><author><style face="normal" font="default" size="100%">Mansour, Wissam</style></author><author><style face="normal" font="default" size="100%">Seligsohn, Uri</style></author><author><style face="normal" font="default" size="100%">Savoia, Anna</style></author><author><style face="normal" font="default" size="100%">Rosenberg, Nurit</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Abnormal cytoplasmic extensions associated with active αIIbβ3 are probably the cause for macrothrombocytopenia in Glanzmann thrombasthenia-like syndrome.</style></title><secondary-title><style face="normal" font="default" size="100%">Blood Coagul Fibrinolysis</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Blood Coagul. Fibrinolysis</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Cricetinae</style></keyword><keyword><style  face="normal" font="default" size="100%">Cytoskeleton</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Complementary</style></keyword><keyword><style  face="normal" font="default" size="100%">Fibrinogen</style></keyword><keyword><style  face="normal" font="default" size="100%">Genetic Vectors</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Integrin alpha2</style></keyword><keyword><style  face="normal" font="default" size="100%">Integrin beta3</style></keyword><keyword><style  face="normal" font="default" size="100%">Megakaryocytes</style></keyword><keyword><style  face="normal" font="default" size="100%">Mesocricetus</style></keyword><keyword><style  face="normal" font="default" size="100%">Microtubules</style></keyword><keyword><style  face="normal" font="default" size="100%">Mutation, Missense</style></keyword><keyword><style  face="normal" font="default" size="100%">Platelet Glycoprotein GPIIb-IIIa Complex</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Conformation</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Interaction Mapping</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Structure, Tertiary</style></keyword><keyword><style  face="normal" font="default" size="100%">Recombinant Fusion Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Deletion</style></keyword><keyword><style  face="normal" font="default" size="100%">Thrombasthenia</style></keyword><keyword><style  face="normal" font="default" size="100%">Tubulin</style></keyword><keyword><style  face="normal" font="default" size="100%">von Willebrand Factor</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2015</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2015 Apr</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">26</style></volume><pages><style face="normal" font="default" size="100%">302-8</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Mutations in the ITGA2B or ITGB3 genes that encode for the αIIbβ3 platelet integrin usually cause Glanzmann thrombasthenia, a severe autosomal recessive bleeding disorder characterized by absence of platelet aggregation, but normal platelet number and size. Several rare mutations cause a Glanzmann-like syndrome which manifests macrothrombocytopenia and usually displays autosomal dominant inheritance. The exact mechanism causing Glanzmann-like syndrome is unknown. One typical example of Glanzmann-like mutations causes deletion of 40 amino acids (p.647-686) in the β3 β-tail domain (βTD_del) that was found in the heterozygous state in Italian and Japanese families. A second example is a missense mutation, C560R, located in the epidermal growth factor-like domain, found in the homozygous state in a French patient. Both mutations cause constitutive activation of αIIbβ3, but differ in their surface expression. In the current study, we generated cultured cells expressing β3-βTD_del or β3-C560R mutations along with wild-type αIIb, and examined the cells' ability to create tubulin-dependent protrusions compared to cells expressing wild-type αIIbβ3. Unlike cells expressing wild-type αIIbβ3, cells harboring each of the mutations exhibited abnormal cytoplasmic extensions on immobilized fibrinogen or Von Willebrand factor, which resembled extensions formed in megakaryocyte leading to proplatelets. Moreover, we showed that formation of abnormal extensions occurred also in wild-type αIIbβ3 cells when activated by activating antibody. These results suggest that the active conformation of αIIbβ3 can induce cytoskeletal rearrangements that lead to impaired proplatelet formation.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/25806962?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Savoia, Anna</style></author><author><style face="normal" font="default" size="100%">Kunishima, Shinji</style></author><author><style face="normal" font="default" size="100%">De Rocco, Daniela</style></author><author><style face="normal" font="default" size="100%">Zieger, Barbara</style></author><author><style face="normal" font="default" size="100%">Rand, Margaret L</style></author><author><style face="normal" font="default" size="100%">Pujol-Moix, Núria</style></author><author><style face="normal" font="default" size="100%">Caliskan, Umran</style></author><author><style face="normal" font="default" size="100%">Tokgoz, Huseyin</style></author><author><style face="normal" font="default" size="100%">Pecci, Alessandro</style></author><author><style face="normal" font="default" size="100%">Noris, Patrizia</style></author><author><style face="normal" font="default" size="100%">Srivastava, Alok</style></author><author><style face="normal" font="default" size="100%">Ward, Christopher</style></author><author><style face="normal" font="default" size="100%">Morel-Kopp, Marie-Christine</style></author><author><style face="normal" font="default" size="100%">Alessi, Marie-Christine</style></author><author><style face="normal" font="default" size="100%">Bellucci, Sylvia</style></author><author><style face="normal" font="default" size="100%">Beurrier, Philippe</style></author><author><style face="normal" font="default" size="100%">de Maistre, Emmanuel</style></author><author><style face="normal" font="default" size="100%">Favier, Rémi</style></author><author><style face="normal" font="default" size="100%">Hézard, Nathalie</style></author><author><style face="normal" font="default" size="100%">Hurtaud-Roux, Marie-Françoise</style></author><author><style face="normal" font="default" size="100%">Latger-Cannard, Véronique</style></author><author><style face="normal" font="default" size="100%">Lavenu-Bombled, Cécile</style></author><author><style face="normal" font="default" size="100%">Proulle, Valérie</style></author><author><style face="normal" font="default" size="100%">Meunier, Sandrine</style></author><author><style face="normal" font="default" size="100%">Négrier, Claude</style></author><author><style face="normal" font="default" size="100%">Nurden, Alan</style></author><author><style face="normal" font="default" size="100%">Randrianaivo, Hanitra</style></author><author><style face="normal" font="default" size="100%">Fabris, Fabrizio</style></author><author><style face="normal" font="default" size="100%">Platokouki, Helen</style></author><author><style face="normal" font="default" size="100%">Rosenberg, Nurit</style></author><author><style face="normal" font="default" size="100%">HadjKacem, Basma</style></author><author><style face="normal" font="default" size="100%">Heller, Paula G</style></author><author><style face="normal" font="default" size="100%">Karimi, Mehran</style></author><author><style face="normal" font="default" size="100%">Balduini, Carlo L</style></author><author><style face="normal" font="default" size="100%">Pastore, Annalisa</style></author><author><style face="normal" font="default" size="100%">Lanza, Francois</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Spectrum of the mutations in Bernard-Soulier syndrome.</style></title><secondary-title><style face="normal" font="default" size="100%">Hum Mutat</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Hum. Mutat.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Alleles</style></keyword><keyword><style  face="normal" font="default" size="100%">Bernard-Soulier Syndrome</style></keyword><keyword><style  face="normal" font="default" size="100%">Databases, Nucleic Acid</style></keyword><keyword><style  face="normal" font="default" size="100%">Founder Effect</style></keyword><keyword><style  face="normal" font="default" size="100%">Genetic Variation</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Mutation</style></keyword><keyword><style  face="normal" font="default" size="100%">Platelet Glycoprotein GPIb-IX Complex</style></keyword><keyword><style  face="normal" font="default" size="100%">Polymorphism, Single Nucleotide</style></keyword><keyword><style  face="normal" font="default" size="100%">von Willebrand Diseases</style></keyword><keyword><style  face="normal" font="default" size="100%">Web Browser</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2014</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2014 Sep</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">35</style></volume><pages><style face="normal" font="default" size="100%">1033-45</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Bernard-Soulier syndrome (BSS) is a rare autosomal recessive bleeding disorder characterized by defects of the GPIb-IX-V complex, a platelet receptor for von Willebrand factor (VWF). Most of the mutations identified in the genes encoding for the GP1BA (GPIbα), GP1BB (GPIbβ), and GP9 (GPIX) subunits prevent expression of the complex at the platelet membrane or more rarely its interaction with VWF. As a consequence, platelets are unable to adhere to the vascular subendothelium and agglutinate in response to ristocetin. In order to collect information on BSS patients, we established an International Consortium for the study of BSS, allowing us to enrol and genotype 132 families (56 previously unreported). With 79 additional families for which molecular data were gleaned from the literature, the 211 families characterized so far have mutations in the GP1BA (28%), GP1BB (28%), or GP9 (44%) genes. There is a wide spectrum of mutations with 112 different variants, including 22 novel alterations. Consistent with the rarity of the disease, 85% of the probands carry homozygous mutations with evidence of founder effects in some geographical areas. This overview provides the first global picture of the molecular basis of BSS and will lead to improve patient diagnosis and management.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">9</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/24934643?dopt=Abstract</style></custom1></record></records></xml>